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Conserved domains on  [gi|42565719|ref|NP_190423|]
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Cytidine/deoxycytidylate deaminase family protein [Arabidopsis thaliana]

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];
61-215 4.21e-56

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 175.80  E-value: 4.21e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  61 KRNGYLSWDDYFMAIAFLSAERSKDPNRQVGACLVsQNGVILGIGYNGFPRGCSDDKLP-WA-KKSRTGDPLETKYPYVC 138
Cdd:COG2131   1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLrEKLGIPSGERGECCRTV 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42565719 139 HAEVNAILNT--NHASAAGQKLYVTMFPCNECAKIILQSGVAEVIYfVEKRPNDsdvayvASHKLLSMANVKVRKHQPE 215
Cdd:COG2131  80 HAEQNAILQAarHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVY-LEDYPDE------LAKELLKEAGVEVRQLELE 151
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
61-215 4.21e-56

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 175.80  E-value: 4.21e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  61 KRNGYLSWDDYFMAIAFLSAERSKDPNRQVGACLVsQNGVILGIGYNGFPRGCSDDKLP-WA-KKSRTGDPLETKYPYVC 138
Cdd:COG2131   1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLrEKLGIPSGERGECCRTV 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42565719 139 HAEVNAILNT--NHASAAGQKLYVTMFPCNECAKIILQSGVAEVIYfVEKRPNDsdvayvASHKLLSMANVKVRKHQPE 215
Cdd:COG2131  80 HAEQNAILQAarHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVY-LEDYPDE------LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 69-182 3.57e-51

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: 162.44  E-value: 3.57e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  69 DDYFMAIAFLSAERSKDPNRQVGACLVSQNGVIlGIGYNGFPRGCSDDKLPWAKKSRTGDPLETKYPYVCHAEVNAILNT 148
Cdd:cd01286   1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRII-STGYNGSPSGLPHCAEVGCERDDLPSGEDQKCCRTVHAEQNAILQA 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 42565719 149 --NHASAAGQKLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:cd01286  80 arHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
68-182 1.49e-27

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 100.84  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719    68 WDDYFMAIAFLSAERS-KDPNRQVGACLVSQNGVILGIGYNGFPRGcsddklpwakksrtgdpletkYPYVCHAEVNAIL 146
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG---------------------YDPTIHAERNAIR 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 42565719   147 N----TNHASAAGQKLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:pfam00383  60 QagkrGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cd PHA02588
deoxycytidylate deaminase; Provisional
 72-182 8.04e-19

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 80.19  E-value: 8.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719   72 FMAIAFLSAERSKDPNRQVGAcLVSQNGVILGIGYNGFPRG---CSD--DKLPWAKKsrTGDPLETKYP--------YVC 138
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGA-VIEKNGRIISTGYNGTPAGgvnCCDhaNEQGWLDD--EGKLKKEHRPehsawsskNEI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 42565719  139 HAEVNAIL--NTNHASAAGQKLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:PHA02588  83 HAELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVY 128
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 69-182 1.14e-15

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: 75.29  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719   69 DDYFMAIAFLSAERSKDPNRQVGACLVSQNGVILGIGYNGFPR--------------------GCSDD------------ 116
Cdd:NF041025 219 DERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPKaggglywpgdepdhrdyslgYDRNDeekrkiiedilk 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  117 KLPWA--------------------KKSRTGDPLEtkYPYVCHAEVNAILntnhaSAA-------GQKLYVTMFPCNECA 169
Cdd:NF041025 299 RLADAgseslkkkgrnasecfklilKKSRIKDLIE--FGRAVHAEMNAIL-----SAArlggstkGGTLYTTTFPCHNCA 371

                        170
                 ....*....|...
gi 42565719  170 KIILQSGVAEVIY 182
Cdd:NF041025 372 KHIVAAGIKRVVY 384
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 86-189 7.50e-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: 54.83  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719    86 PNRQVGaCLVSQNGVILGIGYNgfprgcsddklpwakkSRTGDPletkypyvcHAEVNAIlntNHA--SAAGQKLYVTMF 163
Cdd:TIGR00326  17 PNPLVG-CVIVKNGEIVGEGAH----------------QKAGEP---------HAEVHAL---RQAgeNAKGATAYVTLE 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 42565719   164 PCNE------CAKIILQSGVAEVIYFVeKRPN 189
Cdd:TIGR00326  68 PCSHqgrtppCAEAIIEAGIKKVVVSM-QDPN 98
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
61-215 4.21e-56

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 175.80  E-value: 4.21e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  61 KRNGYLSWDDYFMAIAFLSAERSKDPNRQVGACLVsQNGVILGIGYNGFPRGCSDDKLP-WA-KKSRTGDPLETKYPYVC 138
Cdd:COG2131   1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLrEKLGIPSGERGECCRTV 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42565719 139 HAEVNAILNT--NHASAAGQKLYVTMFPCNECAKIILQSGVAEVIYfVEKRPNDsdvayvASHKLLSMANVKVRKHQPE 215
Cdd:COG2131  80 HAEQNAILQAarHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVY-LEDYPDE------LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 69-182 3.57e-51

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: 162.44  E-value: 3.57e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  69 DDYFMAIAFLSAERSKDPNRQVGACLVSQNGVIlGIGYNGFPRGCSDDKLPWAKKSRTGDPLETKYPYVCHAEVNAILNT 148
Cdd:cd01286   1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRII-STGYNGSPSGLPHCAEVGCERDDLPSGEDQKCCRTVHAEQNAILQA 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 42565719 149 --NHASAAGQKLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:cd01286  80 arHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
68-182 1.49e-27

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 100.84  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719    68 WDDYFMAIAFLSAERS-KDPNRQVGACLVSQNGVILGIGYNGFPRGcsddklpwakksrtgdpletkYPYVCHAEVNAIL 146
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG---------------------YDPTIHAERNAIR 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 42565719   147 N----TNHASAAGQKLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:pfam00383  60 QagkrGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 70-184 3.49e-27

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: 99.93  E-value: 3.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  70 DYFMAIAFLSAerSKDPNRQVGACLVSQNGvilgigYNGFPRGCSDDKLPwakksrtgdpletkYPYVCHAEVNAILNTN 149
Cdd:cd00786   2 TEALKAADLGY--AKESNFQVGACLVNKKD------GGKVGRGCNIENAA--------------YSMCNHAERTALFNAG 59

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 42565719 150 -HASAAGQKLYVTMFPCNECAKIILQSGVAEVIYFV 184
Cdd:cd00786  60 sEGDTKGQMLYVALSPCGACAQLIIELGIKDVIVVL 95
cd PHA02588
deoxycytidylate deaminase; Provisional
 72-182 8.04e-19

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 80.19  E-value: 8.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719   72 FMAIAFLSAERSKDPNRQVGAcLVSQNGVILGIGYNGFPRG---CSD--DKLPWAKKsrTGDPLETKYP--------YVC 138
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGA-VIEKNGRIISTGYNGTPAGgvnCCDhaNEQGWLDD--EGKLKKEHRPehsawsskNEI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 42565719  139 HAEVNAIL--NTNHASAAGQKLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:PHA02588  83 HAELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVY 128
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 69-182 1.14e-15

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: 75.29  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719   69 DDYFMAIAFLSAERSKDPNRQVGACLVSQNGVILGIGYNGFPR--------------------GCSDD------------ 116
Cdd:NF041025 219 DERGMYAAFSAALRSACLSRQVGAAITDKDGEIISTGWNDVPKaggglywpgdepdhrdyslgYDRNDeekrkiiedilk 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  117 KLPWA--------------------KKSRTGDPLEtkYPYVCHAEVNAILntnhaSAA-------GQKLYVTMFPCNECA 169
Cdd:NF041025 299 RLADAgseslkkkgrnasecfklilKKSRIKDLIE--FGRAVHAEMNAIL-----SAArlggstkGGTLYTTTFPCHNCA 371

                        170
                 ....*....|...
gi 42565719  170 KIILQSGVAEVIY 182
Cdd:NF041025 372 KHIVAAGIKRVVY 384
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 71-182 2.16e-11

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: 62.38  E-value: 2.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  71 YFMAIAFLSAERSK---DPNRQVGACLVsQNGVILGIGYNgfprgcsddklpwakkSRTGDPletkypyvcHAEVNAIln 147
Cdd:COG0117   2 RYMRRALELARRGLgttSPNPLVGCVIV-KDGRIVGEGYH----------------QRAGGP---------HAEVNAL-- 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 42565719 148 tNHA--SAAGQKLYVTMFPCNE------CAKIILQSGVAEVIY 182
Cdd:COG0117  54 -AQAgeAARGATLYVTLEPCSHhgrtppCADALIEAGIKRVVI 95
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 85-182 3.10e-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: 58.40  E-value: 3.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  85 DPNRQVGACLVSQNGVILGIGYNgfprgcsddklpwakkSRTGDPletkypyvcHAEVNAILNTNHASAAGQKLYVTMFP 164
Cdd:cd01284  16 SPNPPVGCVIVDDDGEIVGEGYH----------------RKAGGP---------HAEVNALASAGEKLARGATLYVTLEP 70

                        90       100
                ....*....|....*....|....
gi 42565719 165 CNE------CAKIILQSGVAEVIY 182
Cdd:cd01284  71 CSHhgktppCVDAIIEAGIKRVVV 94
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 67-223 1.72e-10

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: 57.15  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719    67 SWDDYFMAIAFLSAERSKDPNRQVGAcLVSQNGVILGIGYNgfprgcsddklpwaKKSRTGDPLEtkypyvcHAEVNAIl 146
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVPIGA-VIVKDGKVIARGYN--------------RKELNADTTA-------HAEILAI- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719   147 ntNHASAAGQK-------LYVTMFPCNECAKIILQSGVAEVIYFVEKrPNDSDVAYVASHKLLSMANVKVRKHQPEMDEI 219
Cdd:pfam14437  59 --QQAAKKLGSwrlddatLYVTLEPCPMCAGAIVQAGLKSLVYGAGN-PKGGAVGSVLNKLVIVLWNHRVELVEEDCSEI 135


                  ....
gi 42565719   220 LIKF 223
Cdd:pfam14437 136 LKGF 139
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 86-189 7.50e-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: 54.83  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719    86 PNRQVGaCLVSQNGVILGIGYNgfprgcsddklpwakkSRTGDPletkypyvcHAEVNAIlntNHA--SAAGQKLYVTMF 163
Cdd:TIGR00326  17 PNPLVG-CVIVKNGEIVGEGAH----------------QKAGEP---------HAEVHAL---RQAgeNAKGATAYVTLE 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 42565719   164 PCNE------CAKIILQSGVAEVIYFVeKRPN 189
Cdd:TIGR00326  68 PCSHqgrtppCAEAIIEAGIKKVVVSM-QDPN 98
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 73-182 5.03e-08

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: 49.54  E-value: 5.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719  73 MAIAFLSAERSKDPNRQ-VGACLVSQNGVILGIGYNgfprgcsddklpwaKKSRTGDPLetkypyvCHAEVNAILNtnha 151
Cdd:cd01285   1 MRLAIELARKALAEGEVpFGAVIVDDDGKVIARGHN--------------RVEQDGDPT-------AHAEIVAIRN---- 55

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42565719 152 saAGQK----------LYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:cd01285  56 --AARRlgsyllsgctLYTTLEPCPMCAGALLWARIKRVVY 94
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 69-182 4.02e-03

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 37.09  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565719   69 DDYFMAIAFLSAERSKDPNR-QVGACLVSQNGVIlGIGYNGfPRGCSDdklPWAkksrtgdpletkypyvcHAEVNAI-- 145
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDEREvPVGAVLVHNNRVI-GEGWNR-PIGRHD---PTA-----------------HAEIMALrq 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 42565719  146 ----------LNTNhasaagqkLYVTMFPCNECAKIILQSGVAEVIY 182
Cdd:PRK10860  71 gglvlqnyrlLDAT--------LYVTLEPCVMCAGAMVHSRIGRLVF 109
 
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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