NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|555943775|ref|NP_001273188|]
View 

tRNA-specific adenosine deaminase 2 isoform b [Homo sapiens]

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 ...
 2-126 1.06e-34

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: 117.53  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   2 VYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCRQSGkspSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQN 81
Cdd:COG0590   31 VKDGEIIARGHNRVETLNDPTAHAEILAIRAA---ARKLG---NWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASD 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 555943775  82 ERFGGCGSVLNIASADLPNtgRPFQCIPGYRAEEAVEMLKTFYKQ 126
Cdd:COG0590  105 PKAGAAGSIYDLLADPRLN--HRVEVVGGVLAEECAALLRDFFAA 147
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-126 1.06e-34

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: 117.53  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   2 VYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCRQSGkspSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQN 81
Cdd:COG0590   31 VKDGEIIARGHNRVETLNDPTAHAEILAIRAA---ARKLG---NWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASD 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 555943775  82 ERFGGCGSVLNIASADLPNtgRPFQCIPGYRAEEAVEMLKTFYKQ 126
Cdd:COG0590  105 PKAGAAGSIYDLLADPRLN--HRVEVVGGVLAEECAALLRDFFAA 147
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 4-92 1.80e-31

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: 108.47  E-value: 1.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   4 NNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCRQSGkspSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNER 83
Cdd:cd01285   27 DGKVIARGHNRVEQDGDPTAHAEIVAIRNA---ARRLG---SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPK 100


                 ....*....
gi 555943775  84 FGGCGSVLN 92
Cdd:cd01285  101 LGGIGFLIE 109
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-126 6.27e-18

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 75.61  E-value: 6.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   1 MVYNNEVVGKGRNEVNQTKNATRHAEMVAIdqvldwcRQSGkspsEVFEH-----TVLYVTVEPCIMCAAALRLMKIPLV 75
Cdd:PRK10860  39 LVHNNRVIGEGWNRPIGRHDPTAHAEIMAL-------RQGG----LVLQNyrlldATLYVTLEPCVMCAGAMVHSRIGRL 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 555943775  76 VYGCQNERFGGCGSVLNIASAdlPNTGRPFQCIPGYRAEEAVEMLKTFYKQ 126
Cdd:PRK10860 108 VFGARDAKTGAAGSLMDVLHH--PGMNHRVEITEGVLADECAALLSDFFRM 156
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 2-100 2.29e-15

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: 67.93  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775    2 VYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwcrqSGKSPSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQN 81
Cdd:pfam14437  30 VKDGKVIARGYNRKELNADTTAHAEILAIQQA------AKKLGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGN 103

                          90
                  ....*....|....*....
gi 555943775   82 ERFGGCGSVLNIASADLPN 100
Cdd:pfam14437 104 PKGGAVGSVLNKLVIVLWN 122
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-126 1.06e-34

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: 117.53  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   2 VYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCRQSGkspSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQN 81
Cdd:COG0590   31 VKDGEIIARGHNRVETLNDPTAHAEILAIRAA---ARKLG---NWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASD 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 555943775  82 ERFGGCGSVLNIASADLPNtgRPFQCIPGYRAEEAVEMLKTFYKQ 126
Cdd:COG0590  105 PKAGAAGSIYDLLADPRLN--HRVEVVGGVLAEECAALLRDFFAA 147
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 4-92 1.80e-31

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: 108.47  E-value: 1.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   4 NNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCRQSGkspSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNER 83
Cdd:cd01285   27 DGKVIARGHNRVEQDGDPTAHAEIVAIRNA---ARRLG---SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPK 100


                 ....*....
gi 555943775  84 FGGCGSVLN 92
Cdd:cd01285  101 LGGIGFLIE 109
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-126 6.27e-18

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 75.61  E-value: 6.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   1 MVYNNEVVGKGRNEVNQTKNATRHAEMVAIdqvldwcRQSGkspsEVFEH-----TVLYVTVEPCIMCAAALRLMKIPLV 75
Cdd:PRK10860  39 LVHNNRVIGEGWNRPIGRHDPTAHAEIMAL-------RQGG----LVLQNyrlldATLYVTLEPCVMCAGAMVHSRIGRL 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 555943775  76 VYGCQNERFGGCGSVLNIASAdlPNTGRPFQCIPGYRAEEAVEMLKTFYKQ 126
Cdd:PRK10860 108 VFGARDAKTGAAGSLMDVLHH--PGMNHRVEITEGVLADECAALLSDFFRM 156
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 2-100 2.29e-15

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: 67.93  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775    2 VYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwcrqSGKSPSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQN 81
Cdd:pfam14437  30 VKDGKVIARGYNRKELNADTTAHAEILAIQQA------AKKLGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGN 103

                          90
                  ....*....|....*....
gi 555943775   82 ERFGGCGSVLNIASADLPN 100
Cdd:pfam14437 104 PKGGAVGSVLNKLVIVLWN 122
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
4-78 4.60e-15

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 66.17  E-value: 4.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 555943775    4 NNEVVGKGRNEVNQTKNATRHAEMVAIDQVLDwcrqsgKSPSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYG 78
Cdd:pfam00383  32 DGEIIATGYNGENAGYDPTIHAERNAIRQAGK------RGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 2-88 1.09e-06

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: 46.59  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   2 VYNNEVVGKGRnevnqTKNA-TRHAEMVAIDQVldwcrqsGKSPSEvfehTVLYVTVEPCIM------CAAALRLMKIPL 74
Cdd:COG0117   29 VKDGRIVGEGY-----HQRAgGPHAEVNALAQA-------GEAARG----ATLYVTLEPCSHhgrtppCADALIEAGIKR 92

                         90
                 ....*....|....*.
gi 555943775  75 VVYGCQ--NERFGGCG 88
Cdd:COG0117   93 VVIAMLdpNPLVAGKG 108
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
24-77 3.93e-05

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 40.98  E-value: 3.93e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 555943775  24 HAEMVAIDQvldwCRQSGKSPsevfEHTVLYVTVEPCIMCAAALRLMKIPLVVY 77
Cdd:COG2131   80 HAEQNAILQ----AARHGVST----EGATLYVTHFPCLECAKMIIQAGIKRVVY 125
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 24-77 1.02e-04

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 39.57  E-value: 1.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 555943775  24 HAEMVAIDQvldwCRQSGKSPsevfEHTVLYVTVEPCIMCAAALRLMKIPLVVY 77
Cdd:cd01286   70 HAEQNAILQ----AARHGVSL----EGATLYVTLFPCIECAKLIIQAGIKKVVY 115
Bd3614-deam pfam14439
Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 6-65 1.04e-04

Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Bdellovibrio Bd3614. They are typified by a distinct N-terminal globular domain. The Bdellovibrio version occurs in a predicted operon with a 23S rRNA G2445-modifying methylase suggesting that it might be involved in RNA editing.


Pssm-ID: 405177 [Multi-domain]  Cd Length: 113  Bit Score: 39.43  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775    6 EVVGKGRNevNQTKNATRHAEMVAIdQVLDWCRQSGKSPsevfEHTVLYVTVEPCIMCAA 65
Cdd:pfam14439  20 QLLDAAVN--TNAKNKTLHAEVNLL-QPLLRETARRPIP----PGARLLVTLQCCKMCAA 72
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 7-78 4.15e-04

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. 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.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 37.53  E-value: 4.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555943775   7 VVGKGRNEVNQTKNATRHAEMVAIDQvldwcrqsgKSPSEVFEHTVLYVTVEPCIMCAAALRL--MKIPLVVYG 78
Cdd:cd00786   32 KVGRGCNIENAAYSMCNHAERTALFN---------AGSEGDTKGQMLYVALSPCGACAQLIIElgIKDVIVVLT 96
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 4-79 5.43e-03

Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.


Pssm-ID: 238611 [Multi-domain]  Cd Length: 115  Bit Score: 34.52  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943775   4 NNEVVGKGRNEvnqtKNATRHAEMVAIDQVLDwcrqsgkspsEVFEHTVLYVTVEPCIM------CAAALRLMKIPLVVY 77
Cdd:cd01284   29 DGEIVGEGYHR----KAGGPHAEVNALASAGE----------KLARGATLYVTLEPCSHhgktppCVDAIIEAGIKRVVV 94


                 ..
gi 555943775  78 GC 79
Cdd:cd01284   95 GV 96
 
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