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Conserved domains on  [gi|1197977499|ref|NP_001338676|]
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deoxycytidylate deaminase isoform b [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];
8-158 1.09e-61

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 187.74  E-value: 1.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499   8 KRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVnSENKIVGIGYNGMPNGCSDDVLP-WRRTAENKL---DTKYPYVC 83
Cdd:COG2131     1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197977499  84 HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDsdeatAARLLFNMAGVTFRKFIPK 158
Cdd:COG2131    80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
8-158 1.09e-61

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 187.74  E-value: 1.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499   8 KRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVnSENKIVGIGYNGMPNGCSDDVLP-WRRTAENKL---DTKYPYVC 83
Cdd:COG2131     1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197977499  84 HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDsdeatAARLLFNMAGVTFRKFIPK 158
Cdd:COG2131    80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 17-138 1.99e-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: 171.30  E-value: 1.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  17 EYFMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNGCSDDVLPWRRTAE--NKLDTKYPYVCHAELNAIMN-- 92
Cdd:cd01286     2 EYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVGCERDDlpSGEDQKCCRTVHAEQNAILQaa 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1197977499  93 KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEA 138
Cdd:cd01286    81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAA 126
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
15-127 2.04e-31

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 109.31  E-value: 2.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  15 WPEYFMAVAFLSAQRS-KDPNSQVGACIVNSENKIVGIGYNGMPNGcsddvlpwrrtaenkldtkYPYVCHAELNAIMNK 93
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG-------------------YDPTIHAERNAIRQA 61

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1197977499  94 NST----DVKGCSMYVALFPCNECAKLIIQAGIKEVIF 127
Cdd:pfam00383  62 GKRgegvRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cd PHA02588
deoxycytidylate deaminase; Provisional
 19-143 2.52e-20

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 82.88  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  19 FMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNG---CSD--DVLPWRrTAENKLDTKYP---------YVCH 84
Cdd:PHA02588    6 YLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGgvnCCDhaNEQGWL-DDEGKLKKEHRpehsawsskNEIH 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1197977499  85 AELNAIM--NKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMsDKYHDSDEATAARL 143
Cdd:PHA02588   84 AELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC-EKYDRNGPGWDDIL 143
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 17-128 8.55e-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: 79.52  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  17 EYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMP--------------------NGCSDDV------------ 64
Cdd:NF041025  220 ERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPkaggglywpgdepdhrdyslGYDRNDEekrkiiedilkr 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  65 LPWRRTAENKLDTKYPYVC--------------------HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGI 122
Cdd:NF041025  300 LADAGSESLKKKGRNASECfklilkksrikdliefgravHAEMNAILSaaRLGGSTKGGTLYTTTFPCHNCAKHIVAAGI 379


                  ....*.
gi 1197977499 123 KEVIFM 128
Cdd:NF041025  380 KRVVYI 385
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 33-130 7.60e-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: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  33 PNSQVGACIVNSEnKIVGIGYNGMPNGCsddvlpwrrtaenkldtkypyvcHAELNAI-MNKNSTdvKGCSMYVALFPCN 111
Cdd:TIGR00326  17 PNPLVGCVIVKNG-EIVGEGAHQKAGEP-----------------------HAEVHALrQAGENA--KGATAYVTLEPCS 70

                          90       100
                  ....*....|....*....|....*.
gi 1197977499 112 E------CAKLIIQAGIKEVIF-MSD 130
Cdd:TIGR00326  71 HqgrtppCAEAIIEAGIKKVVVsMQD 96
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
8-158 1.09e-61

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 187.74  E-value: 1.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499   8 KRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVnSENKIVGIGYNGMPNGCSDDVLP-WRRTAENKL---DTKYPYVC 83
Cdd:COG2131     1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197977499  84 HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDsdeatAARLLFNMAGVTFRKFIPK 158
Cdd:COG2131    80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 17-138 1.99e-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: 171.30  E-value: 1.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  17 EYFMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNGCSDDVLPWRRTAE--NKLDTKYPYVCHAELNAIMN-- 92
Cdd:cd01286     2 EYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVGCERDDlpSGEDQKCCRTVHAEQNAILQaa 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1197977499  93 KNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEA 138
Cdd:cd01286    81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAA 126
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 16-130 9.02e-40

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: 130.36  E-value: 9.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  16 PEYFMAVAFLSAQrsKDPNSQVGACIVNSEnkivgiGYNGMPNGCSDDVLPwrrtaenkldtkYPYVCHAELNAIMNKNS 95
Cdd:cd00786     1 MTEALKAADLGYA--KESNFQVGACLVNKK------DGGKVGRGCNIENAA------------YSMCNHAERTALFNAGS 60

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1197977499  96 T-DVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSD 130
Cdd:cd00786    61 EgDTKGQMLYVALSPCGACAQLIIELGIKDVIVVLT 96
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
15-127 2.04e-31

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 109.31  E-value: 2.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  15 WPEYFMAVAFLSAQRS-KDPNSQVGACIVNSENKIVGIGYNGMPNGcsddvlpwrrtaenkldtkYPYVCHAELNAIMNK 93
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG-------------------YDPTIHAERNAIRQA 61

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1197977499  94 NST----DVKGCSMYVALFPCNECAKLIIQAGIKEVIF 127
Cdd:pfam00383  62 GKRgegvRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cd PHA02588
deoxycytidylate deaminase; Provisional
 19-143 2.52e-20

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 82.88  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  19 FMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNGMPNG---CSD--DVLPWRrTAENKLDTKYP---------YVCH 84
Cdd:PHA02588    6 YLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGgvnCCDhaNEQGWL-DDEGKLKKEHRpehsawsskNEIH 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1197977499  85 AELNAIM--NKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMsDKYHDSDEATAARL 143
Cdd:PHA02588   84 AELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC-EKYDRNGPGWDDIL 143
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 17-128 8.55e-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: 79.52  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  17 EYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMP--------------------NGCSDDV------------ 64
Cdd:NF041025  220 ERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPkaggglywpgdepdhrdyslGYDRNDEekrkiiedilkr 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  65 LPWRRTAENKLDTKYPYVC--------------------HAELNAIMN--KNSTDVKGCSMYVALFPCNECAKLIIQAGI 122
Cdd:NF041025  300 LADAGSESLKKKGRNASECfklilkksrikdliefgravHAEMNAILSaaRLGGSTKGGTLYTTTFPCHNCAKHIVAAGI 379


                  ....*.
gi 1197977499 123 KEVIFM 128
Cdd:NF041025  380 KRVVYI 385
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 17-130 9.00e-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: 67.78  E-value: 9.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  17 EYFMAVAFLSAQRSK---DPNSQVGACIVNsENKIVGIGY---NGMPngcsddvlpwrrtaenkldtkypyvcHAELNAI 90
Cdd:COG0117     1 ERYMRRALELARRGLgttSPNPLVGCVIVK-DGRIVGEGYhqrAGGP--------------------------HAEVNAL 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1197977499  91 mNKNSTDVKGCSMYVALFPCNE------CAKLIIQAGIKEVIF-MSD 130
Cdd:COG0117    54 -AQAGEAARGATLYVTLEPCSHhgrtppCADALIEAGIKRVVIaMLD 99
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 32-130 1.87e-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: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  32 DPNSQVGACIVNSENKIVGIGYN---GMPngcsddvlpwrrtaenkldtkypyvcHAELNAIMNKNSTDVKGCSMYVALF 108
Cdd:cd01284    16 SPNPPVGCVIVDDDGEIVGEGYHrkaGGP--------------------------HAEVNALASAGEKLARGATLYVTLE 69

                          90       100
                  ....*....|....*....|....*....
gi 1197977499 109 PCNE------CAKLIIQAGIKEVIF-MSD 130
Cdd:cd01284    70 PCSHhgktppCVDAIIEAGIKRVVVgVRD 98
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 14-166 7.23e-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: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  14 EWPEYFMAVAFLSAQRSKDPNSQVGACIVNsENKIVGIGYNgmpngcsddvlpwrRTAENKLDTKypyvcHAELNAIM-- 91
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVK-DGKVIARGYN--------------RKELNADTTA-----HAEILAIQqa 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1197977499  92 -NKN-STDVKGCSMYVALFPCNECAKLIIQAGIKEVIF-MSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDF 166
Cdd:pfam14437  62 aKKLgSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYgAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGF 139
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 20-127 7.83e-11

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: 7.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  20 MAVAFLSAQRSKDPNSQ-VGACIVNSENKIVGIGYNgmpngcsddvlpwRRTAENklDTkypyVCHAELNAIMN----KN 94
Cdd:cd01285     1 MRLAIELARKALAEGEVpFGAVIVDDDGKVIARGHN-------------RVEQDG--DP----TAHAEIVAIRNaarrLG 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1197977499  95 STDVKGCSMYVALFPCNECAKLIIQAGIKEVIF 127
Cdd:cd01285    62 SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVY 94
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 33-130 7.60e-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: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197977499  33 PNSQVGACIVNSEnKIVGIGYNGMPNGCsddvlpwrrtaenkldtkypyvcHAELNAI-MNKNSTdvKGCSMYVALFPCN 111
Cdd:TIGR00326  17 PNPLVGCVIVKNG-EIVGEGAHQKAGEP-----------------------HAEVHALrQAGENA--KGATAYVTLEPCS 70

                          90       100
                  ....*....|....*....|....*.
gi 1197977499 112 E------CAKLIIQAGIKEVIF-MSD 130
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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