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Conserved domains on  [gi|270483870|ref|NP_001162009|]
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cytidine and dCMP deaminase domain-containing protein 1 isoform 4 [Mus musculus]

Protein Classification

cytidine deaminase; cytidine/deoxycytidylate deaminase family protein( domain architecture ID 10217272)

cytidine deaminase catalyzes the deamination of cytidine to uridine| 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
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 320-455 2.37e-37

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: 133.55  E-value: 2.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 320 ARHCMVQARLLAYRTEDHKTGVGAVIWAEAKSRScdgTGAMYFIGCGYNAFPVGSEYADFPhmddkhkDREIRKFRYIIH 399
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 270483870 400 AEQNALTFRCQDIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 455
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
cytidine_deaminase-like super family cl00269
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 83-152 1.37e-07

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: 50.35  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870  83 KKQVkktGLVVVKNMKIIGL----------HCSSED-----------------LHTGQIALI---KHGSRLKNCDLYFSR 132
Cdd:cd01286   19 RRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATLYVTL 95

                         90       100
                 ....*....|....*....|
gi 270483870 133 KPCSACLKMIVNAGVNRISY 152
Cdd:cd01286   96 FPCIECAKLIIQAGIKKVVY 115
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 320-455 2.37e-37

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: 133.55  E-value: 2.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 320 ARHCMVQARLLAYRTEDHKTGVGAVIWAEAKSRScdgTGAMYFIGCGYNAFPVGSEYADFPhmddkhkDREIRKFRYIIH 399
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 270483870 400 AEQNALTFRCQDIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 455
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
324-443 2.32e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 61.78  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 324 MVQARLLAYRTEDHKTGVGAVIwaeAKSRScdgtgamyFIGCGYNAFPVGSEYADFP-HMDDKHKDREIR--KFRYIIHA 400
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVI---VKDKR--------ILATGYNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 270483870 401 EQNALtfrCQDIK---PEERSMIFVTKCPCDECVPLIKGAGIKQIY 443
Cdd:COG2131   82 EQNAI---LQAARhgvSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 83-152 1.37e-07

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: 50.35  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870  83 KKQVkktGLVVVKNMKIIGL----------HCSSED-----------------LHTGQIALI---KHGSRLKNCDLYFSR 132
Cdd:cd01286   19 RRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATLYVTL 95

                         90       100
                 ....*....|....*....|
gi 270483870 133 KPCSACLKMIVNAGVNRISY 152
Cdd:cd01286   96 FPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
115-165 1.19e-06

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 48.30  E-value: 1.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 270483870 115 ALI---KHGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY---WPSDPEISLLTEA 165
Cdd:COG2131   85 AILqaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
324-445 1.90e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 46.14  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870  324 MVQARLLAYRTEDHKTG-VGAVIWAEAKSRscdgtgamyfIGCGYNafpvgseyadfphmddkhkdREIRKFRYIIHAEQ 402
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 270483870  403 NALTFRC--QDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 445
Cdd:pfam00383  56 NAIRQAGkrGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 341-446 1.38e-05

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 45.52  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 341 VGAVIwaeaksrSCDGTgamyFIGCGYNAFPVGS----EYADFP-HMDDKHKDREIRKFRY-------IIHAEQNALTFR 408
Cdd:PHA02588  24 VGAVI-------EKNGR----IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 270483870 409 CQDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 446
Cdd:PHA02588  93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
90-152 3.84e-04

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 39.59  E-value: 3.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270483870   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 ...
 320-455 2.37e-37

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: 133.55  E-value: 2.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 320 ARHCMVQARLLAYRTEDHKTGVGAVIWAEAKSRScdgTGAMYFIGCGYNAFPVGSEYADFPhmddkhkDREIRKFRYIIH 399
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 270483870 400 AEQNALTFRCQDIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 455
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
324-443 2.32e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 61.78  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 324 MVQARLLAYRTEDHKTGVGAVIwaeAKSRScdgtgamyFIGCGYNAFPVGSEYADFP-HMDDKHKDREIR--KFRYIIHA 400
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVI---VKDKR--------ILATGYNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 270483870 401 EQNALtfrCQDIK---PEERSMIFVTKCPCDECVPLIKGAGIKQIY 443
Cdd:COG2131   82 EQNAI---LQAARhgvSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 83-152 1.37e-07

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: 50.35  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870  83 KKQVkktGLVVVKNMKIIGL----------HCSSED-----------------LHTGQIALI---KHGSRLKNCDLYFSR 132
Cdd:cd01286   19 RRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATLYVTL 95

                         90       100
                 ....*....|....*....|
gi 270483870 133 KPCSACLKMIVNAGVNRISY 152
Cdd:cd01286   96 FPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
115-165 1.19e-06

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 48.30  E-value: 1.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 270483870 115 ALI---KHGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY---WPSDPEISLLTEA 165
Cdd:COG2131   85 AILqaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
324-445 1.90e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 46.14  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870  324 MVQARLLAYRTEDHKTG-VGAVIWAEAKSRscdgtgamyfIGCGYNafpvgseyadfphmddkhkdREIRKFRYIIHAEQ 402
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 270483870  403 NALTFRC--QDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 445
Cdd:pfam00383  56 NAIRQAGkrGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 341-446 1.38e-05

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 45.52  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483870 341 VGAVIwaeaksrSCDGTgamyFIGCGYNAFPVGS----EYADFP-HMDDKHKDREIRKFRY-------IIHAEQNALTFR 408
Cdd:PHA02588  24 VGAVI-------EKNGR----IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 270483870 409 CQDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 446
Cdd:PHA02588  93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
90-152 3.84e-04

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 39.59  E-value: 3.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270483870   90 GLVVVK-NMKIIGLHCSSED------LHTGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 152
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 390-442 4.38e-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: 39.46  E-value: 4.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 270483870 390 EIRKFRYIIHAEQNALtFRCQDIKPEERSMIFVTKCPCDECVPLIKGAGIKQI 442
Cdd:cd00786   40 ENAAYSMCNHAERTAL-FNAGSEGDTKGQMLYVALSPCGACAQLIIELGIKDV 91
 
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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