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Conserved domains on  [gi|568918067|ref|XP_006500082|]
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diphthine--ammonia ligase isoform X1 [Mus musculus]

Protein Classification

diphthine--ammonia ligase family protein( domain architecture ID 10113407)

diphthine--ammonia ligase family protein belonging to the adenine nucleotide alpha hydrolase (AANH) superfamily, similar to diphthine--ammonia ligase, an amidase that catalyzes the conversion of diphthine to diphthamide using ammonium and ATP

CATH:  3.40.50.620
EC:  6.3.1.14
Gene Ontology:  GO:0005524|GO:0017178|GO:0017183
PubMed:  12012333
SCOP:  3001593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 46-148 2.47e-43

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


:

Pssm-ID: 467498  Cd Length: 211  Bit Score: 143.58  E-value: 2.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067  46 RVAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRSLET 125
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                         90       100
                 ....*....|....*....|...
gi 568918067 126 GRVYTQCEGDEVEDLYELLKLVK 148
Cdd:cd01994   74 ELGYEGEEEDEVEDLYELLKKVK 96
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 46-148 2.47e-43

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 143.58  E-value: 2.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067  46 RVAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRSLET 125
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                         90       100
                 ....*....|....*....|...
gi 568918067 126 GRVYTQCEGDEVEDLYELLKLVK 148
Cdd:cd01994   74 ELGYEGEEEDEVEDLYELLKKVK 96
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 45-151 1.37e-21

MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.


Pssm-ID: 273000  Cd Length: 223  Bit Score: 87.91  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067   45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAirgrsle 124
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVN-------IMPENEESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65

                          90       100
                  ....*....|....*....|....*..
gi 568918067  125 tgrvYTQCEGDEVEDLYELLKLVKVQA 151
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLDVEA 88
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 47-148 8.18e-13

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 63.99  E-value: 8.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067  47 VAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYrrairgrsletg 126
Cdd:COG2102    1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61

                         90       100
                 ....*....|....*....|...
gi 568918067 127 RVYTQCEGD-EVEDLYELLKLVK 148
Cdd:COG2102   62 EIELSGSNEeYEEELEEALKELK 84
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 45-151 1.69e-11

Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.


Pssm-ID: 280139  Cd Length: 219  Bit Score: 60.59  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067   45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRsle 124
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALKE-MEVDSLVC-------VMSENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69

                          90       100
                  ....*....|....*....|....*..
gi 568918067  125 tgrvytqcEGDEVEDLYELLKLVKVQA 151
Cdd:pfam01902  70 --------EEKEVEDLKGILHRLDVEA 88
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 46-148 2.47e-43

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 143.58  E-value: 2.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067  46 RVAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRSLET 125
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                         90       100
                 ....*....|....*....|...
gi 568918067 126 GRVYTQCEGDEVEDLYELLKLVK 148
Cdd:cd01994   74 ELGYEGEEEDEVEDLYELLKKVK 96
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 45-151 1.37e-21

MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.


Pssm-ID: 273000  Cd Length: 223  Bit Score: 87.91  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067   45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAirgrsle 124
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVN-------IMPENEESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65

                          90       100
                  ....*....|....*....|....*..
gi 568918067  125 tgrvYTQCEGDEVEDLYELLKLVKVQA 151
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLDVEA 88
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
 48-153 2.91e-16

arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; This protein consists of an N-terminal possible metal-binding domain (pfam04068) followed by a 4Fe-4S cluster binding domain (pfam00037) followed by a C-terminal ABC transporter, ATP-binding domain (pfam00005). This combination of N-terminal domains is observed in the RNase L inhibitor, RLI. This model has the same scope as an archaeal COG (arCOG00187) and is found in all completely sequenced archaea and does not recognize any known non-archaeal genes.


Pssm-ID: 188368  Cd Length: 218  Bit Score: 73.45  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067   48 AALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRrairgrsLETGR 127
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVPENE-------DSYMFHTPNIELTRLQAEALGIPLVE-------IETSG 66

                          90       100
                  ....*....|....*....|....*.
gi 568918067  128 VytqcEGDEVEDLYELLKlvKVQARG 153
Cdd:TIGR03679  67 E----KEKEVEDLKGALK--ELKEEG 86
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 47-148 8.18e-13

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 63.99  E-value: 8.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067  47 VAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYrrairgrsletg 126
Cdd:COG2102    1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61

                         90       100
                 ....*....|....*....|...
gi 568918067 127 RVYTQCEGD-EVEDLYELLKLVK 148
Cdd:COG2102   62 EIELSGSNEeYEEELEEALKELK 84
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 45-151 1.69e-11

Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.


Pssm-ID: 280139  Cd Length: 219  Bit Score: 60.59  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918067   45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRsle 124
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALKE-MEVDSLVC-------VMSENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69

                          90       100
                  ....*....|....*....|....*..
gi 568918067  125 tgrvytqcEGDEVEDLYELLKLVKVQA 151
Cdd:pfam01902  70 --------EEKEVEDLKGILHRLDVEA 88
 
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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