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Conserved domains on  [gi|1466823148|gb|RGL55300|]
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nucleoside deaminase [Bifidobacterium adolescentis]

Protein Classification

nucleoside deaminase( domain architecture ID 10001752)

nucleoside deaminase such as adenosine, guanine, or cytosine deaminase is a Zn-dependent enzyme which catalyzes 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

EC:  3.5.4.-
Gene Ontology:  GO:0008270|GO:0019239|GO:0009116
PubMed:  38524700
SCOP:  3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 21-148 4.20e-62

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: 187.63  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAaDGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:COG0590    22 GEVPVGAVLVK-DGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVY 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1466823148 101 GAWDAKLGACGSVWDIPRDPHVGLVPEVIGGVREAECGRLMTDFFARR 148
Cdd:COG0590   101 GASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 21-148 4.20e-62

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: 187.63  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAaDGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:COG0590    22 GEVPVGAVLVK-DGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVY 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1466823148 101 GAWDAKLGACGSVWDIPRDPHVGLVPEVIGGVREAECGRLMTDFFARR 148
Cdd:COG0590   101 GASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 21-115 1.48e-41

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: 134.28  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAADGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:cd01285    15 GEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMCAGALLWARIKRVVY 94

                          90
                  ....*....|....*
gi 1466823148 101 GAWDAKLGACGSVWD 115
Cdd:cd01285    95 GASDPKLGGIGFLIE 109
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 20-149 5.84e-40

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 132.24  E-value: 5.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  20 DGEVPVGAVvLAADGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIV 99
Cdd:PRK10860   30 EREVPVGAV-LVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCVMCAGAMVHSRIGRLV 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1466823148 100 FGAWDAKLGACGSVWDIPRDPHVGLVPEVIGGVREAECGRLMTDFFARRR 149
Cdd:PRK10860  109 FGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRR 158
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 21-149 7.94e-32

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: 110.69  E-value: 7.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAaDGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:pfam14437  21 GEVPIGAVIVK-DGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVY 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1466823148 101 GAWDAKLGACGSV---WDIPRDPHvglvpEVigGVREAECGRLMTDFFARRR 149
Cdd:pfam14437 100 GAGNPKGGAVGSVlnkLVIVLWNH-----RV--ELVEEDCSEILKGFFKKLR 144
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 24-149 1.05e-10

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 58.30  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  24 PVGAVVLAaDGRVIGRGRNLREThadpLAHAEVKAMAEAAAslgtwNLADCTLVVTLEPC------PMCAGACLQTHIGR 97
Cdd:TIGR00326  20 LVGCVIVK-NGEIVGEGAHQKAG----EPHAEVHALRQAGE-----NAKGATAYVTLEPCshqgrtPPCAEAIIEAGIKK 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1466823148  98 IVFGAWDAKLGACGSvwDIPRDPHVGLvpEVIGGVREAECGRLMTDFFARRR 149
Cdd:TIGR00326  90 VVVSMQDPNPLVAGR--GAERLKQAGI--EVTFGILKEEAERLNKGFLKRMR 137
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 21-148 4.20e-62

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: 187.63  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAaDGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:COG0590    22 GEVPVGAVLVK-DGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVY 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1466823148 101 GAWDAKLGACGSVWDIPRDPHVGLVPEVIGGVREAECGRLMTDFFARR 148
Cdd:COG0590   101 GASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 21-115 1.48e-41

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: 134.28  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAADGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:cd01285    15 GEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMCAGALLWARIKRVVY 94

                          90
                  ....*....|....*
gi 1466823148 101 GAWDAKLGACGSVWD 115
Cdd:cd01285    95 GASDPKLGGIGFLIE 109
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 20-149 5.84e-40

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 132.24  E-value: 5.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  20 DGEVPVGAVvLAADGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIV 99
Cdd:PRK10860   30 EREVPVGAV-LVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCVMCAGAMVHSRIGRLV 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1466823148 100 FGAWDAKLGACGSVWDIPRDPHVGLVPEVIGGVREAECGRLMTDFFARRR 149
Cdd:PRK10860  109 FGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRR 158
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 21-149 7.94e-32

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: 110.69  E-value: 7.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  21 GEVPVGAVVLAaDGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIVF 100
Cdd:pfam14437  21 GEVPIGAVIVK-DGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVY 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1466823148 101 GAWDAKLGACGSV---WDIPRDPHvglvpEVigGVREAECGRLMTDFFARRR 149
Cdd:pfam14437 100 GAGNPKGGAVGSVlnkLVIVLWNH-----RV--ELVEEDCSEILKGFFKKLR 144
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
20-101 2.11e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 95.45  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  20 DGEVPVGAVVLAADGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTWNLADCTLVVTLEPCPMCAGACLQTHIGRIV 99
Cdd:pfam00383  19 YSNFPVGAVIVKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVV 98


                  ..
gi 1466823148 100 FG 101
Cdd:pfam00383  99 FG 100
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 24-112 1.17e-14

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: 65.72  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  24 PVGAVVLAADGRVIGRGRnlreTHADPLAHAEVKAMAEAAASLgtwnLADCTLVVTLEPC------PMCAGACLQTHIGR 97
Cdd:cd01284    20 PVGCVIVDDDGEIVGEGY----HRKAGGPHAEVNALASAGEKL----ARGATLYVTLEPCshhgktPPCVDAIIEAGIKR 91

                          90
                  ....*....|....*
gi 1466823148  98 IVFGAWDAKLGACGS 112
Cdd:cd01284    92 VVVGVRDPNPLVAGK 106
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 24-149 5.63e-14

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: 67.39  E-value: 5.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  24 PVGAVVLAaDGRVIGRGRnlretHADPL-AHAEVKAMAEAAASLgtwnlADCTLVVTLEPC------PMCAGACLQTHIG 96
Cdd:COG0117    23 LVGCVIVK-DGRIVGEGY-----HQRAGgPHAEVNALAQAGEAA-----RGATLYVTLEPCshhgrtPPCADALIEAGIK 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1466823148  97 RIVFGAWDAKLGACGSVWDIPRDPHVglvpEVIGGVREAECGRLMTDFFARRR 149
Cdd:COG0117    92 RVVIAMLDPNPLVAGKGIARLRAAGI----EVEVGVLEEEARALNRGFLKRMR 140
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 20-100 6.18e-11

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: 55.63  E-value: 6.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  20 DGEVPVGAVVL-AADGRVIGRGRNLRETHADPLAHAEVKAMAEAAASLGTwnlADCTLVVTLEPCPMCAGACLQTHIGRI 98
Cdd:cd00786    15 ESNFQVGACLVnKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDT---KGQMLYVALSPCGACAQLIIELGIKDV 91


                  ..
gi 1466823148  99 VF 100
Cdd:cd00786    92 IV 93
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 24-149 1.05e-10

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 58.30  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  24 PVGAVVLAaDGRVIGRGRNLREThadpLAHAEVKAMAEAAAslgtwNLADCTLVVTLEPC------PMCAGACLQTHIGR 97
Cdd:TIGR00326  20 LVGCVIVK-NGEIVGEGAHQKAG----EPHAEVHALRQAGE-----NAKGATAYVTLEPCshqgrtPPCAEAIIEAGIKK 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1466823148  98 IVFGAWDAKLGACGSvwDIPRDPHVGLvpEVIGGVREAECGRLMTDFFARRR 149
Cdd:TIGR00326  90 VVVSMQDPNPLVAGR--GAERLKQAGI--EVTFGILKEEAERLNKGFLKRMR 137
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
25-100 5.52e-08

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 49.07  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  25 VGAVvLAADGRVIGRGRN--------------LRETHADPLA---------HAEVKAMAEAAASlGTwNLADCTLVVTLE 81
Cdd:COG2131    30 VGAV-IVKDKRILATGYNgapsglphcdevgcLREKLGIPSGergeccrtvHAEQNAILQAARH-GV-STEGATLYVTHF 106

                          90
                  ....*....|....*....
gi 1466823148  82 PCPMCAGACLQTHIGRIVF 100
Cdd:COG2131   107 PCLECAKMIIQAGIKRVVY 125
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 25-100 7.65e-08

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: 48.04  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  25 VGAVVLAaDGRVIGRGRN-----------LRETHADPLA----------HAEVKAMAeAAASLGTwNLADCTLVVTLEPC 83
Cdd:cd01286    22 VGAVIVK-DKRIISTGYNgspsglphcaeVGCERDDLPSgedqkccrtvHAEQNAIL-QAARHGV-SLEGATLYVTLFPC 98

                          90
                  ....*....|....*..
gi 1466823148  84 PMCAGACLQTHIGRIVF 100
Cdd:cd01286    99 IECAKLIIQAGIKKVVY 115
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 25-147 4.55e-06

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 44.76  E-value: 4.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  25 VGAVVLAaDGRVIGRGRNLREthADPlaHAEVKAMAEAAaslgtwNLAD-CTLVVTLEPC------PMCAGACLQTHIGR 97
Cdd:PLN02807   56 VGCVIVK-DGRIVGEGFHPKA--GQP--HAEVFALRDAG------DLAEnATAYVSLEPCnhygrtPPCTEALIKAKVKR 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1466823148  98 IVFGAWDAKLGACGSVWDIPRDPHVglvpEVIGGVREAECGRLMTDFFAR 147
Cdd:PLN02807  125 VVVGMVDPNPIVASKGIERLRDAGI----EVTVGVEEELCRKLNEAFIHR 170
cd PHA02588
deoxycytidylate deaminase; Provisional
 25-101 1.69e-04

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 39.74  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466823148  25 VGAVvLAADGRVIGRGRN------------------------LRETHADPLA--------HAEVKAMAEAAASlGTwNLA 72
Cdd:PHA02588   24 VGAV-IEKNGRIISTGYNgtpaggvnccdhaneqgwlddegkLKKEHRPEHSawsskneiHAELNAILFAARN-GI-SIE 100

                          90       100
                  ....*....|....*....|....*....
gi 1466823148  73 DCTLVVTLEPCPMCAGACLQTHIGRIVFG 101
Cdd:PHA02588  101 GATMYVTASPCPDCAKAIAQSGIKKLVYC 129
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 29-99 2.67e-03

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 36.67  E-value: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466823148  29 VLAADGRVIGRGRNLRETHAdplaHAEVKA--MAEAAASlgtwnlaDCTLVVTLEPC------PMCAGACLQTHIGRIV 99
Cdd:PRK10786   30 VIVKDGEIVGEGYHQRAGEP----HAEVHAlrMAGEKAK-------GATAYVTLEPCshhgrtPPCCDALIAAGVARVV 97
 
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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