NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907142771|ref|XP_036018356|]
View 

diphthine--ammonia ligase isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 46-149 1.69e-42

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: 140.11  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  46 RVAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRSLET 125
Cdd:cd01994     1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                          90       100
                  ....*....|....*....|....
gi 1907142771 126 GRVYTQCEGDEVEDLYELLKLVKA 149
Cdd:cd01994    74 ELGYEGEEEDEVEDLYELLKKVKE 97
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 46-149 1.69e-42

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: 140.11  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  46 RVAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRSLET 125
Cdd:cd01994     1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                          90       100
                  ....*....|....*....|....
gi 1907142771 126 GRVYTQCEGDEVEDLYELLKLVKA 149
Cdd:cd01994    74 ELGYEGEEEDEVEDLYELLKKVKE 97
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 45-149 2.91e-20

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: 83.29  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAirgrsle 124
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVN-------IMPENEESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65

                          90       100
                  ....*....|....*....|....*
gi 1907142771 125 tgrvYTQCEGDEVEDLYELLKLVKA 149
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLDV 86
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 47-149 8.30e-13

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 63.22  E-value: 8.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  47 VAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYrrairgrsletg 126
Cdd:COG2102     1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61

                          90       100
                  ....*....|....*....|....
gi 1907142771 127 RVYTQCEGD-EVEDLYELLKLVKA 149
Cdd:COG2102    62 EIELSGSNEeYEEELEEALKELKA 85
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 45-149 2.16e-10

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: 56.73  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRsle 124
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALKE-MEVDSLVC-------VMSENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69

                          90       100
                  ....*....|....*....|....*
gi 1907142771 125 tgrvytqcEGDEVEDLYELLKLVKA 149
Cdd:pfam01902  70 --------EEKEVEDLKGILHRLDV 86
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 46-149 1.69e-42

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: 140.11  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  46 RVAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRSLET 125
Cdd:cd01994     1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                          90       100
                  ....*....|....*....|....
gi 1907142771 126 GRVYTQCEGDEVEDLYELLKLVKA 149
Cdd:cd01994    74 ELGYEGEEEDEVEDLYELLKKVKE 97
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 45-149 2.91e-20

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: 83.29  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAirgrsle 124
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVN-------IMPENEESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65

                          90       100
                  ....*....|....*....|....*
gi 1907142771 125 tgrvYTQCEGDEVEDLYELLKLVKA 149
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLDV 86
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
 48-149 7.03e-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: 71.52  E-value: 7.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  48 AALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYRrairgrsLETGR 127
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVPENE-------DSYMFHTPNIELTRLQAEALGIPLVE-------IETSG 66

                          90       100
                  ....*....|....*....|..
gi 1907142771 128 VytqcEGDEVEDLYELLKLVKA 149
Cdd:TIGR03679  67 E----KEKEVEDLKGALKELKE 84
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 47-149 8.30e-13

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 63.22  E-value: 8.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  47 VAALISGGKDSCYNMMQCIAEGHQIVALANLRPDENqvesdelDSYMYQTVGHHAIDLYAEAMALPLYrrairgrsletg 126
Cdd:COG2102     1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61

                          90       100
                  ....*....|....*....|....
gi 1907142771 127 RVYTQCEGD-EVEDLYELLKLVKA 149
Cdd:COG2102    62 EIELSGSNEeYEEELEEALKELKA 85
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 45-149 2.16e-10

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: 56.73  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142771  45 MRVAALISGGKDSCYNMMQCIAEgHQIVALANlrpdenqVESDELDSYMYQTVGHHAIDLYAEAMALPLYRRAIRGRsle 124
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALKE-MEVDSLVC-------VMSENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69

                          90       100
                  ....*....|....*....|....*
gi 1907142771 125 tgrvytqcEGDEVEDLYELLKLVKA 149
Cdd:pfam01902  70 --------EEKEVEDLKGILHRLDV 86
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH