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Conserved domains on  [gi|238859563|ref|NP_001154984|]
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deoxycytidylate deaminase isoform 2 [Rattus norvegicus]

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
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];
14-126 1.60e-48

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 154.23  E-value: 1.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  14 KRDDYLEWPEYFMAVAFLSAQRSKDPSSQVGACIVnTENKIVGIGYNGMPNGCSDDLLP-WRRTAENKL---DTKYPYVC 89
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 238859563  90 HAELNAIMN--KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:COG2131   80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQA 118
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
14-126 1.60e-48

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 154.23  E-value: 1.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  14 KRDDYLEWPEYFMAVAFLSAQRSKDPSSQVGACIVnTENKIVGIGYNGMPNGCSDDLLP-WRRTAENKL---DTKYPYVC 89
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 238859563  90 HAELNAIMN--KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:COG2131   80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQA 118
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
23-126 2.96e-47

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: 150.12  E-value: 2.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  23 EYFMAVAFLSAQRSKDPSSQVGACIVNtENKIVGIGYNGMPNGCSDDLLPWRRTAE--NKLDTKYPYVCHAELNAIMN-- 98
Cdd:cd01286    2 EYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVGCERDDlpSGEDQKCCRTVHAEQNAILQaa 80
                         90       100
                 ....*....|....*....|....*...
gi 238859563  99 KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:cd01286   81 RHGVSLEGATLYVTLFPCIECAKLIIQA 108
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
21-126 2.10e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 96.22  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563   21 WPEYFMAVAFLSAQRS-KDPSSQVGACIVNTENKIVGIGYNGMPNGcsddllpwrrtaenkldtkYPYVCHAELNAIMN- 98
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG-------------------YDPTIHAERNAIRQa 61
                          90       100       110
                  ....*....|....*....|....*....|.
gi 238859563   99 ---KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:pfam00383  62 gkrGEGVRLEGATLYVTLEPCGMCAQAIIES 92
cd PHA02588
deoxycytidylate deaminase; Provisional
25-126 3.45e-17

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 74.41  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  25 FMAVAFLSAQRSKDPSSQVGACIVNtENKIVGIGYNGMPNG---CSD------------DLLPWRRTAENKLDTKYpyVC 89
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGgvnCCDhaneqgwlddegKLKKEHRPEHSAWSSKN--EI 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 238859563  90 HAELNAIM--NKNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:PHA02588  83 HAELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQS 121
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
23-126 1.10e-12

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: 64.89  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  23 EYFMAVAFLSAQRSKDPSSQVGACIVNTENKIVGIGYNGMP--------------------NGCS---------DDLLPW 73
Cdd:NF041025 220 ERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPkaggglywpgdepdhrdyslGYDRndeekrkiiEDILKR 299
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238859563  74 -------------------RRTAENKLDTK----YPYVCHAELNAIMN--KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:NF041025 300 ladagseslkkkgrnasecFKLILKKSRIKdlieFGRAVHAEMNAILSaaRLGGSTKGGTLYTTTFPCHNCAKHIVAA 377
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
14-126 1.60e-48

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 154.23  E-value: 1.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  14 KRDDYLEWPEYFMAVAFLSAQRSKDPSSQVGACIVnTENKIVGIGYNGMPNGCSDDLLP-WRRTAENKL---DTKYPYVC 89
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIPsgeRGECCRTV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 238859563  90 HAELNAIMN--KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:COG2131   80 HAEQNAILQaaRHGVSTEGATLYVTHFPCLECAKMIIQA 118
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
23-126 2.96e-47

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: 150.12  E-value: 2.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  23 EYFMAVAFLSAQRSKDPSSQVGACIVNtENKIVGIGYNGMPNGCSDDLLPWRRTAE--NKLDTKYPYVCHAELNAIMN-- 98
Cdd:cd01286    2 EYFMAIARLAALRSTCPRRQVGAVIVK-DKRIISTGYNGSPSGLPHCAEVGCERDDlpSGEDQKCCRTVHAEQNAILQaa 80
                         90       100
                 ....*....|....*....|....*...
gi 238859563  99 KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:cd01286   81 RHGVSLEGATLYVTLFPCIECAKLIIQA 108
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
22-126 1.11e-32

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: 112.26  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  22 PEYFMAVAFLSAQrsKDPSSQVGACIVNTEnkivgiGYNGMPNGCSDDLLPwrrtaenkldtkYPYVCHAELNAIMNKNS 101
Cdd:cd00786    1 MTEALKAADLGYA--KESNFQVGACLVNKK------DGGKVGRGCNIENAA------------YSMCNHAERTALFNAGS 60
                         90       100
                 ....*....|....*....|....*.
gi 238859563 102 -ADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:cd00786   61 eGDTKGQMLYVALSPCGACAQLIIEL 86
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
21-126 2.10e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 96.22  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563   21 WPEYFMAVAFLSAQRS-KDPSSQVGACIVNTENKIVGIGYNGMPNGcsddllpwrrtaenkldtkYPYVCHAELNAIMN- 98
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG-------------------YDPTIHAERNAIRQa 61
                          90       100       110
                  ....*....|....*....|....*....|.
gi 238859563   99 ---KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:pfam00383  62 gkrGEGVRLEGATLYVTLEPCGMCAQAIIES 92
cd PHA02588
deoxycytidylate deaminase; Provisional
25-126 3.45e-17

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 74.41  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  25 FMAVAFLSAQRSKDPSSQVGACIVNtENKIVGIGYNGMPNG---CSD------------DLLPWRRTAENKLDTKYpyVC 89
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEK-NGRIISTGYNGTPAGgvnCCDhaneqgwlddegKLKKEHRPEHSAWSSKN--EI 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 238859563  90 HAELNAIM--NKNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:PHA02588  83 HAELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQS 121
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
23-126 1.10e-12

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: 64.89  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  23 EYFMAVAFLSAQRSKDPSSQVGACIVNTENKIVGIGYNGMP--------------------NGCS---------DDLLPW 73
Cdd:NF041025 220 ERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPkaggglywpgdepdhrdyslGYDRndeekrkiiEDILKR 299
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238859563  74 -------------------RRTAENKLDTK----YPYVCHAELNAIMN--KNSADVKGCSMYVALFPCNECAKLIIQA 126
Cdd:NF041025 300 ladagseslkkkgrnasecFKLILKKSRIKdlieFGRAVHAEMNAILSaaRLGGSTKGGTLYTTTFPCHNCAKHIVAA 377
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
23-126 2.88e-08

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: 51.60  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  23 EYFMAVAFLSAQRSK---DPSSQVGACIVNtENKIVGIGY---NGMPngcsddllpwrrtaenkldtkypyvcHAELNAI 96
Cdd:COG0117    1 ERYMRRALELARRGLgttSPNPLVGCVIVK-DGRIVGEGYhqrAGGP--------------------------HAEVNAL 53
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 238859563  97 mnkNSA--DVKGCSMYVALFPCNE------CAKLIIQA 126
Cdd:COG0117   54 ---AQAgeAARGATLYVTLEPCSHhgrtppCADALIEA 88
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
20-126 4.27e-08

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: 49.83  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563   20 EWPEYFMAVAFLSAQRSKDPSSQVGACIVNtENKIVGIGYNgmpngcsddllpwrRTAENKLDTKypyvcHAELNAIM-- 97
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGAVIVK-DGKVIARGYN--------------RKELNADTTA-----HAEILAIQqa 61
                          90       100       110
                  ....*....|....*....|....*....|.
gi 238859563   98 -NKNSA-DVKGCSMYVALFPCNECAKLIIQA 126
Cdd:pfam14437  62 aKKLGSwRLDDATLYVTLEPCPMCAGAIVQA 92
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
38-126 7.46e-07

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: 45.69  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859563  38 DPSSQVGACIVNTENKIVGIGYN---GMPngcsddllpwrrtaenkldtkypyvcHAELNAIMNKNSADVKGCSMYVALF 114
Cdd:cd01284   16 SPNPPVGCVIVDDDGEIVGEGYHrkaGGP--------------------------HAEVNALASAGEKLARGATLYVTLE 69
                         90
                 ....*....|....*...
gi 238859563 115 PCNE------CAKLIIQA 126
Cdd:cd01284   70 PCSHhgktppCVDAIIEA 87
 
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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