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Conserved domains on  [gi|116326433|ref|YP_803153|]
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dCMP deaminase [Escherichia phage RB32]

Protein Classification

cytidine/deoxycytidylate deaminase family protein; cytidine deaminase( domain architecture ID 10010089)

cytidine/deoxycytidylate deaminase family protein similar to Bacillus subtilis cytidine deaminase that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; cytidine deaminase catalyzes the deamination of cytidine to uridine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cd PHA02588
deoxycytidylate deaminase; Provisional
 1-188 6.61e-106

deoxycytidylate deaminase; Provisional


:

Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 300.91  E-value: 6.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   1 MKASTVLQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLlnkpkhtiiqghkpecvsfgs 80
Cdd:PHA02588   1 MKDSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGWL--------------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  81 TDRFVLAKEHRSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGW 160
Cdd:PHA02588  60 DDEGKLKKEHRPEHSAWSSKNEIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGPGW 139

                        170       180
                 ....*....|....*....|....*...
gi 116326433 161 DDILRNAGIEVFNVPKKNLNKLNWENIN 188
Cdd:PHA02588 140 DDILRKSGIEVIQIPKEELNKLNWESNQ 167
 
Name Accession Description Interval E-value
cd PHA02588
deoxycytidylate deaminase; Provisional
 1-188 6.61e-106

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 300.91  E-value: 6.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   1 MKASTVLQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLlnkpkhtiiqghkpecvsfgs 80
Cdd:PHA02588   1 MKDSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGWL--------------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  81 TDRFVLAKEHRSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGW 160
Cdd:PHA02588  60 DDEGKLKKEHRPEHSAWSSKNEIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGPGW 139

                        170       180
                 ....*....|....*....|....*...
gi 116326433 161 DDILRNAGIEVFNVPKKNLNKLNWENIN 188
Cdd:PHA02588 140 DDILRKSGIEVIQIPKEELNKLNWESNQ 167
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 7-165 4.72e-55

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: 170.92  E-value: 4.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   7 LQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLlnkpkhtiiqghkpecvsfgstdrfvl 86
Cdd:cd01286    5 MAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL--------------------------- 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116326433  87 akehrSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGWDDILR 165
Cdd:cd01286   58 -----PSGEDQKCCRTVHAEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAAAELLE 131
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
7-178 1.69e-51

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 162.70  E-value: 1.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   7 LQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCdyaaEQGWLlnKPKHTIIQGHKPECVsfgstdrfvl 86
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCD----EVGCL--REKLGIPSGERGECC---------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  87 akehRSahsewsskneIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPgwDDILRN 166
Cdd:COG2131   77 ----RT----------VHAEQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELA--KELLKE 140

                        170
                 ....*....|..
gi 116326433 167 AGIEVFNVPKKN 178
Cdd:COG2131  141 AGVEVRQLELEE 152
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 5-155 8.74e-25

anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase.


Pssm-ID: 468954 [Multi-domain]  Cd Length: 435  Bit Score: 99.55  E-value: 8.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   5 TVLQIAYLVSQESKCCSWKVGAVI-EKNGRIISTGYNGSPA--GGVnccdYaaeqgWLLNKP---------------KHT 66
Cdd:NF041025 221 RGMYAAFSAALRSACLSRQVGAAItDKDGEIISTGWNDVPKagGGL----Y-----WPGDEPdhrdyslgydrndeeKRK 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  67 IIQ--------GHKPECVSFGSTDRFVLAKEHRSahsewsSKNE--------IHAELNAILFAARNGSSIEGATMYVTLS 130
Cdd:NF041025 292 IIEdilkrladAGSESLKKKGRNASECFKLILKK------SRIKdliefgraVHAEMNAILSAARLGGSTKGGTLYTTTF 365

                        170       180
                 ....*....|....*....|....*
gi 116326433 131 PCPDCAKAIAQSGIKKLVYCETYDK 155
Cdd:NF041025 366 PCHNCAKHIVAAGIKRVVYIEPYPK 390
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
2-149 1.30e-24

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 92.36  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433    2 KASTVLQIAYLVSQESKCCS-WKVGAVIEK-NGRIISTGYNGSPAGGVNCcdyaaeqgwllnkpkhtiiqghkpecvsfg 79
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSnFPVGAVIVKkDGEIIATGYNGENAGYDPT------------------------------ 50

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116326433   80 stdrfvlakehrsahsewsskneIHAELNAILFAARNG--SSIEGATMYVTLSPCPDCAKAIAQSGIKKLVY 149
Cdd:pfam00383  51 -----------------------IHAERNAIRQAGKRGegVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 102-183 3.13e-12

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: 63.69  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  102 EIHAELNAILFAarnGSSIEGATMYVTLSPC------PDCAKAIAQSGIKKLVYcETYDKNK--PGWD-DILRNAGIEV- 171
Cdd:TIGR00326  42 EPHAEVHALRQA---GENAKGATAYVTLEPCshqgrtPPCAEAIIEAGIKKVVV-SMQDPNPlvAGRGaERLKQAGIEVt 117

                          90
                  ....*....|..
gi 116326433  172 FNVPKKNLNKLN 183
Cdd:TIGR00326 118 FGILKEEAERLN 129
 
Name Accession Description Interval E-value
cd PHA02588
deoxycytidylate deaminase; Provisional
 1-188 6.61e-106

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 300.91  E-value: 6.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   1 MKASTVLQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLlnkpkhtiiqghkpecvsfgs 80
Cdd:PHA02588   1 MKDSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGWL--------------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  81 TDRFVLAKEHRSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGW 160
Cdd:PHA02588  60 DDEGKLKKEHRPEHSAWSSKNEIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGPGW 139

                        170       180
                 ....*....|....*....|....*...
gi 116326433 161 DDILRNAGIEVFNVPKKNLNKLNWENIN 188
Cdd:PHA02588 140 DDILRKSGIEVIQIPKEELNKLNWESNQ 167
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 7-165 4.72e-55

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: 170.92  E-value: 4.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   7 LQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLlnkpkhtiiqghkpecvsfgstdrfvl 86
Cdd:cd01286    5 MAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL--------------------------- 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116326433  87 akehrSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGWDDILR 165
Cdd:cd01286   58 -----PSGEDQKCCRTVHAEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAAAELLE 131
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
7-178 1.69e-51

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 162.70  E-value: 1.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   7 LQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCdyaaEQGWLlnKPKHTIIQGHKPECVsfgstdrfvl 86
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCD----EVGCL--REKLGIPSGERGECC---------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  87 akehRSahsewsskneIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPgwDDILRN 166
Cdd:COG2131   77 ----RT----------VHAEQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELA--KELLKE 140

                        170
                 ....*....|..
gi 116326433 167 AGIEVFNVPKKN 178
Cdd:COG2131  141 AGVEVRQLELEE 152
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 5-155 8.74e-25

anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase.


Pssm-ID: 468954 [Multi-domain]  Cd Length: 435  Bit Score: 99.55  E-value: 8.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   5 TVLQIAYLVSQESKCCSWKVGAVI-EKNGRIISTGYNGSPA--GGVnccdYaaeqgWLLNKP---------------KHT 66
Cdd:NF041025 221 RGMYAAFSAALRSACLSRQVGAAItDKDGEIISTGWNDVPKagGGL----Y-----WPGDEPdhrdyslgydrndeeKRK 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  67 IIQ--------GHKPECVSFGSTDRFVLAKEHRSahsewsSKNE--------IHAELNAILFAARNGSSIEGATMYVTLS 130
Cdd:NF041025 292 IIEdilkrladAGSESLKKKGRNASECFKLILKK------SRIKdliefgraVHAEMNAILSAARLGGSTKGGTLYTTTF 365

                        170       180
                 ....*....|....*....|....*
gi 116326433 131 PCPDCAKAIAQSGIKKLVYCETYDK 155
Cdd:NF041025 366 PCHNCAKHIVAAGIKRVVYIEPYPK 390
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
2-149 1.30e-24

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 92.36  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433    2 KASTVLQIAYLVSQESKCCS-WKVGAVIEK-NGRIISTGYNGSPAGGVNCcdyaaeqgwllnkpkhtiiqghkpecvsfg 79
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSnFPVGAVIVKkDGEIIATGYNGENAGYDPT------------------------------ 50

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116326433   80 stdrfvlakehrsahsewsskneIHAELNAILFAARNG--SSIEGATMYVTLSPCPDCAKAIAQSGIKKLVY 149
Cdd:pfam00383  51 -----------------------IHAERNAIRQAGKRGegVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 24-155 1.31e-15

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: 70.15  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  24 VGAVIEKNGRIISTGYNgspaggvnccdyaaeqgwllnkpkhTIIQGHKPecvsfgstdrfvlakehrSAHsewssknei 103
Cdd:COG0590   26 VGAVLVKDGEIIARGHN-------------------------RVETLNDP------------------TAH--------- 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116326433 104 hAELNAILFAARNGSSI--EGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDK 155
Cdd:COG0590   54 -AEILAIRAAARKLGNWrlSGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPK 106
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 24-171 1.59e-14

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: 70.09  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  24 VGAVIEKNGRIISTGYngspaggvnccdyaaeqgwllnkpkhtiiqgHKPecvsFGstdrfvlakehrsahsewssknEI 103
Cdd:COG0117   24 VGCVIVKDGRIVGEGY-------------------------------HQR----AG----------------------GP 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433 104 HAELNAIlfaARNGSSIEGATMYVTLSPC------PDCAKAIAQSGIKKLVYcetydknkpGWDD-----------ILRN 166
Cdd:COG0117   47 HAEVNAL---AQAGEAARGATLYVTLEPCshhgrtPPCADALIEAGIKRVVI---------AMLDpnplvagkgiaRLRA 114


                 ....*
gi 116326433 167 AGIEV 171
Cdd:COG0117  115 AGIEV 119
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 104-152 3.63e-13

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: 62.63  E-value: 3.63e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 116326433 104 HAELNAILFAARNGSSI--EGATMYVTLSPCPDCAKAIAQSGIKKLVYCET 152
Cdd:cd01285   47 HAEIVAIRNAARRLGSYllSGCTLYTTLEPCPMCAGALLWARIKRVVYGAS 97
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 8-188 5.42e-13

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: 63.31  E-value: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433    8 QIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNgspaggvnccdyaaeqgwllnkpkhtiiqghkpecvsFGSTDRFVLA 87
Cdd:pfam14437   9 KALGLAEKAYDAGEVPIGAVIVKDGKVIARGYN-------------------------------------RKELNADTTA 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433   88 kehrsahsewsskneiHAELNAILFAARNGSSI--EGATMYVTLSPCPDCAKAIAQSGIKKLVYcetydknkpgwddilr 165
Cdd:pfam14437  52 ----------------HAEILAIQQAAKKLGSWrlDDATLYVTLEPCPMCAGAIVQAGLKSLVY---------------- 99

                         170       180
                  ....*....|....*....|...
gi 116326433  166 NAGIEVFNVPKKNLNKLNWENIN 188
Cdd:pfam14437 100 GAGNPKGGAVGSVLNKLVIVLWN 122
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 102-183 3.13e-12

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: 63.69  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433  102 EIHAELNAILFAarnGSSIEGATMYVTLSPC------PDCAKAIAQSGIKKLVYcETYDKNK--PGWD-DILRNAGIEV- 171
Cdd:TIGR00326  42 EPHAEVHALRQA---GENAKGATAYVTLEPCshqgrtPPCAEAIIEAGIKKVVV-SMQDPNPlvAGRGaERLKQAGIEVt 117

                          90
                  ....*....|..
gi 116326433  172 FNVPKKNLNKLN 183
Cdd:TIGR00326 118 FGILKEEAERLN 129
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 104-168 1.08e-11

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: 59.17  E-value: 1.08e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116326433 104 HAELNAILFAARNGSsiEGATMYVTLSPC------PDCAKAIAQSGIKKLVYCeTYDKNKP---GWDDILRNAG 168
Cdd:cd01284   45 HAEVNALASAGEKLA--RGATLYVTLEPCshhgktPPCVDAIIEAGIKRVVVG-VRDPNPLvagKGAERLRAAG 115
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 102-145 2.00e-09

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: 52.55  E-value: 2.00e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 116326433 102 EIHAELNAILFAARNGSsIEGATMYVTLSPCPDCAKAIAQSGIK 145
Cdd:cd00786   47 CNHAERTALFNAGSEGD-TKGQMLYVALSPCGACAQLIIELGIK 89
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 102-171 1.28e-05

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 44.76  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326433 102 EIHAELnailFAARN-GSSIEGATMYVTLSPC------PDCAKAIAQSGIKKLVyCETYDKN----KPGWDDiLRNAGIE 170
Cdd:PLN02807  77 QPHAEV----FALRDaGDLAENATAYVSLEPCnhygrtPPCTEALIKAKVKRVV-VGMVDPNpivaSKGIER-LRDAGIE 150


                 .
gi 116326433 171 V 171
Cdd:PLN02807 151 V 151
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 102-148 2.63e-05

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 43.60  E-value: 2.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116326433 102 EIHAELNAILFAarnGSSIEGATMYVTLSPC------PDCAKAIAQSGIKKLV 148
Cdd:PRK10786  48 EPHAEVHALRMA---GEKAKGATAYVTLEPCshhgrtPPCCDALIAAGVARVV 97
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 104-149 1.55e-04

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 40.56  E-value: 1.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116326433 104 HAELNAIlfaaRNGSSIEG------ATMYVTLSPCPDCAKAIAQSGIKKLVY 149
Cdd:PRK10860  62 HAEIMAL----RQGGLVLQnyrlldATLYVTLEPCVMCAGAMVHSRIGRLVF 109
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 98-157 1.68e-03

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: 36.55  E-value: 1.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326433  98 SSKNEIHAELNAILFAARNGSSIEGATMYVT-----LSPCPDCAKAIAQSGIKKLVYCETYDKNK 157
Cdd:cd01283   41 SYGLTLCAERTAIGKAVSEGLRRYLVTWAVSdeggvWSPCGACRQVLAEFLPSRLYIIIDNPKGE 105
SNAD4 pfam18750
Secreted Novel AID/APOBEC-like Deaminase 4; A family of secreted AID/APOBEC like deaminases ...
 98-140 7.39e-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: 7.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 116326433   98 SSKNEIHAELN------AILFAARNGSSIegaTMYVTLSPCPDCAKAIA 140
Cdd:pfam18750  18 SNEHEQHAEICflenirSRELDPSQRYRV---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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