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Conserved domains on  [gi|160339756|gb|ABX12843|]
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CMP/dCMP deaminase zinc-binding [Nitrosopumilus maritimus SCM1]

Protein Classification

deoxycytidylate deaminase( domain architecture ID 10788416)

deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase

CATH:  3.40.140.10
EC:  3.5.4.12
Gene Ontology:  GO:0004132|GO:0008270|GO:0009972|GO:0006220
PubMed:  2247612
SCOP:  4000564

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
29-182 5.44e-72

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 214.70  E-value: 5.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  29 STFERPNWDEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCkrcqLRMEGKIESGASLDRC 108
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGC----LREKLGIPSGERGECC 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160339756 109 LCNHAEANAIMHCAILGIeaGIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYP-ETDFDLLKEAGVEVIQLD 182
Cdd:COG2131   77 RTVHAEQNAILQAARHGV--STEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPdELAKELLKEAGVEVRQLE 149
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
29-182 5.44e-72

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 214.70  E-value: 5.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  29 STFERPNWDEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCkrcqLRMEGKIESGASLDRC 108
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGC----LREKLGIPSGERGECC 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160339756 109 LCNHAEANAIMHCAILGIeaGIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYP-ETDFDLLKEAGVEVIQLD 182
Cdd:COG2131   77 RTVHAEQNAILQAARHGV--STEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPdELAKELLKEAGVEVRQLE 149
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 37-167 6.60e-56

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: 173.23  E-value: 6.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  37 DEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCKRCQLrmegkiESGASLDRCLCNHAEAN 116
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL------PSGEDQKCCRTVHAEQN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160339756 117 AIMHCAILGIEagIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYPETD 167
Cdd:cd01286   75 AILQAARHGVS--LEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDD 123
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 32-192 2.40e-32

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 113.80  E-value: 2.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756   32 ERPNWDEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCkrcqlrmegKIESGASLdRCLcn 111
Cdd:TIGR02571   1 ERIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGC---------YVVDGHCV-RTI-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  112 HAEANAIMHCAILGieAGIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYPETDF--DLLKEAGVEV--IQLDKAKIA 187
Cdd:TIGR02571  69 HAEMNALLQCAKFG--VSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYaiELFEQAGVELkkVPFDPSYLA 146


                  ....*
gi 160339756  188 KWAQE 192
Cdd:TIGR02571 147 QYNTQ 151
cd PHA02588
deoxycytidylate deaminase; Provisional
 40-188 1.04e-28

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 105.22  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  40 FMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCKRCQLRMEGKIESGASLDRCL---CN--HAE 114
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGWLDDEGKLKKEHRPEHSAwssKNeiHAE 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160339756 115 ANAIMHCAILGIEagIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSY---PETDFDLLKEAGVEVIQLDKAKIAK 188
Cdd:PHA02588  86 LNAILFAARNGIS--IEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdrnGPGWDDILRKSGIEVIQIPKEELNK 160
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
36-160 1.35e-24

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 92.36  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756   36 WDEYFMLQAELAKLRS-NCITRQVGAVIVR-NHRQLATGYNGTPpgikncfdggckrcqlrmegkiesgASLDRCLcnHA 113
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGEN-------------------------AGYDPTI--HA 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 160339756  114 EANAIMHCAILGIEAGIEGAVLYTTFVPCLECTKMAITIGIRKFVCL 160
Cdd:pfam00383  54 ERNAIRQAGKRGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
29-182 5.44e-72

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 214.70  E-value: 5.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  29 STFERPNWDEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCkrcqLRMEGKIESGASLDRC 108
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGC----LREKLGIPSGERGECC 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160339756 109 LCNHAEANAIMHCAILGIeaGIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYP-ETDFDLLKEAGVEVIQLD 182
Cdd:COG2131   77 RTVHAEQNAILQAARHGV--STEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPdELAKELLKEAGVEVRQLE 149
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 37-167 6.60e-56

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: 173.23  E-value: 6.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  37 DEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCKRCQLrmegkiESGASLDRCLCNHAEAN 116
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL------PSGEDQKCCRTVHAEQN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160339756 117 AIMHCAILGIEagIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYPETD 167
Cdd:cd01286   75 AILQAARHGVS--LEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDD 123
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 32-192 2.40e-32

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 113.80  E-value: 2.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756   32 ERPNWDEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCkrcqlrmegKIESGASLdRCLcn 111
Cdd:TIGR02571   1 ERIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGC---------YVVDGHCV-RTI-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  112 HAEANAIMHCAILGieAGIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSYPETDF--DLLKEAGVEV--IQLDKAKIA 187
Cdd:TIGR02571  69 HAEMNALLQCAKFG--VSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYaiELFEQAGVELkkVPFDPSYLA 146


                  ....*
gi 160339756  188 KWAQE 192
Cdd:TIGR02571 147 QYNTQ 151
cd PHA02588
deoxycytidylate deaminase; Provisional
 40-188 1.04e-28

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 105.22  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  40 FMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNGTPPGIKNCFDGGCKRCQLRMEGKIESGASLDRCL---CN--HAE 114
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGWLDDEGKLKKEHRPEHSAwssKNeiHAE 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160339756 115 ANAIMHCAILGIEagIEGAVLYTTFVPCLECTKMAITIGIRKFVCLDSY---PETDFDLLKEAGVEVIQLDKAKIAK 188
Cdd:PHA02588  86 LNAILFAARNGIS--IEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdrnGPGWDDILRKSGIEVIQIPKEELNK 160
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
36-160 1.35e-24

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 92.36  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756   36 WDEYFMLQAELAKLRS-NCITRQVGAVIVR-NHRQLATGYNGTPpgikncfdggckrcqlrmegkiesgASLDRCLcnHA 113
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGEN-------------------------AGYDPTI--HA 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 160339756  114 EANAIMHCAILGIEAGIEGAVLYTTFVPCLECTKMAITIGIRKFVCL 160
Cdd:pfam00383  54 ERNAIRQAGKRGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 35-158 8.58e-11

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: 57.53  E-value: 8.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756   35 NWDEYFMLQAELAKLRSNCITRQVGAVIVRNHRQLATGYNgtppgikncfdggckrcqlRMEGKIESGAsldrclcnHAE 114
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYN-------------------RKELNADTTA--------HAE 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 160339756  115 ANAIMHCAILGIEAGIEGAVLYTTFVPCLECTKMAITIGIRKFV 158
Cdd:pfam14437  55 ILAIQQAAKKLGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLV 98
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 57-160 7.28e-08

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: 48.32  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  57 QVGAVIVRNHrqlatGYNGTPPGikncfdggckrCQLRMegkiesgasLDRCLCNHAEANAIMHCailGIEAGIEGAVLY 136
Cdd:cd00786   19 QVGACLVNKK-----DGGKVGRG-----------CNIEN---------AAYSMCNHAERTALFNA---GSEGDTKGQMLY 70

                         90       100
                 ....*....|....*....|....
gi 160339756 137 TTFVPCLECTKMAITIGIRKFVCL 160
Cdd:cd00786   71 VALSPCGACAQLIIELGIKDVIVV 94
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 37-166 3.91e-04

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: 38.95  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  37 DEYFMLQA-ELAK--LRSNCItrQVGAVIVRNHRQLATGYNgtppgikncfdggckrcqlRMEGkiesgaslDRCLCNHA 113
Cdd:COG0590    4 DEEFMRRAlELARkaVAEGEV--PVGAVLVKDGEIIARGHN-------------------RVET--------LNDPTAHA 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 160339756 114 EANAIMH-CAILGiEAGIEGAVLYTTFVPCLECTkMAITI-GIRKFVCLDSYPET 166
Cdd:COG0590   55 EILAIRAaARKLG-NWRLSGCTLYVTLEPCPMCA-GAIVWaRIGRVVYGASDPKA 107
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 58-175 6.89e-04

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: 37.98  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160339756  58 VGAVIVR-NHRQLATGYN---GTPpgikncfdggckrcqlrmegkiesgasldrclcnHAEANAIMHCAilgiEAGIEGA 133
Cdd:cd01284   21 VGCVIVDdDGEIVGEGYHrkaGGP----------------------------------HAEVNALASAG----EKLARGA 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 160339756 134 VLYTTFVPCLE------CTKMAITIGIRKFVCLDSYPETD-----FDLLKEAG 175
Cdd:cd01284   63 TLYVTLEPCSHhgktppCVDAIIEAGIKRVVVGVRDPNPLvagkgAERLRAAG 115
 
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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