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Conserved domains on  [gi|530377248|ref|XP_005262835|]
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deoxycytidylate deaminase isoform X1 [Homo sapiens]

Protein Classification

deoxycytidylate deaminase( domain architecture ID 10788416)

deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase

CATH:  3.40.140.10
EC:  3.5.4.12
Gene Ontology:  GO:0004132|GO:0008270|GO:0009972|GO:0006220
PubMed:  2247612
SCOP:  4000564

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
19-169 1.13e-61

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 188.13  E-value: 1.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  19 KRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVnSENKIVGIGYNGMPNGCSDDVLP-WRRTAENKL---DTKYPYVC 94
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377248  95 HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDsdeatAARLLFNMAGVTFRKFIPK 169
Cdd:COG2131   80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
19-169 1.13e-61

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 188.13  E-value: 1.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  19 KRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVnSENKIVGIGYNGMPNGCSDDVLP-WRRTAENKL---DTKYPYVC 94
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377248  95 HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDsdeatAARLLFNMAGVTFRKFIPK 169
Cdd:COG2131   80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 28-149 1.69e-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: 171.69  E-value: 1.69e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  28 EYFMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNGCSDDVLPWRRTAE--NKLDTKYPYVCHAELNAIMN-- 103
Cdd:cd01286    2 EYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVGCERDDlpSGEDQKCCRTVHAEQNAILQaa 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530377248 104 KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEA 149
Cdd:cd01286   81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAA 126
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
26-138 2.35e-31

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 109.31  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248   26 WPEYFMAVAFLSAQRS-KDPNSQVGACIVNSENKIVGIGYNGMPNGcsddvlpwrrtaenkldtkYPYVCHAELNAIMNK 104
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG-------------------YDPTIHAERNAIRQA 61

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530377248  105 NST----DVKGCSMYVALFPCNECAKLIIQAGIKEVIF 138
Cdd:pfam00383  62 GKRgegvRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cd PHA02588
deoxycytidylate deaminase; Provisional
 30-154 2.70e-20

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 82.88  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  30 FMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNG---CSD--DVLPWRrTAENKLDTKYP---------YVCH 95
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGgvnCCDhaNEQGWL-DDEGKLKKEHRpehsawsskNEIH 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377248  96 AELNAIM--NKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMsDKYHDSDEATAARL 154
Cdd:PHA02588  84 AELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC-EKYDRNGPGWDDIL 143
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 28-139 7.26e-18

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: 80.29  E-value: 7.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  28 EYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMP--------------------NGCSDDV------------ 75
Cdd:NF041025 220 ERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPkaggglywpgdepdhrdyslGYDRNDEekrkiiedilkr 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  76 LPWRRTAENKLDTKYPYVC--------------------HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGI 133
Cdd:NF041025 300 LADAGSESLKKKGRNASECfklilkksrikdliefgravHAEMNAILSaaRLGGSTKGGTLYTTTFPCHNCAKHIVAAGI 379


                 ....*.
gi 530377248 134 KEVIFM 139
Cdd:NF041025 380 KRVVYI 385
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 44-141 9.52e-09

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: 53.68  E-value: 9.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248   44 PNSQVGACIVNSEnKIVGIGYNGMPNGCsddvlpwrrtaenkldtkypyvcHAELNAI-MNKNSTdvKGCSMYVALFPCN 122
Cdd:TIGR00326  17 PNPLVGCVIVKNG-EIVGEGAHQKAGEP-----------------------HAEVHALrQAGENA--KGATAYVTLEPCS 70

                          90       100
                  ....*....|....*....|....*.
gi 530377248  123 E------CAKLIIQAGIKEVIF-MSD 141
Cdd:TIGR00326  71 HqgrtppCAEAIIEAGIKKVVVsMQD 96
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
19-169 1.13e-61

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 188.13  E-value: 1.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  19 KRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVnSENKIVGIGYNGMPNGCSDDVLP-WRRTAENKL---DTKYPYVC 94
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377248  95 HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDsdeatAARLLFNMAGVTFRKFIPK 169
Cdd:COG2131   80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 28-149 1.69e-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: 171.69  E-value: 1.69e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  28 EYFMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNGCSDDVLPWRRTAE--NKLDTKYPYVCHAELNAIMN-- 103
Cdd:cd01286    2 EYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVGCERDDlpSGEDQKCCRTVHAEQNAILQaa 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530377248 104 KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEA 149
Cdd:cd01286   81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAA 126
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 27-141 1.81e-39

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: 129.98  E-value: 1.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  27 PEYFMAVAFLSAQrsKDPNSQVGACIVNSEnkivgiGYNGMPNGCSDDVLPwrrtaenkldtkYPYVCHAELNAIMNKNS 106
Cdd:cd00786    1 MTEALKAADLGYA--KESNFQVGACLVNKK------DGGKVGRGCNIENAA------------YSMCNHAERTALFNAGS 60

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530377248 107 T-DVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSD 141
Cdd:cd00786   61 EgDTKGQMLYVALSPCGACAQLIIELGIKDVIVVLT 96
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
26-138 2.35e-31

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 109.31  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248   26 WPEYFMAVAFLSAQRS-KDPNSQVGACIVNSENKIVGIGYNGMPNGcsddvlpwrrtaenkldtkYPYVCHAELNAIMNK 104
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG-------------------YDPTIHAERNAIRQA 61

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530377248  105 NST----DVKGCSMYVALFPCNECAKLIIQAGIKEVIF 138
Cdd:pfam00383  62 GKRgegvRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cd PHA02588
deoxycytidylate deaminase; Provisional
 30-154 2.70e-20

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 82.88  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  30 FMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNG---CSD--DVLPWRrTAENKLDTKYP---------YVCH 95
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGgvnCCDhaNEQGWL-DDEGKLKKEHRpehsawsskNEIH 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377248  96 AELNAIM--NKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMsDKYHDSDEATAARL 154
Cdd:PHA02588  84 AELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC-EKYDRNGPGWDDIL 143
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 28-139 7.26e-18

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: 80.29  E-value: 7.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  28 EYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMP--------------------NGCSDDV------------ 75
Cdd:NF041025 220 ERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPkaggglywpgdepdhrdyslGYDRNDEekrkiiedilkr 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  76 LPWRRTAENKLDTKYPYVC--------------------HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGI 133
Cdd:NF041025 300 LADAGSESLKKKGRNASECfklilkksrikdliefgravHAEMNAILSaaRLGGSTKGGTLYTTTFPCHNCAKHIVAAGI 379


                 ....*.
gi 530377248 134 KEVIFM 139
Cdd:NF041025 380 KRVVYI 385
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 28-141 1.18e-13

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: 67.78  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  28 EYFMAVAFLSAQRSK---DPNSQVGACIVNsENKIVGIGY---NGMPngcsddvlpwrrtaenkldtkypyvcHAELNAI 101
Cdd:COG0117    1 ERYMRRALELARRGLgttSPNPLVGCVIVK-DGRIVGEGYhqrAGGP--------------------------HAEVNAL 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530377248 102 mNKNSTDVKGCSMYVALFPCNE------CAKLIIQAGIKEVIF-MSD 141
Cdd:COG0117   54 -AQAGEAARGATLYVTLEPCSHhgrtppCADALIEAGIKRVVIaMLD 99
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 43-141 2.37e-12

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: 60.71  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  43 DPNSQVGACIVNSENKIVGIGYN---GMPngcsddvlpwrrtaenkldtkypyvcHAELNAIMNKNSTDVKGCSMYVALF 119
Cdd:cd01284   16 SPNPPVGCVIVDDDGEIVGEGYHrkaGGP--------------------------HAEVNALASAGEKLARGATLYVTLE 69

                         90       100
                 ....*....|....*....|....*....
gi 530377248 120 PCNE------CAKLIIQAGIKEVIF-MSD 141
Cdd:cd01284   70 PCSHhgktppCVDAIIEAGIKRVVVgVRD 98
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 25-177 9.49e-12

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: 59.84  E-value: 9.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248   25 EWPEYFMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNgmpngcsddvlpwrRTAENKLDTKypyvcHAELNAIM-- 102
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVK-DGKVIARGYN--------------RKELNADTTA-----HAEILAIQqa 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377248  103 -NKN-STDVKGCSMYVALFPCNECAKLIIQAGIKEVIF-MSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDF 177
Cdd:pfam14437  62 aKKLgSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYgAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGF 139
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 31-138 1.20e-10

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: 56.09  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248  31 MAVAFLSAQRSKDPNSQ-VGACIVNSENKIVGIGYNgmpngcsddvlpwRRTAENklDTkypyVCHAELNAIMN----KN 105
Cdd:cd01285    1 MRLAIELARKALAEGEVpFGAVIVDDDGKVIARGHN-------------RVEQDG--DP----TAHAEIVAIRNaarrLG 61

                         90       100       110
                 ....*....|....*....|....*....|...
gi 530377248 106 STDVKGCSMYVALFPCNECAKLIIQAGIKEVIF 138
Cdd:cd01285   62 SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVY 94
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 44-141 9.52e-09

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: 53.68  E-value: 9.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377248   44 PNSQVGACIVNSEnKIVGIGYNGMPNGCsddvlpwrrtaenkldtkypyvcHAELNAI-MNKNSTdvKGCSMYVALFPCN 122
Cdd:TIGR00326  17 PNPLVGCVIVKNG-EIVGEGAHQKAGEP-----------------------HAEVHALrQAGENA--KGATAYVTLEPCS 70

                          90       100
                  ....*....|....*....|....*.
gi 530377248  123 E------CAKLIIQAGIKEVIF-MSD 141
Cdd:TIGR00326  71 HqgrtppCAEAIIEAGIKKVVVsMQD 96
 
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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