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Conserved domains on  [gi|1842032931|ref|YP_009819870|]
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dCMP deaminase [Streptomyces phage Vash]

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
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
6-128 8.35e-33

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 113.01  E-value: 8.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931   6 RPDWDTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCASAGaCPRGRLSAAEcAPNSDYANCVad 85
Cdd:COG2131     5 RPSWDEYFMEIAKLVALRSTCLRRQVGAVIVK-DKRILATGYNGAPSGLPHCDEVG-CLREKLGIPS-GERGECCRTV-- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1842032931  86 HAERNAIRHAPA--AELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:COG2131    80 HAEQNAILQAARhgVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
6-128 8.35e-33

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 113.01  E-value: 8.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931   6 RPDWDTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCASAGaCPRGRLSAAEcAPNSDYANCVad 85
Cdd:COG2131     5 RPSWDEYFMEIAKLVALRSTCLRRQVGAVIVK-DKRILATGYNGAPSGLPHCDEVG-CLREKLGIPS-GERGECCRTV-- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1842032931  86 HAERNAIRHAPA--AELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:COG2131    80 HAEQNAILQAARhgVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-131 9.47e-27

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: 96.96  E-value: 9.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931  10 DTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCASAGaCPRGRLSAAEcapNSDYANCVadHAER 89
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVG-CERDDLPSGE---DQKCCRTV--HAEQ 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1842032931  90 NAIRHA--PAAELPGSTLYTTREPCPACWTLIRAARIRRVVTPE 131
Cdd:cd01286    74 NAILQAarHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAE 117
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-128 2.46e-19

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 76.96  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931   9 WDTYFLAGAAWVATRA-DCTRSQVGAILVNANHEVRGTGYNGAPSGVPGCAsagacprgrlsaaecapnsdyancvadHA 87
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAGYDPTI---------------------------HA 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1842032931  88 ERNAIRHA----PAAELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:pfam00383  54 ERNAIRQAgkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVV 98
cd PHA02588
deoxycytidylate deaminase; Provisional
 10-128 2.93e-17

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 73.64  E-value: 2.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931  10 DTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCA-----SAGACPRGRLSAAECAPNSDYANCVA 84
Cdd:PHA02588    3 DSTYLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGGVNCCdhaneQGWLDDEGKLKKEHRPEHSAWSSKNE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1842032931  85 DHAERNAIRHAPAA--ELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:PHA02588   82 IHAELNAILFAARNgiSIEGATMYVTASPCPDCAKAIAQSGIKKLV 127
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
6-128 8.35e-33

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 113.01  E-value: 8.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931   6 RPDWDTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCASAGaCPRGRLSAAEcAPNSDYANCVad 85
Cdd:COG2131     5 RPSWDEYFMEIAKLVALRSTCLRRQVGAVIVK-DKRILATGYNGAPSGLPHCDEVG-CLREKLGIPS-GERGECCRTV-- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1842032931  86 HAERNAIRHAPA--AELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:COG2131    80 HAEQNAILQAARhgVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-131 9.47e-27

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: 96.96  E-value: 9.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931  10 DTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCASAGaCPRGRLSAAEcapNSDYANCVadHAER 89
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVG-CERDDLPSGE---DQKCCRTV--HAEQ 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1842032931  90 NAIRHA--PAAELPGSTLYTTREPCPACWTLIRAARIRRVVTPE 131
Cdd:cd01286    74 NAILQAarHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAE 117
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-128 2.46e-19

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 76.96  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931   9 WDTYFLAGAAWVATRA-DCTRSQVGAILVNANHEVRGTGYNGAPSGVPGCAsagacprgrlsaaecapnsdyancvadHA 87
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAGYDPTI---------------------------HA 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1842032931  88 ERNAIRHA----PAAELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:pfam00383  54 ERNAIRQAgkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVV 98
cd PHA02588
deoxycytidylate deaminase; Provisional
 10-128 2.93e-17

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 73.64  E-value: 2.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931  10 DTYFLAGAAWVATRADCTRSQVGAILVNaNHEVRGTGYNGAPSGVPGCA-----SAGACPRGRLSAAECAPNSDYANCVA 84
Cdd:PHA02588    3 DSTYLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGGVNCCdhaneQGWLDDEGKLKKEHRPEHSAWSSKNE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1842032931  85 DHAERNAIRHAPAA--ELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:PHA02588   82 IHAELNAILFAARNgiSIEGATMYVTASPCPDCAKAIAQSGIKKLV 127
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 31-128 6.30e-10

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: 53.00  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931  31 VGAILVNANHEVRGTGYNGAPSGvpgcasagacprgrlsaaecapnsdyaNCVADHAERNAIRHAPAA----ELPGSTLY 106
Cdd:cd01285    19 FGAVIVDDDGKVIARGHNRVEQD---------------------------GDPTAHAEIVAIRNAARRlgsyLLSGCTLY 71

                          90       100
                  ....*....|....*....|..
gi 1842032931 107 TTREPCPACWTLIRAARIRRVV 128
Cdd:cd01285    72 TTLEPCPMCAGALLWARIKRVV 93
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 31-128 2.17e-09

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: 51.85  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931  31 VGAILVNANHEVRGTGYNgAPSGVPgcasagacprgrlsaaecapnsdyancvadHAERNAIRHAPAAELPGSTLYTTRE 110
Cdd:cd01284    21 VGCVIVDDDGEIVGEGYH-RKAGGP------------------------------HAEVNALASAGEKLARGATLYVTLE 69

                          90       100
                  ....*....|....*....|....
gi 1842032931 111 PC------PACWTLIRAARIRRVV 128
Cdd:cd01284    70 PCshhgktPPCVDAIIEAGIKRVV 93
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 86-128 2.21e-09

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: 52.43  E-value: 2.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1842032931  86 HAERNAIRHAPAA----ELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:COG0590    53 HAEILAIRAAARKlgnwRLSGCTLYVTLEPCPMCAGAIVWARIGRVV 99
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 8-128 2.37e-08

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: 49.44  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842032931   8 DWDTYFLAGAAWVATRADCTRSQVGAILVNANhEVRGTGYNGAPSgvpgcasagacprgrlsaaecapNSDyancVADHA 87
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVKDG-KVIARGYNRKEL-----------------------NAD----TTAHA 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1842032931  88 ERNAIRHAP----AAELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:pfam14437  54 EILAIQQAAkklgSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLV 98
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 85-128 2.68e-08

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 50.83  E-value: 2.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1842032931  85 DHAERNAIRHApAAELPGSTLYTTREPC------PACWTLIRAARIRRVV 128
Cdd:COG0117    46 PHAEVNALAQA-GEAARGATLYVTLEPCshhgrtPPCADALIEAGIKRVV 94
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 86-128 1.91e-03

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: 35.60  E-value: 1.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1842032931  86 HAERNAIRHAPA-AELPGSTLYTTREPCPACWTLIRAARIRRVV 128
Cdd:cd00786    49 HAERTALFNAGSeGDTKGQMLYVALSPCGACAQLIIELGIKDVI 92
 
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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