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Conserved domains on  [gi|490232952|ref|WP_004131292|]
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nucleoside deaminase [Gardnerella pickettii]

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 ...
 12-153 3.87e-70

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: 208.05  E-value: 3.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:COG0590    8 MRRALELARKAVAEGEVPVGAVLVKD-GEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMC 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIGSHPQVFGSVCESQCVQLLRNFFENH 153
Cdd:COG0590   87 AGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 12-153 3.87e-70

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: 208.05  E-value: 3.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:COG0590    8 MRRALELARKAVAEGEVPVGAVLVKD-GEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMC 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIGSHPQVFGSVCESQCVQLLRNFFENH 153
Cdd:COG0590   87 AGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 12-120 5.92e-50

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: 155.47  E-value: 5.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGSGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|....*....
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWD 120
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 12-150 2.38e-41

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: 134.96  E-value: 2.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952   12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:pfam14437   7 FRKALGLAEKAYDAGEVPIGAVIVKD-GKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPCPMC 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490232952   92 AGAILQTHISSVVFGAWDSKLGACGSVWDILrDPHIGSHpQVfgSVCESQCVQLLRNFF 150
Cdd:pfam14437  86 AGAIVQAGLKSLVYGAGNPKGGAVGSVLNKL-VIVLWNH-RV--ELVEEDCSEILKGFF 140
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 12-154 4.27e-41

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 135.32  E-value: 4.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:PRK10860  17 MRHALTLAKRAWDEREVPVGAVLVHN-NRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCVMC 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIGSHPQVFGSVCESQCVQLLRNFFENHR 154
Cdd:PRK10860  96 AGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRR 158
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 12-149 1.23e-14

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: 69.47  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952   12 MQEALRLAQVAADCGEV--PVGAVVVDGsGAIIGRGSNLREQdadpLSHAEILAIRQAADvrkswNLSDCTLVVTLEPC- 88
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPnpLVGCVIVKN-GEIVGEGAHQKAG----EPHAEVHALRQAGE-----NAKGATAYVTLEPCs 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490232952   89 -----PMCAGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIgshpQVFGSVCESQCVQLLRNF 149
Cdd:TIGR00326  71 hqgrtPPCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGF 132
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 12-153 3.87e-70

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: 208.05  E-value: 3.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:COG0590    8 MRRALELARKAVAEGEVPVGAVLVKD-GEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMC 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIGSHPQVFGSVCESQCVQLLRNFFENH 153
Cdd:COG0590   87 AGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 12-120 5.92e-50

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: 155.47  E-value: 5.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGSGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|....*....
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWD 120
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 12-150 2.38e-41

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: 134.96  E-value: 2.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952   12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:pfam14437   7 FRKALGLAEKAYDAGEVPIGAVIVKD-GKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPCPMC 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490232952   92 AGAILQTHISSVVFGAWDSKLGACGSVWDILrDPHIGSHpQVfgSVCESQCVQLLRNFF 150
Cdd:pfam14437  86 AGAIVQAGLKSLVYGAGNPKGGAVGSVLNKL-VIVLWNH-RV--ELVEEDCSEILKGFF 140
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 12-154 4.27e-41

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 135.32  E-value: 4.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEVPVGAVVVDGsGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPMC 91
Cdd:PRK10860  17 MRHALTLAKRAWDEREVPVGAVLVHN-NRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCVMC 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490232952  92 AGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIGSHPQVFGSVCESQCVQLLRNFFENHR 154
Cdd:PRK10860  96 AGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRR 158
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
11-106 6.96e-36

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 119.71  E-value: 6.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952   11 LMQEALRLAQVAADCGEVPVGAVVVDGSGAIIGRGSNLREQDADPLSHAEILAIRQAADVRKSWNLSDCTLVVTLEPCPM 90
Cdd:pfam00383   5 FMRLALKAAKRAYPYSNFPVGAVIVKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEPCGM 84

                          90
                  ....*....|....*.
gi 490232952   91 CAGAILQTHISSVVFG 106
Cdd:pfam00383  85 CAQAIIESGIKRVVFG 100
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 12-124 2.15e-19

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: 78.05  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAAdcGEV----PVGAVVVDGSGAIIGRGSNLReqdaDPLSHAEILAIRQAADVRkswnLSDCTLVVTLEP 87
Cdd:cd01284    1 MRRALELAEKGR--GLTspnpPVGCVIVDDDGEIVGEGYHRK----AGGPHAEVNALASAGEKL----ARGATLYVTLEP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490232952  88 C------PMCAGAILQTHISSVVFGAWDSKLGACGSVWDILRD 124
Cdd:cd01284   71 CshhgktPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRA 113
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 12-154 5.26e-19

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: 81.26  E-value: 5.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAAdcGEV----PVGAVVVDGsGAIIGRGsnlREQDAD-PlsHAEILAIRQAADvrkswNLSDCTLVVTLE 86
Cdd:COG0117    4 MRRALELARRGL--GTTspnpLVGCVIVKD-GRIVGEG---YHQRAGgP--HAEVNALAQAGE-----AARGATLYVTLE 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490232952  87 PC------PMCAGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIgshpQVFGSVCESQCVQLLRNFFENHR 154
Cdd:COG0117   71 PCshhgrtPPCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGI----EVEVGVLEEEARALNRGFLKRMR 140
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 12-149 1.23e-14

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: 69.47  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952   12 MQEALRLAQVAADCGEV--PVGAVVVDGsGAIIGRGSNLREQdadpLSHAEILAIRQAADvrkswNLSDCTLVVTLEPC- 88
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPnpLVGCVIVKN-GEIVGEGAHQKAG----EPHAEVHALRQAGE-----NAKGATAYVTLEPCs 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490232952   89 -----PMCAGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIgshpQVFGSVCESQCVQLLRNF 149
Cdd:TIGR00326  71 hqgrtPPCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGF 132
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 12-105 2.16e-13

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: 62.18  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLA-QVAADCGEVPVGAVVV-DGSGAIIGRGSNLREQDADPLSHAEILAIRQAAdvrKSWNLSDCTLVVTLEPCP 89
Cdd:cd00786    1 MTEALKAAdLGYAKESNFQVGACLVnKKDGGKVGRGCNIENAAYSMCNHAERTALFNAG---SEGDTKGQMLYVALSPCG 77

                         90
                 ....*....|....*.
gi 490232952  90 MCAGAILQTHISSVVF 105
Cdd:cd00786   78 ACAQLIIELGIKDVIV 93
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 16-105 6.96e-12

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: 58.83  E-value: 6.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  16 LRLAQVAA---DCGEVPVGAVVVDgSGAIIGRGSN------------LREQDADPLS---------HAEILAIRQAAdvR 71
Cdd:cd01286    5 MAIARLAAlrsTCPRRQVGAVIVK-DKRIISTGYNgspsglphcaevGCERDDLPSGedqkccrtvHAEQNAILQAA--R 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490232952  72 KSWNLSDCTLVVTLEPCPMCAGAILQTHISSVVF 105
Cdd:cd01286   82 HGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
30-105 4.84e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 51.77  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  30 VGAVVV-DGSgaIIGRGSN--------------LREQDADPLS---------HAEILAIRQAAdvRKSWNLSDCTLVVTL 85
Cdd:COG2131   30 VGAVIVkDKR--ILATGYNgapsglphcdevgcLREKLGIPSGergeccrtvHAEQNAILQAA--RHGVSTEGATLYVTH 105

                         90       100
                 ....*....|....*....|
gi 490232952  86 EPCPMCAGAILQTHISSVVF 105
Cdd:COG2131  106 FPCLECAKMIIQAGIKRVVY 125
cd PHA02588
deoxycytidylate deaminase; Provisional
 12-112 2.50e-07

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 47.44  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQvAADCGEVPVGAVVVDGsGAIIGRGSN------------------------LREQDADPLS--------HA 59
Cdd:PHA02588   7 LQIAYLVSQ-ESKCVSWKVGAVIEKN-GRIISTGYNgtpaggvnccdhaneqgwlddegkLKKEHRPEHSawsskneiHA 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490232952  60 EILAIRQAAdvRKSWNLSDCTLVVTLEPCPMCAGAILQTHISSVVFGA--------WDSKL 112
Cdd:PHA02588  85 ELNAILFAA--RNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEkydrngpgWDDIL 143
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 12-154 1.52e-06

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 46.30  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  12 MQEALRLAQVAADCGEvP---VGAVVVDgSGAIIGRGsnLREQDADPlsHAEILAIRQAADVRKswnlsDCTLVVTLEPC 88
Cdd:PLN02807  36 MRRCVELARKAIGCTS-PnpmVGCVIVK-DGRIVGEG--FHPKAGQP--HAEVFALRDAGDLAE-----NATAYVSLEPC 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490232952  89 ------PMCAGAILQTHISSVVFGAWDSKLGACGSVWDILRDPHIgshpQVFGSVCESQCVQLLRNFFenHR 154
Cdd:PLN02807 105 nhygrtPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGI----EVTVGVEEELCRKLNEAFI--HR 170
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 30-104 3.70e-06

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 45.14  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490232952  30 VGAVVVDGsGAIIGRGSNLREQDAdplsHAEILAIRQAADVRKSwnlsdCTLVVTLEPC------PMCAGAILQTHISSV 103
Cdd:PRK10786  27 VGCVIVKD-GEIVGEGYHQRAGEP----HAEVHALRMAGEKAKG-----ATAYVTLEPCshhgrtPPCCDALIAAGVARV 96


                 .
gi 490232952 104 V 104
Cdd:PRK10786  97 V 97
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 29-95 2.24e-04

Cytidine deaminase zinc-binding domain. These enzymes 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. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes.


Pssm-ID: 238610 [Multi-domain]  Cd Length: 112  Bit Score: 38.48  E-value: 2.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490232952  29 PVGAVVVDGSGAIIgRGSNLrEQDADPLS-HAEILAIRQAAD-----VRKSWNLSDCTLVVTlePCPMCAGAI 95
Cdd:cd01283   19 TVGAALLTKDGRIF-TGVNV-ENASYGLTlCAERTAIGKAVSeglrrYLVTWAVSDEGGVWS--PCGACRQVL 87
 
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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