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Conserved domains on  [gi|18087809|ref|NP_542381|]
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diphthine--ammonia ligase isoform 1 [Homo sapiens]

Protein Classification

adenine nucleotide alpha hydrolase( domain architecture ID 10113407)

adenine nucleotide alpha hydrolase similar to Saccharomyces cerevisiae diphthine--ammonia ligase Dph6 which is an amidase that catalyzes the conversion of diphthine to diphthamide using ammonium and ATP

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 ...
2-219 2.34e-115

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: 329.63  E-value: 2.34e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809   2 RVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDT 81
Cdd:cd01994   1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809  82 RQVYTKCEGDEVEDLYELLKLVKEKEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAM 161
Cdd:cd01994  74 ELGYEGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEAR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18087809 162 IIKVAALGLDPdKHLGKTLDQMEP-YLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKI 219
Cdd:cd01994 154 IVKVAAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKRI 211
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
2-219 2.34e-115

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: 329.63  E-value: 2.34e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809   2 RVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDT 81
Cdd:cd01994   1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809  82 RQVYTKCEGDEVEDLYELLKLVKEKEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAM 161
Cdd:cd01994  74 ELGYEGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEAR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18087809 162 IIKVAALGLDPdKHLGKTLDQMEP-YLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKI 219
Cdd:cd01994 154 IVKVAAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKRI 211
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
1-225 7.58e-68

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: 209.64  E-value: 7.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809     1 MRVAALISGGKDSCYNMMQCiAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTirgrsld 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHA-LKEHEVISLVNIMP-ENE------ESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809    81 trqvYTKCEGDEVEDLYELLKLVKekeeVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQA 160
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLD----VEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEA 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18087809   161 MIIKVAALGLDpDKHLGKTLD-QMEPYLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSE 225
Cdd:TIGR00290 138 RIIAVAAEGLD-ESWLGRRIDrKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIFKKRLEVKEIE 202
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
3-237 7.42e-65

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 201.50  E-value: 7.42e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809   3 VAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYrrtirgrsldtr 82
Cdd:COG2102   1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809  83 QVYTKCEGD-EVEDLYELLKLVKEkEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAM 161
Cdd:COG2102  62 EIELSGSNEeYEEELEEALKELKA-EGIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAI 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18087809 162 IIKVAALGLDPDkHLGKTLDqmEPYLIELsKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSEVVIHSADAFAPV 237
Cdd:COG2102 141 IVCVDAEGLDES-WLGRELD--EELLEEL-PAYGVDPCGEGGEFHTFVLDGPLFKKPIEIEEGEIVWRGGFGFLDI 212
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
1-225 4.33e-46

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: 153.80  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809     1 MRVAALISGGKDSCYNMMQcIAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRsld 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYR-ALKEMEVDSLVCVMS-ENK------ESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809    81 trqvytkcEGDEVEDLYELLKLVkekeEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQA 160
Cdd:pfam01902  70 --------EEKEVEDLKGILHRL----DVEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEA 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18087809   161 MIIKVAALGLDPDkHLGKTLD-QMEPYLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSE 225
Cdd:pfam01902 138 YVVAVKAEGLDES-WLGRRIDrKFIDELKKLNEKYGIHPAGEGGEFETLVLDGPIFKKRLEVKELE 202
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
2-219 2.34e-115

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: 329.63  E-value: 2.34e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809   2 RVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDT 81
Cdd:cd01994   1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-------DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809  82 RQVYTKCEGDEVEDLYELLKLVKEKEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAM 161
Cdd:cd01994  74 ELGYEGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEAR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18087809 162 IIKVAALGLDPdKHLGKTLDQMEP-YLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKI 219
Cdd:cd01994 154 IVKVAAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKRI 211
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
1-225 7.58e-68

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: 209.64  E-value: 7.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809     1 MRVAALISGGKDSCYNMMQCiAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTirgrsld 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHA-LKEHEVISLVNIMP-ENE------ESYMFHGVNAHLTDLQAESIGIPLIKLY------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809    81 trqvYTKCEGDEVEDLYELLKLVKekeeVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQA 160
Cdd:TIGR00290  66 ----TEGTEEDEVEELKGILHTLD----VEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEA 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18087809   161 MIIKVAALGLDpDKHLGKTLD-QMEPYLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSE 225
Cdd:TIGR00290 138 RIIAVAAEGLD-ESWLGRRIDrKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIFKKRLEVKEIE 202
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
4-229 3.52e-66

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: 205.19  E-value: 3.52e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809     4 AALISGGKDSCYNMMQCIAAGHQIVALANLRPaenqvgsDELDSYMYQTVGHHAIDLYAEAMALPLYrrtirgrsldtrQ 83
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVP-------ENEDSYMFHTPNIELTRLQAEALGIPLV------------E 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809    84 VYTKCEGD-EVEDLYELLKLVKEkEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAMI 162
Cdd:TIGR03679  62 IETSGEKEkEVEDLKGALKELKE-EGVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFII 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809   163 IKVAALGLDpDKHLGKTLDqmEPY---LIELSKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSEVVIH 229
Cdd:TIGR03679 141 VSVSAYGLD-ESWLGREID--EKYieeLKALNKRYGINPAGEGGEYETLVLDAPLFKRRIEIVEYEKKWS 207
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
3-237 7.42e-65

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 201.50  E-value: 7.42e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809   3 VAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENqvgsdelDSYMYQTVGHHAIDLYAEAMALPLYrrtirgrsldtr 82
Cdd:COG2102   1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-------DRVMFHGPNLELLEAQAEALGIPLI------------ 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809  83 QVYTKCEGD-EVEDLYELLKLVKEkEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAM 161
Cdd:COG2102  62 EIELSGSNEeYEEELEEALKELKA-EGIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAI 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18087809 162 IIKVAALGLDPDkHLGKTLDqmEPYLIELsKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSEVVIHSADAFAPV 237
Cdd:COG2102 141 IVCVDAEGLDES-WLGRELD--EELLEEL-PAYGVDPCGEGGEFHTFVLDGPLFKKPIEIEEGEIVWRGGFGFLDI 212
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
1-225 4.33e-46

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: 153.80  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809     1 MRVAALISGGKDSCYNMMQcIAAGHQIVALANLRPaENQvgsdelDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRsld 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYR-ALKEMEVDSLVCVMS-ENK------ESYMFHGPNAHLTKLQAESVGIPLIKLYTTGE--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18087809    81 trqvytkcEGDEVEDLYELLKLVkekeEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQA 160
Cdd:pfam01902  70 --------EEKEVEDLKGILHRL----DVEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEA 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18087809   161 MIIKVAALGLDPDkHLGKTLD-QMEPYLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSE 225
Cdd:pfam01902 138 YVVAVKAEGLDES-WLGRRIDrKFIDELKKLNEKYGIHPAGEGGEFETLVLDGPIFKKRLEVKELE 202
 
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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