Cytidine/deoxycytidylate deaminase family protein [Arabidopsis thaliana]
Protein Classification
cytidine/deoxycytidylate deaminase family protein( domain architecture ID 923)
cytidine/deoxycytidylate deaminase family protein similar to Bacillus subtilis cytidine deaminase that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| cytidine_deaminase-like super family | cl00269 | Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
327-375 | 3.47e-15 | ||
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. The actual alignment was detected with superfamily member cd01285: Pssm-ID: 444801 [Multi-domain] Cd Length: 109 Bit Score: 71.11 E-value: 3.47e-15
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| Name | Accession | Description | Interval | E-value | ||
| nucleoside_deaminase | cd01285 | Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
327-375 | 3.47e-15 | ||
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: 71.11 E-value: 3.47e-15
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| TadA | COG0590 | tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
332-402 | 1.77e-14 | ||
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: 70.15 E-value: 1.77e-14
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| PRK10860 | PRK10860 | tRNA-specific adenosine deaminase; Provisional |
336-384 | 1.18e-06 | ||
tRNA-specific adenosine deaminase; Provisional Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 48.26 E-value: 1.18e-06
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| dCMP_cyt_deam_1 | pfam00383 | Cytidine and deoxycytidylate deaminase zinc-binding region; |
333-361 | 5.93e-06 | ||
Cytidine and deoxycytidylate deaminase zinc-binding region; Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 44.60 E-value: 5.93e-06
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| Name | Accession | Description | Interval | E-value | ||
| nucleoside_deaminase | cd01285 | Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ... |
327-375 | 3.47e-15 | ||
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: 71.11 E-value: 3.47e-15
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| TadA | COG0590 | tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ... |
332-402 | 1.77e-14 | ||
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: 70.15 E-value: 1.77e-14
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| PRK10860 | PRK10860 | tRNA-specific adenosine deaminase; Provisional |
336-384 | 1.18e-06 | ||
tRNA-specific adenosine deaminase; Provisional Pssm-ID: 182786 [Multi-domain] Cd Length: 172 Bit Score: 48.26 E-value: 1.18e-06
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| dCMP_cyt_deam_1 | pfam00383 | Cytidine and deoxycytidylate deaminase zinc-binding region; |
333-361 | 5.93e-06 | ||
Cytidine and deoxycytidylate deaminase zinc-binding region; Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 44.60 E-value: 5.93e-06
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| MafB19-deam | pfam14437 | MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ... |
336-389 | 1.57e-04 | ||
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: 41.74 E-value: 1.57e-04
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