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Conserved domains on  [gi|495777593|ref|WP_008502172|]
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MULTISPECIES: tRNA adenosine(34) deaminase TadA [Enterobacter]

Protein Classification

tRNA-specific adenosine deaminase( domain architecture ID 10793491)

tRNA-specific adenosine deaminases generate inosine at the first position of their anticodon (position 34) of specific tRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 11-178 9.63e-125

tRNA-specific adenosine deaminase; Provisional


:

Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 347.95  E-value: 9.63e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  11 PLSNPEFSHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTT 90
Cdd:PRK10860   5 FLSEVEFSHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDAT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  91 LYVTLEPCVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKTIGGVLAPECSGLLSDFFRMRRQQKKQQ 170
Cdd:PRK10860  85 LYVTLEPCVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKAL 164


                 ....*...
gi 495777593 171 KAELKPTD 178
Cdd:PRK10860 165 KKAQRSTD 172
 
Name Accession Description Interval E-value
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 11-178 9.63e-125

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 347.95  E-value: 9.63e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  11 PLSNPEFSHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTT 90
Cdd:PRK10860   5 FLSEVEFSHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDAT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  91 LYVTLEPCVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKTIGGVLAPECSGLLSDFFRMRRQQKKQQ 170
Cdd:PRK10860  85 LYVTLEPCVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKAL 164


                 ....*...
gi 495777593 171 KAELKPTD 178
Cdd:PRK10860 165 KKAQRSTD 172
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 18-163 4.34e-87

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: 251.96  E-value: 4.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  18 SHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLEP 97
Cdd:COG0590    3 DDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777593  98 CVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKTIGGVLAPECSGLLSDFFRMR 163
Cdd:COG0590   83 CPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 23-128 1.55e-51

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: 160.48  E-value: 1.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  23 MRHALTLAQRAWDEGEVPVGAVLVHNN-QVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLEPCVMC 101
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|....*..
gi 495777593 102 SGAMVHSRIGTLVFGARDEKTGAAGSL 128
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFL 107
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 17-164 1.87e-43

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: 141.51  E-value: 1.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593   17 FSHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLE 96
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495777593   97 PCVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKtiggVLAPECSGLLSDFFRMRR 164
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVE----LVEEDCSEILKGFFKKLR 144
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 23-165 2.04e-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: 83.72  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593   23 MRHALTLAQRAW--DEGEVPVGAVLVHNNQVIGEGWNRPIGRhdptAHAEIMALRQGGlvlqnYRLLDTTLYVTLEPCVM 100
Cdd:TIGR00326   1 MNRALDLAKKGQgtTHPNPLVGCVIVKNGEIVGEGAHQKAGE----PHAEVHALRQAG-----ENAKGATAYVTLEPCSH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495777593  101 ------CSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVktigGVLAPECSGLLSDF-FRMRRQ 165
Cdd:TIGR00326  72 qgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTF----GILKEEAERLNKGFlKRMRTG 139
 
Name Accession Description Interval E-value
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 11-178 9.63e-125

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 347.95  E-value: 9.63e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  11 PLSNPEFSHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTT 90
Cdd:PRK10860   5 FLSEVEFSHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDAT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  91 LYVTLEPCVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKTIGGVLAPECSGLLSDFFRMRRQQKKQQ 170
Cdd:PRK10860  85 LYVTLEPCVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKAL 164


                 ....*...
gi 495777593 171 KAELKPTD 178
Cdd:PRK10860 165 KKAQRSTD 172
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 18-163 4.34e-87

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: 251.96  E-value: 4.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  18 SHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLEP 97
Cdd:COG0590    3 DDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777593  98 CVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKTIGGVLAPECSGLLSDFFRMR 163
Cdd:COG0590   83 CPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 23-128 1.55e-51

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: 160.48  E-value: 1.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  23 MRHALTLAQRAWDEGEVPVGAVLVHNN-QVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLEPCVMC 101
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|....*..
gi 495777593 102 SGAMVHSRIGTLVFGARDEKTGAAGSL 128
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFL 107
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 17-164 1.87e-43

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: 141.51  E-value: 1.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593   17 FSHEYWMRHALTLAQRAWDEGEVPVGAVLVHNNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLE 96
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495777593   97 PCVMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVKtiggVLAPECSGLLSDFFRMRR 164
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVE----LVEEDCSEILKGFFKKLR 144
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
19-116 2.60e-42

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 137.05  E-value: 2.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593   19 HEYWMRHALTLAQRAWDEGEVPVGAVLVH-NNQVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDTTLYVTLEP 97
Cdd:pfam00383   2 DEYFMRLALKAAKRAYPYSNFPVGAVIVKkDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEP 81

                          90
                  ....*....|....*....
gi 495777593   98 CVMCSGAMVHSRIGTLVFG 116
Cdd:pfam00383  82 CGMCAQAIIESGIKRVVFG 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 20-165 6.99e-29

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: 108.61  E-value: 6.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  20 EYWMRHALTLAQRAWdeGEV----PVGAVLVHNNQVIGEGWNRPIGRhdptAHAEIMALRQGGLvlqnyRLLDTTLYVTL 95
Cdd:COG0117    1 ERYMRRALELARRGL--GTTspnpLVGCVIVKDGRIVGEGYHQRAGG----PHAEVNALAQAGE-----AARGATLYVTL 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777593  96 EPCVM------CSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLghpgMNHQVKTIGGVLAPECSGLLSDFF-RMRRQ 165
Cdd:COG0117   70 EPCSHhgrtppCADALIEAGIKRVVIAMLDPNPLVAGKGIARL----RAAGIEVEVGVLEEEARALNRGFLkRMRTG 142
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 23-132 2.28e-20

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: 81.13  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  23 MRHALTLAQRAwdEGEV----PVGAVLVHNN-QVIGEGWNRPIGrhdpTAHAEIMALRQGGlvlqNYRLLDTTLYVTLEP 97
Cdd:cd01284    1 MRRALELAEKG--RGLTspnpPVGCVIVDDDgEIVGEGYHRKAG----GPHAEVNALASAG----EKLARGATLYVTLEP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495777593  98 C------VMCSGAMVHSRIGTLVFGARDEKTGAAGSLMDVL 132
Cdd:cd01284   71 CshhgktPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERL 111
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 23-165 2.04e-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: 83.72  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593   23 MRHALTLAQRAW--DEGEVPVGAVLVHNNQVIGEGWNRPIGRhdptAHAEIMALRQGGlvlqnYRLLDTTLYVTLEPCVM 100
Cdd:TIGR00326   1 MNRALDLAKKGQgtTHPNPLVGCVIVKNGEIVGEGAHQKAGE----PHAEVHALRQAG-----ENAKGATAYVTLEPCSH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495777593  101 ------CSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMNHQVktigGVLAPECSGLLSDF-FRMRRQ 165
Cdd:TIGR00326  72 qgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTF----GILKEEAERLNKGFlKRMRTG 139
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 19-115 6.99e-15

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: 67.68  E-value: 6.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  19 HEYWMRHALTLAQRAWDEGeVPVGAVLVHNNQVIGEGWN-RPIGRHDP--------------------TAHAEIMALRQG 77
Cdd:cd01286    1 DEYFMAIARLAALRSTCPR-RQVGAVIVKDKRIISTGYNgSPSGLPHCaevgcerddlpsgedqkccrTVHAEQNAILQA 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495777593  78 GLVlqNYRLLDTTLYVTLEPCVMCSGAMVHSRIGTLVF 115
Cdd:cd01286   80 ARH--GVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
19-115 6.68e-14

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 65.63  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  19 HEYWMRHALTLAQRAWDEGEvPVGAVLVHNNQVIGEGWNR-PIG--------------------RHDP--TAHAEIMAL- 74
Cdd:COG2131    9 DEYFMEIAKLVALRSTCLRR-QVGAVIVKDKRILATGYNGaPSGlphcdevgclreklgipsgeRGECcrTVHAEQNAIl 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 495777593  75 ---RQGGlvlqnyRLLDTTLYVTLEPCVMCSGAMVHSRIGTLVF 115
Cdd:COG2131   88 qaaRHGV------STEGATLYVTHFPCLECAKMIIQAGIKRVVY 125
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 23-115 1.08e-10

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: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  23 MRHALTLA-QRAWDEGEVPVGAVLVHNN--QVIGEGWNRPIGRHDPTAHAEIMALRQGGlVLQNYRllDTTLYVTLEPCV 99
Cdd:cd00786    1 MTEALKAAdLGYAKESNFQVGACLVNKKdgGKVGRGCNIENAAYSMCNHAERTALFNAG-SEGDTK--GQMLYVALSPCG 77

                         90
                 ....*....|....*.
gi 495777593 100 MCSGAMVHSRIGTLVF 115
Cdd:cd00786   78 ACAQLIIELGIKDVIV 93
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 21-138 1.06e-09

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 56.32  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  21 YWMRHALTLAQRAWDEGEvP---VGAVLVHNNQVIGEGWNRPIGRhdptAHAEIMALRQGGLVLQNyrlldTTLYVTLEP 97
Cdd:PLN02807  34 FYMRRCVELARKAIGCTS-PnpmVGCVIVKDGRIVGEGFHPKAGQ----PHAEVFALRDAGDLAEN-----ATAYVSLEP 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 495777593  98 CVM------CSGAMVHSRIGTLVFGARDEKTGAAGSLMDVLGHPGMN 138
Cdd:PLN02807 104 CNHygrtppCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIE 150
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 20-126 7.83e-08

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 50.92  E-value: 7.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777593  20 EYWMRHALTLAQRA-WDEGEVP-VGAVLVHNNQVIGEGWNRPIGRhdptAHAEIMALRQGGlvlqnYRLLDTTLYVTLEP 97
Cdd:PRK10786   4 EFYMARALKLAQRGrFTTHPNPnVGCVIVKDGEIVGEGYHQRAGE----PHAEVHALRMAG-----EKAKGATAYVTLEP 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495777593  98 CVM------CSGAMVHSRIGTLVFGARDEKTGAAG 126
Cdd:PRK10786  75 CSHhgrtppCCDALIAAGVARVVAAMQDPNPQVAG 109
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 62-107 5.39e-04

APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC-1 like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalyitc domain. More specifically, the catalytic domain is a zinc dependent deaminases domain and is essential for cytidine deamination.APOBEC-3 like members contain two copies of this domain. RNA editing by APOBEC-1 requires homodimerization and this complex interacts with RNA binding proteins to from the editosome (and references therein). This family also includes the functionally homologous activation induced deaminase (AID), which is essential for the development of antibody diversity in B lymphocytes, and the sea lamprey PmCDA1 and PmCDA2, which are predicted to play an AID-like role in the adaptive immune response of jawless vertebrates. Divergent members of this family are present in various eukaryotes such as Nematostella, C. elegans, Micromonas and Emiliania, and prokaryotes such as Wolbachia and Pseudomonas brassicacearum.


Pssm-ID: 462396 [Multi-domain]  Cd Length: 170  Bit Score: 38.89  E-value: 5.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 495777593   62 RHDPTAHAEIMALRQGGLVL----QNYRLldtTLYVTLEPCVMCSGAMVH 107
Cdd:pfam08210  41 QAASSLHAEERFLRWIHDLAldpgSNYEV---TWYVSWSPCNECASELAA 87
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 56-106 5.65e-03

Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases found only in sponges that often shows lineage-specific expansions.


Pssm-ID: 465854 [Multi-domain]  Cd Length: 116  Bit Score: 34.93  E-value: 5.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495777593   56 WNRPIGRHDPTAHAEIMALRQ-GGLVL---QNYRLldtTLYVTLEPCVMCSGAMV 106
Cdd:pfam18750  12 WQRGYLSNEHEQHAEICFLENiRSRELdpsQRYRV---TWYLSWSPCPECAQKIA 63
 
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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