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Conserved domains on  [gi|2059018177|emb|CAG7487362|]
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cytidine/deoxycytidylate deaminase [Streptococcus pneumoniae]

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 ...
 5-152 7.90e-74

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: 217.29  E-value: 7.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   5 LEEKEVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTI 84
Cdd:COG0590     1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059018177  85 EPCVMCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEIGILEDKCAAIMQDFFRNR 152
Cdd:COG0590    81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-152 7.90e-74

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: 217.29  E-value: 7.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   5 LEEKEVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTI 84
Cdd:COG0590     1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059018177  85 EPCVMCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEIGILEDKCAAIMQDFFRNR 152
Cdd:COG0590    81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 9-155 2.02e-48

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 153.81  E-value: 2.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   9 EVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIEPCV 88
Cdd:PRK10860   14 EYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCV 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059018177  89 MCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEIGILEDKCAAIMQDFFRNRRKK 155
Cdd:PRK10860   94 MCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQE 160
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 6-153 1.27e-45

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: 145.74  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   6 EEKEVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIE 85
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059018177  86 PCVMCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEigilEDKCAAIMQDFFRNRR 153
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 12-119 2.24e-45

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: 143.91  E-value: 2.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  12 MREALREAEIALEHDEIPIGCVIV-KDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIEPCVMC 90
Cdd:cd01285     1 MRLAIELARKALAEGEVPFGAVIVdDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                          90       100
                  ....*....|....*....|....*....
gi 2059018177  91 SGAIGLARIPNVVYGAKNQKFGAAGSLYD 119
Cdd:cd01285    81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 12-153 3.11e-17

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: 76.79  E-value: 3.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  12 MREALREAE--IALEHDEIPIGCVIVKDGEIIGRGHNareeLQRAVMHAEIMAIEDANLSEEswrllDCTLFVTIEPCVM 89
Cdd:TIGR00326   1 MNRALDLAKkgQGTTHPNPLVGCVIVKNGEIVGEGAH----QKAGEPHAEVHALRQAGENAK-----GATAYVTLEPCSH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2059018177  90 ------CSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLnhrvEVEIGILEDKCAAIMQDF-FRNRR 153
Cdd:TIGR00326  72 qgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGFlKRMRT 138
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-152 7.90e-74

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: 217.29  E-value: 7.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   5 LEEKEVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTI 84
Cdd:COG0590     1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059018177  85 EPCVMCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEIGILEDKCAAIMQDFFRNR 152
Cdd:COG0590    81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 9-155 2.02e-48

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 153.81  E-value: 2.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   9 EVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIEPCV 88
Cdd:PRK10860   14 EYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCV 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059018177  89 MCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEIGILEDKCAAIMQDFFRNRRKK 155
Cdd:PRK10860   94 MCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQE 160
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 6-153 1.27e-45

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: 145.74  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   6 EEKEVFMREALREAEIALEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIE 85
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059018177  86 PCVMCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEigilEDKCAAIMQDFFRNRR 153
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 12-119 2.24e-45

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: 143.91  E-value: 2.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  12 MREALREAEIALEHDEIPIGCVIV-KDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIEPCVMC 90
Cdd:cd01285     1 MRLAIELARKALAEGEVPFGAVIVdDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                          90       100
                  ....*....|....*....|....*....
gi 2059018177  91 SGAIGLARIPNVVYGAKNQKFGAAGSLYD 119
Cdd:cd01285    81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-105 1.04e-32

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 111.62  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   9 EVFMREALREAEIALEHDEIPIGCVIVK-DGEIIGRGHNAREELQRAVMHAEIMAIEDANLSEESWRLLDCTLFVTIEPC 87
Cdd:pfam00383   3 EYFMRLALKAAKRAYPYSNFPVGAVIVKkDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEPC 82

                          90
                  ....*....|....*...
gi 2059018177  88 VMCSGAIGLARIPNVVYG 105
Cdd:pfam00383  83 GMCAQAIIESGIKRVVFG 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 9-155 1.81e-23

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: 93.20  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   9 EVFMREALREAEIALEHDEI--PIGCVIVKDGEIIGRGHNAR--EElqravmHAEIMAIEDANLseeswRLLDCTLFVTI 84
Cdd:COG0117     1 ERYMRRALELARRGLGTTSPnpLVGCVIVKDGRIVGEGYHQRagGP------HAEVNALAQAGE-----AARGATLYVTL 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2059018177  85 EPCVM------CSGAIGLARIPNVVYGAK--NQKfgAAGSLYDILTDerlnHRVEVEIGILEDKCAAIMQDFFRNRRKK 155
Cdd:COG0117    70 EPCSHhgrtppCADALIEAGIKRVVIAMLdpNPL--VAGKGIARLRA----AGIEVEVGVLEEEARALNRGFLKRMRTG 142
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 12-153 3.11e-17

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: 76.79  E-value: 3.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  12 MREALREAE--IALEHDEIPIGCVIVKDGEIIGRGHNareeLQRAVMHAEIMAIEDANLSEEswrllDCTLFVTIEPCVM 89
Cdd:TIGR00326   1 MNRALDLAKkgQGTTHPNPLVGCVIVKNGEIVGEGAH----QKAGEPHAEVHALRQAGENAK-----GATAYVTLEPCSH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2059018177  90 ------CSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLnhrvEVEIGILEDKCAAIMQDF-FRNRR 153
Cdd:TIGR00326  72 qgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGFlKRMRT 138
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 12-123 1.02e-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: 66.10  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  12 MREALREAEIALEHDEI--PIGCVIVKD-GEIIGRGHnareeLQRAVM-HAEIMAIEDAnlseESWRLLDCTLFVTIEPC 87
Cdd:cd01284     1 MRRALELAEKGRGLTSPnpPVGCVIVDDdGEIVGEGY-----HRKAGGpHAEVNALASA----GEKLARGATLYVTLEPC 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2059018177  88 ------VMCSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTD 123
Cdd:cd01284    72 shhgktPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRA 113
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 12-103 5.62e-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: 61.03  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  12 MREALREAEIALEHD-EIPIGCVIV--KDGEIIGRGHNAREELQRAVMHAEIMAIEDANlSEESWRllDCTLFVTIEPCV 88
Cdd:cd00786     1 MTEALKAADLGYAKEsNFQVGACLVnkKDGGKVGRGCNIENAAYSMCNHAERTALFNAG-SEGDTK--GQMLYVALSPCG 77

                          90
                  ....*....|....*
gi 2059018177  89 MCSGAIGLARIPNVV 103
Cdd:cd00786    78 ACAQLIIELGIKDVI 92
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 11-149 2.34e-10

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 57.48  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  11 FMREALREAEIALEHDEiP---IGCVIVKDGEIIGRGHNAREelqrAVMHAEIMAIEDA-NLSEESwrlldcTLFVTIEP 86
Cdd:PLN02807   35 YMRRCVELARKAIGCTS-PnpmVGCVIVKDGRIVGEGFHPKA----GQPHAEVFALRDAgDLAENA------TAYVSLEP 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2059018177  87 CVM------CSGAIGLARIPNVVYGAKNQKFGAAGSLYDILTDERLNHRVEVEigilEDKCAAIMQDFF 149
Cdd:PLN02807  104 CNHygrtppCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVE----EELCRKLNEAFI 168
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 31-104 2.64e-10

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: 54.97  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  31 GCVIVKDGEIIGRGHN----------------------AREELQRAVmHAEIMAIedANLSEESWRLLDCTLFVTIEPCV 88
Cdd:cd01286    23 GAVIVKDKRIISTGYNgspsglphcaevgcerddlpsgEDQKCCRTV-HAEQNAI--LQAARHGVSLEGATLYVTLFPCI 99

                          90
                  ....*....|....*.
gi 2059018177  89 MCSGAIGLARIPNVVY 104
Cdd:cd01286   100 ECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
30-104 1.18e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 53.69  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  30 IGCVIVKDGEIIGRGHN------------------------AREELQRAVmHAEIMAIEDANLSEESwrLLDCTLFVTIE 85
Cdd:COG2131    30 VGAVIVKDKRILATGYNgapsglphcdevgclreklgipsgERGECCRTV-HAEQNAILQAARHGVS--TEGATLYVTHF 106

                          90
                  ....*....|....*....
gi 2059018177  86 PCVMCSGAIGLARIPNVVY 104
Cdd:COG2131   107 PCLECAKMIIQAGIKRVVY 125
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 9-153 1.64e-08

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 52.08  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177   9 EVFMREALREAEIA--LEHDEIPIGCVIVKDGEIIGRGHNAREELQRAVMHAEIMAIEDANLSeeswrlldcTLFVTIEP 86
Cdd:PRK10786    4 EFYMARALKLAQRGrfTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGA---------TAYVTLEP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2059018177  87 CVM------CSGAIGLARIPNVVYGAKNQKFGAAG-SLYdiltdeRLNHR-VEVEIGILEDKCAAIMQDFFRNRR 153
Cdd:PRK10786   75 CSHhgrtppCCDALIAAGVARVVAAMQDPNPQVAGrGLY------RLQQAgIDVSHGLMMSEAEALNKGFLKRMR 143
cd PHA02588
deoxycytidylate deaminase; Provisional
 30-107 3.10e-05

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 41.67  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059018177  30 IGCVIVKDGEIIGRGHN------------AREEL--------------------QRAVMHAEIMAIEDANLSEESwrLLD 77
Cdd:PHA02588   24 VGAVIEKNGRIISTGYNgtpaggvnccdhANEQGwlddegklkkehrpehsawsSKNEIHAELNAILFAARNGIS--IEG 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 2059018177  78 CTLFVTIEPCVMCSGAIGLARIPNVVYGAK 107
Cdd:PHA02588  102 ATMYVTASPCPDCAKAIAQSGIKKLVYCEK 131
 
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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