NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958646971|ref|XP_038937016|]
View 

tRNA-specific adenosine deaminase 2 isoform X4 [Rattus norvegicus]

Protein Classification

nucleoside deaminase( domain architecture ID 10001752)

nucleoside deaminase such as adenosine, guanine, or cytosine deaminase is a Zn-dependent enzyme which catalyzes the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer

EC:  3.5.4.-
Gene Ontology:  GO:0008270|GO:0019239|GO:0009116
PubMed:  38524700
SCOP:  3001838

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-114 6.01e-25

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


:

Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 92.49  E-value: 6.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   2 VYNNEVVGKGRNEVNQTKNVLdwchRHG----------QSPSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNER 71
Cdd:COG0590    31 VKDGEIIARGHNRVETLNDPT----AHAeilairaaarKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958646971  72 FGGCGSVLNIASADLPNtgRPFQCIPGYRAEEAVELLKTFYKQ 114
Cdd:COG0590   107 AGAAGSIYDLLADPRLN--HRVEVVGGVLAEECAALLRDFFAA 147
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-114 6.01e-25

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 92.49  E-value: 6.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   2 VYNNEVVGKGRNEVNQTKNVLdwchRHG----------QSPSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNER 71
Cdd:COG0590    31 VKDGEIIARGHNRVETLNDPT----AHAeilairaaarKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958646971  72 FGGCGSVLNIASADLPNtgRPFQCIPGYRAEEAVELLKTFYKQ 114
Cdd:COG0590   107 AGAAGSIYDLLADPRLN--HRVEVVGGVLAEECAALLRDFFAA 147
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 4-80 5.01e-22

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 83.82  E-value: 5.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   4 NNEVVGKGRNEVNQTKNVLdwchRHG----------QSPSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFG 73
Cdd:cd01285    27 DGKVIARGHNRVEQDGDPT----AHAeivairnaarRLGSYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPKLG 102


                  ....*..
gi 1958646971  74 GCGSVLN 80
Cdd:cd01285   103 GIGFLIE 109
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-114 2.10e-12

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 60.59  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   1 MVYNNEVVGKGRN---------------------EVNQTKNVLDwchrhgqspsavfehTVLYVTVEPCIMCAAALRLMK 59
Cdd:PRK10860   39 LVHNNRVIGEGWNrpigrhdptahaeimalrqggLVLQNYRLLD---------------ATLYVTLEPCVMCAGAMVHSR 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958646971  60 IPLVVYGCQNERFGGCGSVLNIASAdlPNTGRPFQCIPGYRAEEAVELLKTFYKQ 114
Cdd:PRK10860  104 IGRLVFGARDAKTGAAGSLMDVLHH--PGMNHRVEITEGVLADECAALLSDFFRM 156
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 2-88 1.79e-10

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 54.84  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   2 VYNNEVVGKGRNEVNQTKNVLDwcHRHGQS--------PSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFG 73
Cdd:pfam14437  30 VKDGKVIARGYNRKELNADTTA--HAEILAiqqaakklGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGNPKGG 107

                          90
                  ....*....|....*
gi 1958646971  74 GCGSVLNIASADLPN 88
Cdd:pfam14437 108 AVGSVLNKLVIVLWN 122
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-114 6.01e-25

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 92.49  E-value: 6.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   2 VYNNEVVGKGRNEVNQTKNVLdwchRHG----------QSPSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNER 71
Cdd:COG0590    31 VKDGEIIARGHNRVETLNDPT----AHAeilairaaarKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958646971  72 FGGCGSVLNIASADLPNtgRPFQCIPGYRAEEAVELLKTFYKQ 114
Cdd:COG0590   107 AGAAGSIYDLLADPRLN--HRVEVVGGVLAEECAALLRDFFAA 147
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 4-80 5.01e-22

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 83.82  E-value: 5.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   4 NNEVVGKGRNEVNQTKNVLdwchRHG----------QSPSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFG 73
Cdd:cd01285    27 DGKVIARGHNRVEQDGDPT----AHAeivairnaarRLGSYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPKLG 102


                  ....*..
gi 1958646971  74 GCGSVLN 80
Cdd:cd01285   103 GIGFLIE 109
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-114 2.10e-12

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 60.59  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   1 MVYNNEVVGKGRN---------------------EVNQTKNVLDwchrhgqspsavfehTVLYVTVEPCIMCAAALRLMK 59
Cdd:PRK10860   39 LVHNNRVIGEGWNrpigrhdptahaeimalrqggLVLQNYRLLD---------------ATLYVTLEPCVMCAGAMVHSR 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958646971  60 IPLVVYGCQNERFGGCGSVLNIASAdlPNTGRPFQCIPGYRAEEAVELLKTFYKQ 114
Cdd:PRK10860  104 IGRLVFGARDAKTGAAGSLMDVLHH--PGMNHRVEITEGVLADECAALLSDFFRM 156
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 2-88 1.79e-10

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 54.84  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646971   2 VYNNEVVGKGRNEVNQTKNVLDwcHRHGQS--------PSAVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFG 73
Cdd:pfam14437  30 VKDGKVIARGYNRKELNADTTA--HAEILAiqqaakklGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGNPKGG 107

                          90
                  ....*....|....*
gi 1958646971  74 GCGSVLNIASADLPN 88
Cdd:pfam14437 108 AVGSVLNKLVIVLWN 122
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
4-66 1.97e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 45.76  E-value: 1.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958646971   4 NNEVVGKGRNEVNQTK--------NVLDWCHRHGQSPSavFEHTVLYVTVEPCIMCAAALRLMKIPLVVYG 66
Cdd:pfam00383  32 DGEIIATGYNGENAGYdptihaerNAIRQAGKRGEGVR--LEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 12-66 1.01e-03

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 37.04  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958646971  12 RNEVNQTKNVLDWCHRHGQSpsavFEHTVLYVTVEPCIMCAAALRLMKIPLVVYG 66
Cdd:PHA02588   79 KNEIHAELNAILFAARNGIS----IEGATMYVTASPCPDCAKAIAQSGIKKLVYC 129
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 41-76 1.43e-03

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 36.96  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958646971  41 LYVTVEPCIM------CAAALRLMKIPLVVYGCQ--NERFGGCG 76
Cdd:COG0117    65 LYVTLEPCSHhgrtppCADALIEAGIKRVVIAMLdpNPLVAGKG 108
 
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