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Conserved domains on  [gi|58865884|ref|NP_001012156|]
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cytidine and dCMP deaminase domain-containing protein 1 isoform 1 [Rattus norvegicus]

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

Graphical summary

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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 ...
 75-152 7.39e-09

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 cd01286:

Pssm-ID: 444801 [Multi-domain]  Cd Length: 131  Bit Score: 53.43  E-value: 7.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865884  75 DLARV----STD-KKQVkktGLVVVKNMKIIGL----------HCSSED-----------------LHTGQIALI---KH 119
Cdd:cd01286   6 AIARLaalrSTCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRH 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 58865884 120 GSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 152
Cdd:cd01286  83 GVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 75-152 7.39e-09

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: 53.43  E-value: 7.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865884  75 DLARV----STD-KKQVkktGLVVVKNMKIIGL----------HCSSED-----------------LHTGQIALI---KH 119
Cdd:cd01286   6 AIARLaalrSTCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRH 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 58865884 120 GSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 152
Cdd:cd01286  83 GVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
80-165 7.80e-08

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 50.99  E-value: 7.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865884  80 STD-KKQVkktGLVVVKNMKII---------GL-HC-------------SSED------LHTGQIALI---KHGSRLKNC 126
Cdd:COG2131  23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 58865884 127 DLYFSRKPCSACLKMIVNAGVNRISY---WPSDPEISLLTEA 165
Cdd:COG2131 100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
90-152 1.48e-04

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 40.36  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865884    90 GLVVVK-NMKIIGLHCSSED------LHTGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 152
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 75-152 7.39e-09

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: 53.43  E-value: 7.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865884  75 DLARV----STD-KKQVkktGLVVVKNMKIIGL----------HCSSED-----------------LHTGQIALI---KH 119
Cdd:cd01286   6 AIARLaalrSTCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRH 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 58865884 120 GSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 152
Cdd:cd01286  83 GVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
80-165 7.80e-08

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 50.99  E-value: 7.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865884  80 STD-KKQVkktGLVVVKNMKII---------GL-HC-------------SSED------LHTGQIALI---KHGSRLKNC 126
Cdd:COG2131  23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 58865884 127 DLYFSRKPCSACLKMIVNAGVNRISY---WPSDPEISLLTEA 165
Cdd:COG2131 100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
90-152 1.48e-04

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 40.36  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865884    90 GLVVVK-NMKIIGLHCSSED------LHTGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 152
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
 
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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