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Conserved domains on  [gi|2447758272|ref|WP_274379357|]
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MULTISPECIES: tRNA adenosine(34) deaminase TadA [Bacteria]

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 ...
 7-155 2.19e-76

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: 224.23  E-value: 2.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   7 DNEEHWMRHAFALADRAEREfDEIPVGAVLVsPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVT 86
Cdd:COG0590     2 EDDEEFMRRALELARKAVAE-GEVPVGAVLV-KDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  87 LEPCAMCAMALVHARVARVVYGASDPKTGACGSVFDLVADPRHNHRIEVIGGVLGDEAGRRLTNYFRAK 155
Cdd:COG0590    80 LEPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 7-155 2.19e-76

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: 224.23  E-value: 2.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   7 DNEEHWMRHAFALADRAEREfDEIPVGAVLVsPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVT 86
Cdd:COG0590     2 EDDEEFMRRALELARKAVAE-GEVPVGAVLV-KDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  87 LEPCAMCAMALVHARVARVVYGASDPKTGACGSVFDLVADPRHNHRIEVIGGVLGDEAGRRLTNYFRAK 155
Cdd:COG0590    80 LEPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 8-156 3.28e-67

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 201.96  E-value: 3.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   8 NEEHWMRHAFALADRAEREfDEIPVGAVLVSpEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTL 87
Cdd:PRK10860   12 SHEYWMRHALTLAKRAWDE-REVPVGAVLVH-NNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTL 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  88 EPCAMCAMALVHARVARVVYGASDPKTGACGSVFDLVADPRHNHRIEVIGGVLGDEAGRRLTNYFRAKR 156
Cdd:PRK10860   90 EPCVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRR 158
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 13-122 6.56e-49

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: 153.16  E-value: 6.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  13 MRHAFALADRAeREFDEIPVGAVLVSPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTLEPCAM 92
Cdd:cd01285     1 MRLAIELARKA-LAEGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPM 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2447758272  93 CAMALVHARVARVVYGASDPKTGACGSVFD 122
Cdd:cd01285    80 CAGALLWARIKRVVYGASDPKLGGIGFLIE 109
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-108 4.18e-35

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 117.79  E-value: 4.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  10 EHWMRHAFALADRAeREFDEIPVGAVLVSPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTLEP 89
Cdd:pfam00383   3 EYFMRLALKAAKRA-YPYSNFPVGAVIVKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEP 81

                          90
                  ....*....|....*....
gi 2447758272  90 CAMCAMALVHARVARVVYG 108
Cdd:pfam00383  82 CGMCAQAIIESGIKRVVFG 100
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 13-161 7.29e-19

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: 81.41  E-value: 7.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  13 MRHAFALADRAEREFDEIP-VGAVLVSpEGQVLGEGWnrnildHDPS--AHAEIVAMREAGRvlgnhRLVGCTLYVTLEP 89
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPlVGCVIVK-NGEIVGEGA------HQKAgePHAEVHALRQAGE-----NAKGATAYVTLEP 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  90 CAM------CAMALVHARVARVVYGASDPKTGACGSVFDLVADprhnHRIEVIGGVLGDEAGRRLTNY-FRAKRGRPLV 161
Cdd:TIGR00326  69 CSHqgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQ----AGIEVTFGILKEEAERLNKGFlKRMRTGLPYV 143
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 7-155 2.19e-76

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: 224.23  E-value: 2.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   7 DNEEHWMRHAFALADRAEREfDEIPVGAVLVsPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVT 86
Cdd:COG0590     2 EDDEEFMRRALELARKAVAE-GEVPVGAVLV-KDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  87 LEPCAMCAMALVHARVARVVYGASDPKTGACGSVFDLVADPRHNHRIEVIGGVLGDEAGRRLTNYFRAK 155
Cdd:COG0590    80 LEPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 8-156 3.28e-67

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 201.96  E-value: 3.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   8 NEEHWMRHAFALADRAEREfDEIPVGAVLVSpEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTL 87
Cdd:PRK10860   12 SHEYWMRHALTLAKRAWDE-REVPVGAVLVH-NNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTL 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  88 EPCAMCAMALVHARVARVVYGASDPKTGACGSVFDLVADPRHNHRIEVIGGVLGDEAGRRLTNYFRAKR 156
Cdd:PRK10860   90 EPCVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRR 158
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 13-122 6.56e-49

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: 153.16  E-value: 6.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  13 MRHAFALADRAeREFDEIPVGAVLVSPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTLEPCAM 92
Cdd:cd01285     1 MRLAIELARKA-LAEGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPM 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2447758272  93 CAMALVHARVARVVYGASDPKTGACGSVFD 122
Cdd:cd01285    80 CAGALLWARIKRVVYGASDPKLGGIGFLIE 109
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-108 4.18e-35

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 117.79  E-value: 4.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  10 EHWMRHAFALADRAeREFDEIPVGAVLVSPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTLEP 89
Cdd:pfam00383   3 EYFMRLALKAAKRA-YPYSNFPVGAVIVKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEP 81

                          90
                  ....*....|....*....
gi 2447758272  90 CAMCAMALVHARVARVVYG 108
Cdd:pfam00383  82 CGMCAQAIIESGIKRVVFG 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 8-156 4.30e-35

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: 119.55  E-value: 4.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   8 NEEHWMRHAFALADRAErEFDEIPVGAVLVSpEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHRLVGCTLYVTL 87
Cdd:pfam14437   2 NHEKWFRKALGLAEKAY-DAGEVPIGAVIVK-DGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  88 EPCAMCAMALVHARVARVVYGASDPKTGACGSVFDLVADPRHNHRIEVIggvlGDEAGRRLTNYFRAKR 156
Cdd:pfam14437  80 EPCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 10-161 1.47e-28

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: 107.07  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  10 EHWMRHAFALADRAEREFDEIP-VGAVLVSpEGQVLGEGWnrnildHDP--SAHAEIVAMREAGrvlgnHRLVGCTLYVT 86
Cdd:COG0117     1 ERYMRRALELARRGLGTTSPNPlVGCVIVK-DGRIVGEGY------HQRagGPHAEVNALAQAG-----EAARGATLYVT 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  87 LEPCAM------CAMALVHARVARVVYGASDPKTGACGSVFDLVADprhnHRIEVIGGVLGDEAgRRLTNYF--RAKRGR 158
Cdd:COG0117    69 LEPCSHhgrtppCADALIEAGIKRVVIAMLDPNPLVAGKGIARLRA----AGIEVEVGVLEEEA-RALNRGFlkRMRTGR 143


                  ...
gi 2447758272 159 PLV 161
Cdd:COG0117   144 PFV 146
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 13-119 1.40e-21

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: 83.82  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  13 MRHAFALADRAEREFDEIP-VGAVLVSPEGQVLGEGWNRNIldhdPSAHAEIVAMREAGRVlgnhRLVGCTLYVTLEPCA 91
Cdd:cd01284     1 MRRALELAEKGRGLTSPNPpVGCVIVDDDGEIVGEGYHRKA----GGPHAEVNALASAGEK----LARGATLYVTLEPCS 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2447758272  92 M------CAMALVHARVARVVYGASDPKTGACGS 119
Cdd:cd01284    73 HhgktppCVDAIIEAGIKRVVVGVRDPNPLVAGK 106
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 13-161 7.29e-19

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: 81.41  E-value: 7.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  13 MRHAFALADRAEREFDEIP-VGAVLVSpEGQVLGEGWnrnildHDPS--AHAEIVAMREAGRvlgnhRLVGCTLYVTLEP 89
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPlVGCVIVK-NGEIVGEGA------HQKAgePHAEVHALRQAGE-----NAKGATAYVTLEP 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2447758272  90 CAM------CAMALVHARVARVVYGASDPKTGACGSVFDLVADprhnHRIEVIGGVLGDEAGRRLTNY-FRAKRGRPLV 161
Cdd:TIGR00326  69 CSHqgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQ----AGIEVTFGILKEEAERLNKGFlKRMRTGLPYV 143
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 13-106 9.37e-14

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: 63.34  E-value: 9.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  13 MRHAFALADRAEREFDEIPVGAVLV-SPEGQVLGEGWNRNILDHDPSAHAEIVAMREAGRVLGNHrlvGCTLYVTLEPCA 91
Cdd:cd00786     1 MTEALKAADLGYAKESNFQVGACLVnKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTK---GQMLYVALSPCG 77

                          90
                  ....*....|....*
gi 2447758272  92 MCAMALVHARVARVV 106
Cdd:cd00786    78 ACAQLIIELGIKDVI 92
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 7-161 2.17e-13

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 66.33  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   7 DNEEHWMRHAFALADRAEREFDEIP-VGAVLVSpEGQVLGEGWNrnildhdPSA---HAEIVAMREAGRVLGNhrlvgCT 82
Cdd:PLN02807   30 DDDSFYMRRCVELARKAIGCTSPNPmVGCVIVK-DGRIVGEGFH-------PKAgqpHAEVFALRDAGDLAEN-----AT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  83 LYVTLEPCAM------CAMALVHARVARVVYGASDPKTGACGSVFDLVADPrhnhRIEVIGGVlGDEAGRRLTNYF--RA 154
Cdd:PLN02807   97 AYVSLEPCNHygrtppCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDA----GIEVTVGV-EEELCRKLNEAFihRM 171


                  ....*..
gi 2447758272 155 KRGRPLV 161
Cdd:PLN02807  172 LTGKPFV 178
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-107 5.09e-13

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: 62.29  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  10 EHWMRHAFALADRAE---RefdeiPVGAVLVSpEGQVLGEGWN------RNILDHDP---------------SAHAEIVA 65
Cdd:cd01286     2 EYFMAIARLAALRSTcprR-----QVGAVIVK-DKRIISTGYNgspsglPHCAEVGCerddlpsgedqkccrTVHAEQNA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2447758272  66 MREAGRVlgNHRLVGCTLYVTLEPCAMCAMALVHARVARVVY 107
Cdd:cd01286    76 ILQAARH--GVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
9-107 3.98e-12

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 60.24  E-value: 3.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   9 EEHWMRHAFALADRAE---RefdeiPVGAVLVsPEGQVLGEGWN------------------RNILDHDP-----SAHAE 62
Cdd:COG2131     9 DEYFMEIAKLVALRSTclrR-----QVGAVIV-KDKRILATGYNgapsglphcdevgclrekLGIPSGERgeccrTVHAE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2447758272  63 IVAMREAGRvLGNhRLVGCTLYVTLEPCAMCAMALVHARVARVVY 107
Cdd:COG2131    83 QNAILQAAR-HGV-STEGATLYVTHFPCLECAKMIIQAGIKRVVY 125
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 7-112 4.43e-12

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 62.48  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272   7 DNEEHWMRHAFALADRAEreFDEIP---VGAVLVSpEGQVLGEGWNRnildHDPSAHAEIVAMREAGrvlgnHRLVGCTL 83
Cdd:PRK10786    1 MQDEFYMARALKLAQRGR--FTTHPnpnVGCVIVK-DGEIVGEGYHQ----RAGEPHAEVHALRMAG-----EKAKGATA 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2447758272  84 YVTLEPCAM------CAMALVHARVARVVYGASDP 112
Cdd:PRK10786   69 YVTLEPCSHhgrtppCCDALIAAGVARVVAAMQDP 103
Bd3614-deam pfam14439
Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 32-112 2.02e-07

Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Bdellovibrio Bd3614. They are typified by a distinct N-terminal globular domain. The Bdellovibrio version occurs in a predicted operon with a 23S rRNA G2445-modifying methylase suggesting that it might be involved in RNA editing.


Pssm-ID: 405177 [Multi-domain]  Cd Length: 113  Bit Score: 47.13  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447758272  32 VGAVLVSPEGQVLGEGWNRNilDHDPSAHAEI-----VAMREAGRVLGNhrlvGCTLYVTLEPCAMCAMALVHARVA--- 103
Cdd:pfam14439  10 VVAALVSPQGQLLDAAVNTN--AKNKTLHAEVnllqpLLRETARRPIPP----GARLLVTLQCCKMCAALVCAACDDpgq 83

                          90
                  ....*....|
gi 2447758272 104 -RVVYGASDP 112
Cdd:pfam14439  84 lKVVYLVEDP 93
cd PHA02588
deoxycytidylate deaminase; Provisional
 60-108 5.26e-05

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 41.28  E-value: 5.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2447758272  60 HAEIVAMREAGRvlGNHRLVGCTLYVTLEPCAMCAMALVHARVARVVYG 108
Cdd:PHA02588   83 HAELNAILFAAR--NGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC 129
 
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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