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Conserved domains on  [gi|495617436|ref|WP_008342015|]
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MULTISPECIES: tRNA adenosine(34) deaminase TadA [Bacillus]

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 2.04e-82

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: 239.25  E-value: 2.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   1 MTKDEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTL 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495617436  81 EPCPMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIGGVLENECGELLSQFFRDL 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 2.04e-82

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: 239.25  E-value: 2.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   1 MTKDEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTL 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495617436  81 EPCPMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIGGVLENECGELLSQFFRDL 148
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 4-149 3.17e-51

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: 160.38  E-value: 3.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436    4 DEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLEPC 83
Cdd:pfam14437   3 HEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495617436   84 PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIggvlENECGELLSQFFRDLR 149
Cdd:pfam14437  83 PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 4-156 1.37e-49

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 156.89  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   4 DEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLEPC 83
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPC 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495617436  84 PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIGGVLENECGELLSQFFRDLRQRKKQAK 156
Cdd:PRK10860  93 VMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKALK 165
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 8-115 2.30e-48

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: 151.62  E-value: 2.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   8 MQEAISEALKAKQIGEVPIGAVIVVDD-QIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLEPCPMC 86
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|....*....
gi 495617436  87 AGAIVLSRVKKVVFGAYDPKGGCAGTLMN 115
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 8-150 3.15e-18

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: 79.49  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436    8 MQEAISEALKAKQIGEV--PIGAVIVVDDQIVSRAHNLRESEqrsiAHAELLAIDEACKmtgswRLEDAVLYVTLEPC-- 83
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPnpLVGCVIVKNGEIVGEGAHQKAGE----PHAEVHALRQAGE-----NAKGATAYVTLEPCsh 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495617436   84 ----PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFnhqsEVIGGVLENECGELLSQFFRDLRQ 150
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 ...
 1-148 2.04e-82

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: 239.25  E-value: 2.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   1 MTKDEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTL 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495617436  81 EPCPMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIGGVLENECGELLSQFFRDL 148
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAAR 148
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 4-149 3.17e-51

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: 160.38  E-value: 3.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436    4 DEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLEPC 83
Cdd:pfam14437   3 HEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495617436   84 PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIggvlENECGELLSQFFRDLR 149
Cdd:pfam14437  83 PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 4-156 1.37e-49

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 156.89  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   4 DEQFMQEAISEALKAKQIGEVPIGAVIVVDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLEPC 83
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPC 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495617436  84 PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFNHQSEVIGGVLENECGELLSQFFRDLRQRKKQAK 156
Cdd:PRK10860  93 VMCAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKALK 165
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 8-115 2.30e-48

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: 151.62  E-value: 2.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   8 MQEAISEALKAKQIGEVPIGAVIVVDD-QIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLEPCPMC 86
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|....*....
gi 495617436  87 AGAIVLSRVKKVVFGAYDPKGGCAGTLMN 115
Cdd:cd01285   81 AGALLWARIKRVVYGASDPKLGGIGFLIE 109
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
3-101 5.22e-39

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 127.80  E-value: 5.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436    3 KDEQFMQEAISEALKAKQIGEVPIGAVIV-VDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSWRLEDAVLYVTLE 81
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVGAVIVkKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLE 80

                          90       100
                  ....*....|....*....|
gi 495617436   82 PCPMCAGAIVLSRVKKVVFG 101
Cdd:pfam00383  81 PCGMCAQAIIESGIKRVVFG 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 5-153 1.56e-24

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: 96.28  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   5 EQFMQEAISEALKAKqiGEV----PIGAVIVVDDQIVSRAHNLRESEqrsiAHAELLAIDEACKmtgswRLEDAVLYVTL 80
Cdd:COG0117    1 ERYMRRALELARRGL--GTTspnpLVGCVIVKDGRIVGEGYHQRAGG----PHAEVNALAQAGE-----AARGATLYVTL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436  81 EPC------PMCAGAIVLSRVKKVVFGAYDPkggcagtlmnlldDERFNHQS---------EVIGGVLENECGELLSQFF 145
Cdd:COG0117   70 EPCshhgrtPPCADALIEAGIKRVVIAMLDP-------------NPLVAGKGiarlraagiEVEVGVLEEEARALNRGFL 136


                 ....*...
gi 495617436 146 RdlRQRKK 153
Cdd:COG0117  137 K--RMRTG 142
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 8-150 3.15e-18

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: 79.49  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436    8 MQEAISEALKAKQIGEV--PIGAVIVVDDQIVSRAHNLRESEqrsiAHAELLAIDEACKmtgswRLEDAVLYVTLEPC-- 83
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPnpLVGCVIVKNGEIVGEGAHQKAGE----PHAEVHALRQAGE-----NAKGATAYVTLEPCsh 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495617436   84 ----PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFnhqsEVIGGVLENECGELLSQFFRDLRQ 150
Cdd:TIGR00326  72 qgrtPPCAEAIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGFLKRMRT 138
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 8-105 2.17e-17

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: 73.04  E-value: 2.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   8 MQEAISEALKAKqiGEV----PIGAVIV-VDDQIVSRAHnlreSEQRSIAHAELLAIDEAckmtGSWRLEDAVLYVTLEP 82
Cdd:cd01284    1 MRRALELAEKGR--GLTspnpPVGCVIVdDDGEIVGEGY----HRKAGGPHAEVNALASA----GEKLARGATLYVTLEP 70

                         90       100
                 ....*....|....*....|....*....
gi 495617436  83 C------PMCAGAIVLSRVKKVVFGAYDP 105
Cdd:cd01284   71 CshhgktPPCVDAIIEAGIKRVVVGVRDP 99
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 4-100 5.38e-16

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: 70.00  E-value: 5.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   4 DEQFMQEAISEALKAKQIGeVPIGAVIVVDDQIVS---------------RAHNLRESEQRSIA------HAELLAIDEA 62
Cdd:cd01286    1 DEYFMAIARLAALRSTCPR-RQVGAVIVKDKRIIStgyngspsglphcaeVGCERDDLPSGEDQkccrtvHAEQNAILQA 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495617436  63 CKMTGSwrLEDAVLYVTLEPCPMCAGAIVLSRVKKVVF 100
Cdd:cd01286   80 ARHGVS--LEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-100 1.95e-15

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 69.10  E-value: 1.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   1 MTKDEQFMQEAISEALKAK----QIGevpigAVIVVDDQIVSRAHN--------------LRESEQ----------RSIa 52
Cdd:COG2131    6 PSWDEYFMEIAKLVALRSTclrrQVG-----AVIVKDKRILATGYNgapsglphcdevgcLREKLGipsgergeccRTV- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495617436  53 HAELLAIDEACKMTGSwrLEDAVLYVTLEPCPMCAGAIVLSRVKKVVF 100
Cdd:COG2131   80 HAEQNAILQAARHGVS--TEGATLYVTHFPCLECAKMIIQAGIKRVVY 125
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 8-100 1.32e-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: 65.26  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   8 MQEAISEA-LKAKQIGEVPIGAVIV--VDDQIVSRAHNLRESEQRSIAHAELLAIDEACKMTGSwrlEDAVLYVTLEPCP 84
Cdd:cd00786    1 MTEALKAAdLGYAKESNFQVGACLVnkKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDT---KGQMLYVALSPCG 77

                         90
                 ....*....|....*.
gi 495617436  85 MCAGAIVLSRVKKVVF 100
Cdd:cd00786   78 ACAQLIIELGIKDVIV 93
cd PHA02588
deoxycytidylate deaminase; Provisional
 3-104 3.88e-13

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 63.24  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   3 KDEQFMQEAISEALKAKQIgEVPIGAVIVVDDQIVSRAHN------------------------LRE---------SEQR 49
Cdd:PHA02588   2 KDSTYLQIAYLVSQESKCV-SWKVGAVIEKNGRIISTGYNgtpaggvnccdhaneqgwlddegkLKKehrpehsawSSKN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495617436  50 SIaHAELLAIDEACKmTGSwRLEDAVLYVTLEPCPMCAGAIVLSRVKKVVFGA-YD 104
Cdd:PHA02588  81 EI-HAELNAILFAAR-NGI-SIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEkYD 133
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 4-145 1.20e-10

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 58.25  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   4 DEQFMQEAISEALKAkqIGEVP----IGAVIVVDDQIVSRAHNLRESEqrsiAHAELLAIDEACKMTgswrlEDAVLYVT 79
Cdd:PLN02807  32 DSFYMRRCVELARKA--IGCTSpnpmVGCVIVKDGRIVGEGFHPKAGQ----PHAEVFALRDAGDLA-----ENATAYVS 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495617436  80 LEPC------PMCAGAIVLSRVKKVVFGAYDPKGGCAGTLMNLLDDERFnhqsEVIGGVLENECGELLSQFF 145
Cdd:PLN02807 101 LEPCnhygrtPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGI----EVTVGVEEELCRKLNEAFI 168
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 2-111 4.31e-10

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 56.70  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495617436   2 TKDEQFMqeaiSEALKAKQIGEVP------IGAVIVVDDQIVSRAHNLRESEqrsiAHAELLAIdeacKMTGSwRLEDAV 75
Cdd:PRK10786   1 MQDEFYM----ARALKLAQRGRFTthpnpnVGCVIVKDGEIVGEGYHQRAGE----PHAEVHAL----RMAGE-KAKGAT 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495617436  76 LYVTLEPC------PMCAGAIVLSRVKKVVFGAYDPKGGCAG 111
Cdd:PRK10786  68 AYVTLEPCshhgrtPPCCDALIAAGVARVVAAMQDPNPQVAG 109
Bd3614-deam pfam14439
Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 72-107 1.43e-03

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: 36.35  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 495617436   72 EDAVLYVTLEPCPMCAGAIVLSRVK----KVVFGAYDPKG 107
Cdd:pfam14439  56 PGARLLVTLQCCKMCAALVCAACDDpgqlKVVYLVEDPGG 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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