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Conserved domains on  [gi|300497857|gb|EFK32867|]
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cytidine and deoxycytidylate deaminase zinc-binding region [Lactobacillus delbrueckii subsp. bulgaricus PB2003/044-T3-4]

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 ...
 23-151 5.07e-71

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: 211.13  E-value: 5.07e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  23 RQDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEV 102
Cdd:COG0590   20 AEGEVPVGAVLVK-DGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRV 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 300497857 103 YFAAMDPKAGAAGSVVDLFSVEKFNHHPKVIRGLYKEQGAQLLKDFFRE 151
Cdd:COG0590   99 VYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAA 147
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 23-151 5.07e-71

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: 211.13  E-value: 5.07e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  23 RQDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEV 102
Cdd:COG0590   20 AEGEVPVGAVLVK-DGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRV 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 300497857 103 YFAAMDPKAGAAGSVVDLFSVEKFNHHPKVIRGLYKEQGAQLLKDFFRE 151
Cdd:COG0590   99 VYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAA 147
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 24-162 1.12e-46

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 150.34  E-value: 1.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  24 QDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEVY 103
Cdd:PRK10860  30 EREVPVGAVLVH-NNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCVMCAGAMVHSRIGRLV 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300497857 104 FAAMDPKAGAAGSVVDLFSVEKFNHHPKVIRGLYKEQGAQLLKDFFREIRRKQKLAKKS 162
Cdd:PRK10860 109 FGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKALKKA 167
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-153 1.23e-44

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: 144.20  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857    5 EEKKTYMEAAFAEAEKARRQDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTL 84
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVK-DGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300497857   85 EPCAMCAGAIINSRIKEVYFAAMDPKAGAAGSVVDLFSVEKFNHHPKVIrglyKEQGAQLLKDFFREIR 153
Cdd:pfam14437  80 EPCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 24-117 3.40e-44

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: 141.60  E-value: 3.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  24 QDEVPIGAVVVGPDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEVY 103
Cdd:cd01285   14 EGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMCAGALLWARIKRVV 93

                         90
                 ....*....|....
gi 300497857 104 FAAMDPKAGAAGSV 117
Cdd:cd01285   94 YGASDPKLGGIGFL 107
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 28-154 7.15e-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: 76.41  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857   28 PIGAVVVgPDGQIIGQGYNRREldedGTAHAEILAIKEACQKLDswrliDCSLFVTLEPCAM------CAGAIINSRIKE 101
Cdd:TIGR00326  20 LVGCVIV-KNGEIVGEGAHQKA----GEPHAEVHALRQAGENAK-----GATAYVTLEPCSHqgrtppCAEAIIEAGIKK 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300497857  102 VYFAAMDPKAGAAGSVVDLFSVEKFnhhpKVIRGLYKEQGAQLLKDFFREIRR 154
Cdd:TIGR00326  90 VVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGFLKRMRT 138
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 23-151 5.07e-71

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: 211.13  E-value: 5.07e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  23 RQDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEV 102
Cdd:COG0590   20 AEGEVPVGAVLVK-DGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRV 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 300497857 103 YFAAMDPKAGAAGSVVDLFSVEKFNHHPKVIRGLYKEQGAQLLKDFFRE 151
Cdd:COG0590   99 VYGASDPKAGAAGSIYDLLADPRLNHRVEVVGGVLAEECAALLRDFFAA 147
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 24-162 1.12e-46

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 150.34  E-value: 1.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  24 QDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEVY 103
Cdd:PRK10860  30 EREVPVGAVLVH-NNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCVMCAGAMVHSRIGRLV 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300497857 104 FAAMDPKAGAAGSVVDLFSVEKFNHHPKVIRGLYKEQGAQLLKDFFREIRRKQKLAKKS 162
Cdd:PRK10860 109 FGARDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADECAALLSDFFRMRRQEIKALKKA 167
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-153 1.23e-44

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: 144.20  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857    5 EEKKTYMEAAFAEAEKARRQDEVPIGAVVVGpDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTL 84
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVK-DGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300497857   85 EPCAMCAGAIINSRIKEVYFAAMDPKAGAAGSVVDLFSVEKFNHHPKVIrglyKEQGAQLLKDFFREIR 153
Cdd:pfam14437  80 EPCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELV----EEDCSEILKGFFKKLR 144
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 24-117 3.40e-44

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: 141.60  E-value: 3.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  24 QDEVPIGAVVVGPDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEVY 103
Cdd:cd01285   14 EGEVPFGAVIVDDDGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMCAGALLWARIKRVV 93

                         90
                 ....*....|....
gi 300497857 104 FAAMDPKAGAAGSV 117
Cdd:cd01285   94 YGASDPKLGGIGFL 107
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
25-105 6.38e-34

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 115.09  E-value: 6.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857   25 DEVPIGAVVVGPDGQIIGQGYNRRELDEDGTAHAEILAIKEACQKLDSWRLIDCSLFVTLEPCAMCAGAIINSRIKEVYF 104
Cdd:pfam00383  20 SNFPVGAVIVKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99


                  .
gi 300497857  105 A 105
Cdd:pfam00383 100 G 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 30-159 1.77e-22

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: 91.27  E-value: 1.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  30 GAVVVGpDGQIIGQGYNRReldeDGTAHAEILAIKEACQKLDswrliDCSLFVTLEPCAM------CAGAIINSRIKEVY 103
Cdd:COG0117   25 GCVIVK-DGRIVGEGYHQR----AGGPHAEVNALAQAGEAAR-----GATLYVTLEPCSHhgrtppCADALIEAGIKRVV 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300497857 104 FAAMDPKAGAAGSVVDLFS---VEkfnhhpkVIRGLYKEQGAQLLKDFFREIRRKQ-----KLA 159
Cdd:COG0117   95 IAMLDPNPLVAGKGIARLRaagIE-------VEVGVLEEEARALNRGFLKRMRTGRpfvtlKLA 151
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 28-116 4.54e-22

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: 85.36  E-value: 4.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  28 PIGAVVVGPDGQIIGQGYNRReldeDGTAHAEILAIKEACQKldswRLIDCSLFVTLEPCAM------CAGAIINSRIKE 101
Cdd:cd01284   20 PVGCVIVDDDGEIVGEGYHRK----AGGPHAEVNALASAGEK----LARGATLYVTLEPCSHhgktppCVDAIIEAGIKR 91

                         90
                 ....*....|....*
gi 300497857 102 VYFAAMDPKAGAAGS 116
Cdd:cd01284   92 VVVGVRDPNPLVAGK 106
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 28-154 7.15e-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: 76.41  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857   28 PIGAVVVgPDGQIIGQGYNRREldedGTAHAEILAIKEACQKLDswrliDCSLFVTLEPCAM------CAGAIINSRIKE 101
Cdd:TIGR00326  20 LVGCVIV-KNGEIVGEGAHQKA----GEPHAEVHALRQAGENAK-----GATAYVTLEPCSHqgrtppCAEAIIEAGIKK 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300497857  102 VYFAAMDPKAGAAGSVVDLFSVEKFnhhpKVIRGLYKEQGAQLLKDFFREIRR 154
Cdd:TIGR00326  90 VVVSMQDPNPLVAGRGAERLKQAGI----EVTFGILKEEAERLNKGFLKRMRT 138
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 27-105 1.83e-16

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: 70.66  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  27 VPIGAVVV-GPDGQIIGQGYNRRELDEDGTAHAEILAIkEACQKLDSWRliDCSLFVTLEPCAMCAGAIINSRIKEVYFA 105
Cdd:cd00786   18 FQVGACLVnKKDGGKVGRGCNIENAAYSMCNHAERTAL-FNAGSEGDTK--GQMLYVALSPCGACAQLIIELGIKDVIVV 94
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 22-105 4.94e-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: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  22 RRQdevpIGAVVVGpDGQIIGQGYN-------------RRELDEDG--------TAHAEILAIKEACQKLDSwrLIDCSL 80
Cdd:cd01286   19 RRQ----VGAVIVK-DKRIISTGYNgspsglphcaevgCERDDLPSgedqkccrTVHAEQNAILQAARHGVS--LEGATL 91

                         90       100
                 ....*....|....*....|....*
gi 300497857  81 FVTLEPCAMCAGAIINSRIKEVYFA 105
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVYA 116
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
22-105 3.22e-14

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 66.02  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  22 RRQdevpIGAVVVgPDGQIIGQGYN---------------RREL----DEDG----TAHAEILAIKeACQKLDSwRLIDC 78
Cdd:COG2131   27 RRQ----VGAVIV-KDKRILATGYNgapsglphcdevgclREKLgipsGERGeccrTVHAEQNAIL-QAARHGV-STEGA 99

                         90       100
                 ....*....|....*....|....*..
gi 300497857  79 SLFVTLEPCAMCAGAIINSRIKEVYFA 105
Cdd:COG2131  100 TLYVTHFPCLECAKMIIQAGIKRVVYL 126
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 29-142 7.31e-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: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  29 IGAVVVgPDGQIIGQGYNRREldedGTAHAEILAIKEACQKLDSwrlidCSLFVTLEPCAM------CAGAIINSRIKEV 102
Cdd:PRK10786  27 VGCVIV-KDGEIVGEGYHQRA----GEPHAEVHALRMAGEKAKG-----ATAYVTLEPCSHhgrtppCCDALIAAGVARV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 300497857 103 YFAAMDPKAGAAGsvvdlfsvekfnhhpkviRGLYKEQGA 142
Cdd:PRK10786  97 VAAMQDPNPQVAG------------------RGLYRLQQA 118
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 29-119 5.03e-08

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 51.31  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  29 IGAVVVgPDGQIIGQGYNRREldedGTAHAEILAIKEACQKLDswrliDCSLFVTLEPCAM------CAGAIINSRIKEV 102
Cdd:PLN02807  56 VGCVIV-KDGRIVGEGFHPKA----GQPHAEVFALRDAGDLAE-----NATAYVSLEPCNHygrtppCTEALIKAKVKRV 125

                         90
                 ....*....|....*..
gi 300497857 103 YFAAMDPKAGAAGSVVD 119
Cdd:PLN02807 126 VVGMVDPNPIVASKGIE 142
cd PHA02588
deoxycytidylate deaminase; Provisional
 29-105 5.27e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 44.36  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857  29 IGAVVVgPDGQIIGQGYN--------------------------------RRELDEDGTAHAEILAIKEACQKLDSwrLI 76
Cdd:PHA02588  24 VGAVIE-KNGRIISTGYNgtpaggvnccdhaneqgwlddegklkkehrpeHSAWSSKNEIHAELNAILFAARNGIS--IE 100

                         90       100
                 ....*....|....*....|....*....
gi 300497857  77 DCSLFVTLEPCAMCAGAIINSRIKEVYFA 105
Cdd:PHA02588 101 GATMYVTASPCPDCAKAIAQSGIKKLVYC 129
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 28-95 2.02e-05

Cytidine deaminase zinc-binding domain. These enzymes 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. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes.


Pssm-ID: 238610 [Multi-domain]  Cd Length: 112  Bit Score: 41.56  E-value: 2.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300497857  28 PIGAVVVGPDGQIIgQGYNRRELDEDGTAHAEILAIKEACQKLDswRLIDCSLFVTLE-----PCAMCAGAII 95
Cdd:cd01283   19 TVGAALLTKDGRIF-TGVNVENASYGLTLCAERTAIGKAVSEGL--RRYLVTWAVSDEggvwsPCGACRQVLA 88
Bd3614-deam pfam14439
Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 29-119 2.11e-05

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: 41.74  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300497857   29 IGAVVVGPDGQIIGQGYNRREldEDGTAHAEILAIKEACQKLDSwRLI--DCSLFVTLEPCAMCAGAIIN-----SRIKe 101
Cdd:pfam14439  10 VVAALVSPQGQLLDAAVNTNA--KNKTLHAEVNLLQPLLRETAR-RPIppGARLLVTLQCCKMCAALVCAacddpGQLK- 85

                          90
                  ....*....|....*...
gi 300497857  102 VYFAAMDPKAGAAGSVVD 119
Cdd:pfam14439  86 VVYLVEDPGGLARDTVLR 103
 
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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