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Conserved domains on  [gi|446102432|ref|WP_000180287|]
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tRNA adenosine(34) deaminase TadA [Staphylococcus aureus]

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 ...
1-148 4.78e-83

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: 240.79  E-value: 4.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   1 MTNDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTL 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446102432  81 EPCVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRAIVDKGVLKEACSTLLTTFFKNL 148
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 ...
1-148 4.78e-83

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: 240.79  E-value: 4.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   1 MTNDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTL 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446102432  81 EPCVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRAIVDKGVLKEACSTLLTTFFKNL 148
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
3-149 7.18e-54

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: 166.93  E-value: 7.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432    3 NDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLEP 82
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEP 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446102432   83 CVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRaivdKGVLKEACSTLLTTFFKNLR 149
Cdd:pfam14437  82 CPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHR----VELVEEDCSEILKGFFKKLR 144
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
3-154 2.34e-52

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 163.82  E-value: 2.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   3 NDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLEP 82
Cdd:PRK10860  12 SHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEP 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446102432  83 CVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRAIVDKGVLKEACSTLLTTFFKNLRANKKS 154
Cdd:PRK10860  92 CVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKA 163
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
8-115 1.20e-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: 160.09  E-value: 1.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   8 MTLAIEEAKKAARLGEVPIGAVITKGD-EVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLEPCVMC 86
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80
                         90       100
                 ....*....|....*....|....*....
gi 446102432  87 AGTIVMSRIPRVVYGADDPKGGCSGSLMN 115
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
8-149 1.15e-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: 77.95  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432    8 MTLAIEEAKKAARLGEV--PIGAVITKGDEVIARAHNLRETLqqptAHAEHIAIERAAKvlgswRLEGCTLYVTLEPCVM 85
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPnpLVGCVIVKNGEIVGEGAHQKAGE----PHAEVHALRQAGE-----NAKGATAYVTLEPCSH 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   86 ------CAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNhraiVDKGVLKEACSTLLTTFFKNLR 149
Cdd:TIGR00326  72 qgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIE----VTFGILKEEAERLNKGFLKRMR 137
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
1-148 4.78e-83

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: 240.79  E-value: 4.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   1 MTNDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTL 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446102432  81 EPCVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRAIVDKGVLKEACSTLLTTFFKNL 148
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
3-149 7.18e-54

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: 166.93  E-value: 7.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432    3 NDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLEP 82
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEP 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446102432   83 CVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRaivdKGVLKEACSTLLTTFFKNLR 149
Cdd:pfam14437  82 CPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHR----VELVEEDCSEILKGFFKKLR 144
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
3-154 2.34e-52

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 163.82  E-value: 2.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   3 NDIYFMTLAIEEAKKAARLGEVPIGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLEP 82
Cdd:PRK10860  12 SHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEP 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446102432  83 CVMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNHRAIVDKGVLKEACSTLLTTFFKNLRANKKS 154
Cdd:PRK10860  92 CVMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKA 163
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
8-115 1.20e-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: 160.09  E-value: 1.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   8 MTLAIEEAKKAARLGEVPIGAVITKGD-EVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLEPCVMC 86
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80
                         90       100
                 ....*....|....*....|....*....
gi 446102432  87 AGTIVMSRIPRVVYGADDPKGGCSGSLMN 115
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
3-101 1.77e-36

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 121.25  E-value: 1.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432    3 NDIYFMTLAIEEAKKAARLGEVPIGAVI-TKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSWRLEGCTLYVTLE 81
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVGAVIvKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLE 80
                          90       100
                  ....*....|....*....|
gi 446102432   82 PCVMCAGTIVMSRIPRVVYG 101
Cdd:pfam00383  81 PCGMCAQAIIESGIKRVVFG 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
6-149 2.00e-21

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: 87.81  E-value: 2.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   6 YFMTLAIEEAKKAarLGEV----PIGAVITKGDEVIARAHnlreTLQQPTAHAEHIAIERAAKvlgswRLEGCTLYVTLE 81
Cdd:COG0117    2 RYMRRALELARRG--LGTTspnpLVGCVIVKDGRIVGEGY----HQRAGGPHAEVNALAQAGE-----AARGATLYVTLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432  82 PCVM------CAGTIVMSRIPRVVYGADDP------KGgcsgslMNLLQQSNfnhraI-VDKGVLKEACSTLLTTFFKNL 148
Cdd:COG0117   71 PCSHhgrtppCADALIEAGIKRVVIAMLDPnplvagKG------IARLRAAG-----IeVEVGVLEEEARALNRGFLKRM 139

                 .
gi 446102432 149 R 149
Cdd:COG0117  140 R 140
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
8-119 1.63e-18

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: 75.73  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   8 MTLAIEEAKKAArlGEV----PIGAVITKGD-EVIARAHnlreTLQQPTAHAEHIAIERAAKVlgswRLEGCTLYVTLEP 82
Cdd:cd01284    1 MRRALELAEKGR--GLTspnpPVGCVIVDDDgEIVGEGY----HRKAGGPHAEVNALASAGEK----LARGATLYVTLEP 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446102432  83 C------VMCAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQ 119
Cdd:cd01284   71 CshhgktPPCVDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRA 113
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
8-149 1.15e-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: 77.95  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432    8 MTLAIEEAKKAARLGEV--PIGAVITKGDEVIARAHNLRETLqqptAHAEHIAIERAAKvlgswRLEGCTLYVTLEPCVM 85
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPnpLVGCVIVKNGEIVGEGAHQKAGE----PHAEVHALRQAGE-----NAKGATAYVTLEPCSH 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   86 ------CAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNhraiVDKGVLKEACSTLLTTFFKNLR 149
Cdd:TIGR00326  72 qgrtppCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIE----VTFGILKEEAERLNKGFLKRMR 137
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
4-106 3.89e-17

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 73.34  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   4 DIYFMTLAIEEAKKAA--RLgevPIGAVITKGDEVIARAHN--------------LRETLQQP---------TAHAEHIA 58
Cdd:COG2131    9 DEYFMEIAKLVALRSTclRR---QVGAVIVKDKRILATGYNgapsglphcdevgcLREKLGIPsgergeccrTVHAEQNA 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446102432  59 IERAAKVLGSwrLEGCTLYVTLEPCVMCAGTIVMSRIPRVVYGADDPK 106
Cdd:COG2131   86 ILQAARHGVS--TEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPD 131
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
8-99 1.86e-15

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: 67.58  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   8 MTLAIEEAKKA-ARLGEVPIGAVI--TKGDEVIARAHNLRETLQQPTAHAEHIAIERAAKVLGSwrlEGCTLYVTLEPCV 84
Cdd:cd00786    1 MTEALKAADLGyAKESNFQVGACLvnKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDT---KGQMLYVALSPCG 77
                         90
                 ....*....|....*
gi 446102432  85 MCAGTIVMSRIPRVV 99
Cdd:cd00786   78 ACAQLIIELGIKDVI 92
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
4-107 4.44e-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: 67.30  E-value: 4.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   4 DIYFMTLAIEEAKKAARLGeVPIGAVITKGDEVIARAHN--------------LRETLQQP-------TAHAEHIAIERA 62
Cdd:cd01286    1 DEYFMAIARLAALRSTCPR-RQVGAVIVKDKRIISTGYNgspsglphcaevgcERDDLPSGedqkccrTVHAEQNAILQA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446102432  63 AKVLGSwrLEGCTLYVTLEPCVMCAGTIVMSRIPRVVYGADDPKG 107
Cdd:cd01286   80 ARHGVS--LEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDD 122
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
2-149 6.27e-10

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 56.31  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   2 TNDIYFMTLAIEEAKKAaRLGEVP---IGAVITKGDEVIARAHNLRETLQQPTAHAEHIAIERAakvlgswrlEGCTLYV 78
Cdd:PRK10786   1 MQDEFYMARALKLAQRG-RFTTHPnpnVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKA---------KGATAYV 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446102432  79 TLEPCVM------CAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNhraiVDKGVLKEACSTLLTTFFKNLR 149
Cdd:PRK10786  71 TLEPCSHhgrtppCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGID----VSHGLMMSEAEALNKGFLKRMR 143
cd PHA02588
deoxycytidylate deaminase; Provisional
4-101 1.45e-08

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 50.91  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   4 DIYFMTLAIEEAKKAaRLGEVPIGAVITKGDEVIARAHN------------------------LRETLQQPTA------- 52
Cdd:PHA02588   3 DSTYLQIAYLVSQES-KCVSWKVGAVIEKNGRIISTGYNgtpaggvnccdhaneqgwlddegkLKKEHRPEHSawsskne 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446102432  53 -HAEHIAIERAAKVLGSwrLEGCTLYVTLEPCVMCAGTIVMSRIPRVVYG 101
Cdd:PHA02588  82 iHAELNAILFAARNGIS--IEGATMYVTASPCPDCAKAIAQSGIKKLVYC 129
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
4-145 1.63e-07

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 49.39  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432   4 DIYFMTLAIEEAKKAA-RLGEVPI-GAVITKGDEVIARAHNLRETlqQPtaHAEHIAIeRAAKVLGswrlEGCTLYVTLE 81
Cdd:PLN02807  32 DSFYMRRCVELARKAIgCTSPNPMvGCVIVKDGRIVGEGFHPKAG--QP--HAEVFAL-RDAGDLA----ENATAYVSLE 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102432  82 PCVM------CAGTIVMSRIPRVVYGADDPKGGCSGSLMNLLQQSNFNhraiVDKGVLKEACSTLLTTFF 145
Cdd:PLN02807 103 PCNHygrtppCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIE----VTVGVEEELCRKLNEAFI 168
Bd3614-deam pfam14439
Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
72-107 2.88e-04

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: 38.27  E-value: 2.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446102432   72 EGCTLYVTLEPCVMCAGTIV-----MSRIpRVVYGADDPKG 107
Cdd:pfam14439  56 PGARLLVTLQCCKMCAALVCaacddPGQL-KVVYLVEDPGG 95
 
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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