NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|88853059|ref|NP_001034678|]
View 

2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 isoform b [Homo sapiens]

Protein Classification

2-(3-amino-3-carboxypropyl)histidine synthase subunit 1/2( domain architecture ID 140194)

2-(3-amino-3-carboxypropyl)histidine synthase subunit 1/2 (Dph1/Dph2) is required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue

EC:  2.5.1.108
Gene Ontology:  GO:0017183|GO:0090560

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
diphth2_R super family cl19374
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, ...
 32-162 5.62e-41

diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (pfam04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM.


The actual alignment was detected with superfamily member TIGR00322:

Pssm-ID: 473165  Cd Length: 318  Bit Score: 143.11  E-value: 5.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853059    32 VYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEETTGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACL 111
Cdd:TIGR00322   2 NFEIDKTIEEIKKRGAKRVALQFPDGLLPDAVEVADILEKKPGAEVYILGDTTYGACCVDDVAAKHLGADLIIHYGHSCL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 88853059   112 SPPARPLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALG 162
Cdd:TIGR00322  82 SPITSRIPVLYVFVEIKIDVEHLVEALKENFPDKGKRIALVTTVQYAHALD 132
 
Name Accession Description Interval E-value
diphth2_R TIGR00322
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, ...
 32-162 5.62e-41

diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (pfam04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM.


Pssm-ID: 273013  Cd Length: 318  Bit Score: 143.11  E-value: 5.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853059    32 VYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEETTGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACL 111
Cdd:TIGR00322   2 NFEIDKTIEEIKKRGAKRVALQFPDGLLPDAVEVADILEKKPGAEVYILGDTTYGACCVDDVAAKHLGADLIIHYGHSCL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 88853059   112 SPPARPLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALG 162
Cdd:TIGR00322  82 SPITSRIPVLYVFVEIKIDVEHLVEALKENFPDKGKRIALVTTVQYAHALD 132
Diphthamide_syn pfam01866
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the ...
 54-153 7.11e-27

Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Swiss:Q16439 is a candidate tumour suppressor gene. DPH2 from yeast, which confers resistance to diphtheria toxin has been found to be involved in diphthamide synthesis. Diphtheria toxin inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide, a post-translationally modified histidine residue present in EF2. 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).


Pssm-ID: 460365  Cd Length: 302  Bit Score: 105.68  E-value: 7.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853059    54 FPDQLLGDAVAVAARLEETtGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACLSPPARpLPVAFVLRQRSVALEL 133
Cdd:pfam01866   1 FPEGLLPDAPEIADILEEF-GAEVIILGDTTYGACCVDEVAAEHLGADLLVHYGHSCLSPVDR-LPVLYVFVKIPIDVEH 78

                          90       100
                  ....*....|....*....|
gi 88853059   134 CVKAFEAQNPDPKaPVVLLS 153
Cdd:pfam01866  79 LVETLKKNFPDGK-KIALVT 97
 
Name Accession Description Interval E-value
diphth2_R TIGR00322
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, ...
 32-162 5.62e-41

diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (pfam04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM.


Pssm-ID: 273013  Cd Length: 318  Bit Score: 143.11  E-value: 5.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853059    32 VYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEETTGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACL 111
Cdd:TIGR00322   2 NFEIDKTIEEIKKRGAKRVALQFPDGLLPDAVEVADILEKKPGAEVYILGDTTYGACCVDDVAAKHLGADLIIHYGHSCL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 88853059   112 SPPARPLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALG 162
Cdd:TIGR00322  82 SPITSRIPVLYVFVEIKIDVEHLVEALKENFPDKGKRIALVTTVQYAHALD 132
DPH2 TIGR00272
diphthamide biosynthesis protein 2; This protein has been shown in Saccharomyces cerevisiae to ...
 25-163 1.48e-27

diphthamide biosynthesis protein 2; This protein has been shown in Saccharomyces cerevisiae to be one of several required for the modification of a particular histidine residue of translation elongation factor 2 to diphthamide. This modified site can then become the target for ADP-ribosylation by diphtheria toxin. [Protein fate, Protein modification and repair]


Pssm-ID: 272990  Cd Length: 496  Bit Score: 110.41  E-value: 1.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853059    25 PLPDLDGVYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEET---TGSKMFILGDTAYGSCCVDVLGAEQAGAQ 101
Cdd:TIGR00272  29 LEQDISAYYEIEPTVGYIKQGNEYQVALQFPDDLLKDSSKVVRLLQSKfphGKIKFWVLADTAYSSCCVDEVAAEHVHAE 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88853059   102 ALIHFGPACLSPPARpLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALGS 163
Cdd:TIGR00272 109 AVVHFGDACLSAIQN-LPVVYVFGTPPIDLALVVENFQRAFPDLSSKICLMADAPFSKHQSQ 169
Diphthamide_syn pfam01866
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the ...
 54-153 7.11e-27

Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Swiss:Q16439 is a candidate tumour suppressor gene. DPH2 from yeast, which confers resistance to diphtheria toxin has been found to be involved in diphthamide synthesis. Diphtheria toxin inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide, a post-translationally modified histidine residue present in EF2. 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).


Pssm-ID: 460365  Cd Length: 302  Bit Score: 105.68  E-value: 7.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88853059    54 FPDQLLGDAVAVAARLEETtGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACLSPPARpLPVAFVLRQRSVALEL 133
Cdd:pfam01866   1 FPEGLLPDAPEIADILEEF-GAEVIILGDTTYGACCVDEVAAEHLGADLLVHYGHSCLSPVDR-LPVLYVFVKIPIDVEH 78

                          90       100
                  ....*....|....*....|
gi 88853059   134 CVKAFEAQNPDPKaPVVLLS 153
Cdd:pfam01866  79 LVETLKKNFPDGK-KIALVT 97
 
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