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Conserved domains on  [gi|1720380872|ref|XP_030103902|]
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cytidine and dCMP deaminase domain-containing protein 1 isoform X2 [Mus musculus]

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 ...
 20-139 1.10e-31

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: 111.98  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  20 DHKTGVGAVIWAEAKSRScdgTGAMYFIGCGYNAFPVGSEYADFPhmddkhkDREIRKFRYIIHAEQNALTFRCQDIKPE 99
Cdd:cd01286    17 CPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVHAEQNAILQAARHGVSL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720380872 100 ERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 139
Cdd:cd01286    87 EGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 20-139 1.10e-31

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: 111.98  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  20 DHKTGVGAVIWAEAKSRScdgTGAMYFIGCGYNAFPVGSEYADFPhmddkhkDREIRKFRYIIHAEQNALTFRCQDIKPE 99
Cdd:cd01286    17 CPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVHAEQNAILQAARHGVSL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720380872 100 ERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 139
Cdd:cd01286    87 EGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
25-127 2.60e-08

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 50.99  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  25 VGAVIwaeAKSRScdgtgamyFIGCGYNAFPVGSEYADFP-HMDDKHKDREIR--KFRYIIHAEQNALTFRCQDIKPEER 101
Cdd:COG2131    30 VGAVI---VKDKR--------ILATGYNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHAEQNAILQAARHGVSTEG 98

                          90       100
                  ....*....|....*....|....*.
gi 1720380872 102 SMIFVTKCPCDECVPLIKGAGIKQIY 127
Cdd:COG2131    99 ATLYVTHFPCLECAKMIIQAGIKRVV 124
cd PHA02588
deoxycytidylate deaminase; Provisional
 25-130 5.53e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 44.75  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  25 VGAVIwaeaksrSCDGTgamyFIGCGYNAFPVGS----EYADFP-HMDDKHKDREIRKFRY-------IIHAEQNALTFR 92
Cdd:PHA02588   24 VGAVI-------EKNGR----IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720380872  93 CQDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 130
Cdd:PHA02588   93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
72-129 6.13e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 43.44  E-value: 6.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  72 DREIRKFRYIIHAEQNALTFRC--QDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 129
Cdd:pfam00383  41 NGENAGYDPTIHAERNAIRQAGkrGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 20-139 1.10e-31

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: 111.98  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  20 DHKTGVGAVIWAEAKSRScdgTGAMYFIGCGYNAFPVGSEYADFPhmddkhkDREIRKFRYIIHAEQNALTFRCQDIKPE 99
Cdd:cd01286    17 CPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVHAEQNAILQAARHGVSL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720380872 100 ERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 139
Cdd:cd01286    87 EGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
25-127 2.60e-08

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 50.99  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  25 VGAVIwaeAKSRScdgtgamyFIGCGYNAFPVGSEYADFP-HMDDKHKDREIR--KFRYIIHAEQNALTFRCQDIKPEER 101
Cdd:COG2131    30 VGAVI---VKDKR--------ILATGYNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHAEQNAILQAARHGVSTEG 98

                          90       100
                  ....*....|....*....|....*.
gi 1720380872 102 SMIFVTKCPCDECVPLIKGAGIKQIY 127
Cdd:COG2131    99 ATLYVTHFPCLECAKMIIQAGIKRVV 124
cd PHA02588
deoxycytidylate deaminase; Provisional
 25-130 5.53e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 44.75  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  25 VGAVIwaeaksrSCDGTgamyFIGCGYNAFPVGS----EYADFP-HMDDKHKDREIRKFRY-------IIHAEQNALTFR 92
Cdd:PHA02588   24 VGAVI-------EKNGR----IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720380872  93 CQDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 130
Cdd:PHA02588   93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
72-129 6.13e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 43.44  E-value: 6.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380872  72 DREIRKFRYIIHAEQNALTFRC--QDIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 129
Cdd:pfam00383  41 NGENAGYDPTIHAERNAIRQAGkrGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 74-126 6.88e-05

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: 40.23  E-value: 6.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720380872  74 EIRKFRYIIHAEQNALtFRCQDIKPEERSMIFVTKCPCDECVPLIKGAGIKQI 126
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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