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Conserved domains on  [gi|213972615|ref|NP_001135444|]
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diphthine--ammonia ligase isoform 2 [Homo sapiens]

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 ...
 2-105 3.49e-44

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: 144.73  E-value: 3.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615   2 RVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDT 81
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                         90       100
                 ....*....|....*....|....
gi 213972615  82 RQVYTKCEGDEVEDLYELLKLVKG 105
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 ...
 2-105 3.49e-44

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: 144.73  E-value: 3.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615   2 RVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDT 81
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                         90       100
                 ....*....|....*....|....
gi 213972615  82 RQVYTKCEGDEVEDLYELLKLVKG 105
Cdd:cd01994   74 ELGYEGEEEDEVEDLYELLKKVKE 97
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 1-104 6.89e-19

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: 79.83  E-value: 6.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615    1 MRVAALISGGKDSCYNMMQCiAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTirgrsld 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHA-LKEHEVISLVNIMP-ENE------ESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65

                          90       100
                  ....*....|....*....|....
gi 213972615   81 trqvYTKCEGDEVEDLYELLKLVK 104
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLD 85
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 3-107 7.57e-13

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 63.60  E-value: 7.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615   3 VAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYrrtirgrsldtr 82
Cdd:COG2102    1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61

                         90       100
                 ....*....|....*....|....*...
gi 213972615  83 QVYTKCEGD-EVEDLYELLKLVK--GIT 107
Cdd:COG2102   62 EIELSGSNEeYEEELEEALKELKaeGIE 89
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 1-101 5.62e-09

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: 52.88  E-value: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615    1 MRVAALISGGKDSCYNMMQcIAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRsld 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYR-ALKEMEVDSLVCVMS-ENK------ESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69

                          90       100
                  ....*....|....*....|.
gi 213972615   81 trqvytkcEGDEVEDLYELLK 101
Cdd:pfam01902  70 --------EEKEVEDLKGILH 82
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 2-105 3.49e-44

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: 144.73  E-value: 3.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615   2 RVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDT 81
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73

                         90       100
                 ....*....|....*....|....
gi 213972615  82 RQVYTKCEGDEVEDLYELLKLVKG 105
Cdd:cd01994   74 ELGYEGEEEDEVEDLYELLKKVKE 97
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 1-104 6.89e-19

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: 79.83  E-value: 6.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615    1 MRVAALISGGKDSCYNMMQCiAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTirgrsld 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHA-LKEHEVISLVNIMP-ENE------ESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65

                          90       100
                  ....*....|....*....|....
gi 213972615   81 trqvYTKCEGDEVEDLYELLKLVK 104
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLD 85
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
 4-121 1.88e-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: 73.06  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615    4 AALISGGKDSCYNMMQCIAAGHQIVALANLRPaenqvgsDELDSYMYQTVGHHAIDLYAEAMALPLYrrtirgrsldtrQ 83
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVP-------ENEDSYMFHTPNIELTRLQAEALGIPLV------------E 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 213972615   84 VYTKCEGD-EVEDLYELLK-----LVKGITRMTLLAEYDALNLQ 121
Cdd:TIGR03679  62 IETSGEKEkEVEDLKGALKelkeeGVEGIVTGAIASEYQKSRIE 105
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 3-107 7.57e-13

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 63.60  E-value: 7.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615   3 VAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYrrtirgrsldtr 82
Cdd:COG2102    1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61

                         90       100
                 ....*....|....*....|....*...
gi 213972615  83 QVYTKCEGD-EVEDLYELLKLVK--GIT 107
Cdd:COG2102   62 EIELSGSNEeYEEELEEALKELKaeGIE 89
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 1-101 5.62e-09

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: 52.88  E-value: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972615    1 MRVAALISGGKDSCYNMMQcIAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRsld 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYR-ALKEMEVDSLVCVMS-ENK------ESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69

                          90       100
                  ....*....|....*....|.
gi 213972615   81 trqvytkcEGDEVEDLYELLK 101
Cdd:pfam01902  70 --------EEKEVEDLKGILH 82
 
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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