NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|291334222|gb|ADD93888|]
View 

predicted diaminohydroxyphosphoribosylaminopyrimidine deaminase [uncultured marine bacterium MedDCM-OCT-S08-C1463]

Protein Classification

dihydrofolate reductase family protein( domain architecture ID 106942)

dihydrofolate reductase family protein; similar to Lacticaseibacillus rhamnosus dihydrofolate reductase which reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DHFR super family cl17279
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 10-326 3.55e-74

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


The actual alignment was detected with superfamily member TIGR00326:

Pssm-ID: 473077 [Multi-domain]  Cd Length: 344  Bit Score: 232.80  E-value: 3.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   10 AISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKYKknylsklsGSDLFVTLEPCSKKGKT 89
Cdd:TIGR00326   4 ALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAK--------GATAYVTLEPCSHQGRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   90 GACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAGYELK-NLNNQQCQALNESFFHKVKSNKPFVRAKVAMSSDHKS 164
Cdd:TIGR00326  76 PPCAEAIIEAGIKKVVVSMQDPNPlvagRGAERLKQAGIEVTfGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  165 VFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKIIAnknfvQPERYVFSNSLNLNWSAPFFKLP 244
Cdd:TIGR00326 156 ATASGESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATE-----QPLRVVLDTQLRIPEFAKLIPQI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  245 GKKVVVTSKKNLPKLPQGInDISLMSLKKNSNslssEDFIKRISKLNVNNILIEAGPRLLGSFGDYGLIDEYIFYISPEK 324
Cdd:TIGR00326 231 APTWIFTTARDKKKRLEAF-EVNIFPLEKVTI----REVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKL 305


                  ..
gi 291334222  325 LG 326
Cdd:TIGR00326 306 LG 307
 
Name Accession Description Interval E-value
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 10-326 3.55e-74

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: 232.80  E-value: 3.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   10 AISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKYKknylsklsGSDLFVTLEPCSKKGKT 89
Cdd:TIGR00326   4 ALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAK--------GATAYVTLEPCSHQGRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   90 GACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAGYELK-NLNNQQCQALNESFFHKVKSNKPFVRAKVAMSSDHKS 164
Cdd:TIGR00326  76 PPCAEAIIEAGIKKVVVSMQDPNPlvagRGAERLKQAGIEVTfGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  165 VFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKIIAnknfvQPERYVFSNSLNLNWSAPFFKLP 244
Cdd:TIGR00326 156 ATASGESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATE-----QPLRVVLDTQLRIPEFAKLIPQI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  245 GKKVVVTSKKNLPKLPQGInDISLMSLKKNSNslssEDFIKRISKLNVNNILIEAGPRLLGSFGDYGLIDEYIFYISPEK 324
Cdd:TIGR00326 231 APTWIFTTARDKKKRLEAF-EVNIFPLEKVTI----REVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKL 305


                  ..
gi 291334222  325 LG 326
Cdd:TIGR00326 306 LG 307
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 5-210 5.77e-71

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: 223.40  E-value: 5.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   5 FFISEAISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKykknylskLSGSDLFVTLEPCS 84
Cdd:COG0117    2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEA--------ARGATLYVTLEPCS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  85 KKGKTGACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAGYELK-NLNNQQCQALNESFFHKVKSNKPFVRAKVAMS 159
Cdd:COG0117   74 HHGRTPPCADALIEAGIKRVVIAMLDPNPlvagKGIARLRAAGIEVEvGVLEEEARALNRGFLKRMRTGRPFVTLKLAMS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 291334222 160 SDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVR 210
Cdd:COG0117  154 LDGKIATANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVR 204
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 1-329 9.91e-60

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 196.14  E-value: 9.91e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   1 MSDSFFISEAISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKYKknylsklsGSDLFVTL 80
Cdd:PRK10786   1 MQDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAK--------GATAYVTL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  81 EPCSKKGKTGACVNELKKYDFKRIVVGTKDPTQN----GINNLQSAGYELKN-LNNQQCQALNESFFHKVKSNKPFVRAK 155
Cdd:PRK10786  73 EPCSHHGRTPPCCDALIAAGVARVVAAMQDPNPQvagrGLYRLQQAGIDVSHgLMMSEAEALNKGFLKRMRTGFPYIQLK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 156 VAMSSDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVR-------SKKIIANKNFVQPERYVF 228
Cdd:PRK10786 153 LGASLDGRTAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRwseldaqTQALYPQENLRQPVRIVI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 229 SNSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGINDIslmSLKKNSNSLSSEDFIKRISKLNVNNILIEAGPRLLGSFG 308
Cdd:PRK10786 233 DSQNRVTPEHRIVQQPGETWLARTQEDSREWPETVRTL---LLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALL 309

                        330       340
                 ....*....|....*....|.
gi 291334222 309 DYGLIDEYIFYISPEKLGTKA 329
Cdd:PRK10786 310 QAGLVDELIVYIAPKLLGSDA 330
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 10-123 2.04e-32

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: 116.95  E-value: 2.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  10 AISLGLKGRFTAKPGVKVGCVIVKEN-RIIGRGFYEKYGGSHAEINAINDVKEKykknylsKLSGSDLFVTLEPCSKKGK 88
Cdd:cd01284    4 ALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEK-------LARGATLYVTLEPCSHHGK 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 291334222  89 TGACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAG 123
Cdd:cd01284   77 TPPCVDAIIEAGIKRVVVGVRDPNPlvagKGAERLRAAG 115
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
 150-326 2.60e-27

RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.


Pssm-ID: 396444  Cd Length: 196  Bit Score: 106.31  E-value: 2.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  150 PFVRAKVAMSSDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKiiANKNFVQPERYVFS 229
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVK--GRAAERQPPRVVVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  230 NSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGINDIslmslkknsnSLSSEDFIKRISKLNVNNILIEAGPRLLGSFGD 309
Cdd:pfam01872  79 STLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL----------RVDLKELLRELKERGIRSLLVEGGATLAGSLLR 148

                         170
                  ....*....|....*..
gi 291334222  310 YGLIDEYIFYISPEKLG 326
Cdd:pfam01872 149 AGLVDELRLYIAPKLLG 165
 
Name Accession Description Interval E-value
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 10-326 3.55e-74

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: 232.80  E-value: 3.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   10 AISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKYKknylsklsGSDLFVTLEPCSKKGKT 89
Cdd:TIGR00326   4 ALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAK--------GATAYVTLEPCSHQGRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   90 GACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAGYELK-NLNNQQCQALNESFFHKVKSNKPFVRAKVAMSSDHKS 164
Cdd:TIGR00326  76 PPCAEAIIEAGIKKVVVSMQDPNPlvagRGAERLKQAGIEVTfGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  165 VFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKIIAnknfvQPERYVFSNSLNLNWSAPFFKLP 244
Cdd:TIGR00326 156 ATASGESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATE-----QPLRVVLDTQLRIPEFAKLIPQI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  245 GKKVVVTSKKNLPKLPQGInDISLMSLKKNSNslssEDFIKRISKLNVNNILIEAGPRLLGSFGDYGLIDEYIFYISPEK 324
Cdd:TIGR00326 231 APTWIFTTARDKKKRLEAF-EVNIFPLEKVTI----REVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKL 305


                  ..
gi 291334222  325 LG 326
Cdd:TIGR00326 306 LG 307
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 5-210 5.77e-71

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: 223.40  E-value: 5.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   5 FFISEAISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKykknylskLSGSDLFVTLEPCS 84
Cdd:COG0117    2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEA--------ARGATLYVTLEPCS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  85 KKGKTGACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAGYELK-NLNNQQCQALNESFFHKVKSNKPFVRAKVAMS 159
Cdd:COG0117   74 HHGRTPPCADALIEAGIKRVVIAMLDPNPlvagKGIARLRAAGIEVEvGVLEEEARALNRGFLKRMRTGRPFVTLKLAMS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 291334222 160 SDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVR 210
Cdd:COG0117  154 LDGKIATANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVR 204
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 1-329 9.91e-60

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 196.14  E-value: 9.91e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   1 MSDSFFISEAISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKYKknylsklsGSDLFVTL 80
Cdd:PRK10786   1 MQDEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAK--------GATAYVTL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  81 EPCSKKGKTGACVNELKKYDFKRIVVGTKDPTQN----GINNLQSAGYELKN-LNNQQCQALNESFFHKVKSNKPFVRAK 155
Cdd:PRK10786  73 EPCSHHGRTPPCCDALIAAGVARVVAAMQDPNPQvagrGLYRLQQAGIDVSHgLMMSEAEALNKGFLKRMRTGFPYIQLK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 156 VAMSSDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVR-------SKKIIANKNFVQPERYVF 228
Cdd:PRK10786 153 LGASLDGRTAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRwseldaqTQALYPQENLRQPVRIVI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 229 SNSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGINDIslmSLKKNSNSLSSEDFIKRISKLNVNNILIEAGPRLLGSFG 308
Cdd:PRK10786 233 DSQNRVTPEHRIVQQPGETWLARTQEDSREWPETVRTL---LLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALL 309

                        330       340
                 ....*....|....*....|.
gi 291334222 309 DYGLIDEYIFYISPEKLGTKA 329
Cdd:PRK10786 310 QAGLVDELIVYIAPKLLGSDA 330
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
 148-335 1.59e-41

Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine reductase, riboflavin biosynthesis is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 441588  Cd Length: 217  Bit Score: 144.15  E-value: 1.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 148 NKPFVRAKVAMSSDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKIIAnknfvQPERYV 227
Cdd:COG1985    2 GRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGLGR-----QPLRVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 228 FSNSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGIND--ISLMSLKKNsNSLSSEDFIKRISKLNVNNILIEAGPRLLG 305
Cdd:COG1985   77 VDSSLRLPPDARLFDDAAPTLVLTTEAADAERRAALEAagAEVIVLPGD-GRVDLAALLAALAERGIRSVLVEGGPTLAG 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 291334222 306 SFGDYGLIDEYIFYISPEKLGTKALHFYGG 335
Cdd:COG1985  156 SFLAAGLVDELILYIAPKLLGGDGPTLVGG 185
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 10-123 2.04e-32

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: 116.95  E-value: 2.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  10 AISLGLKGRFTAKPGVKVGCVIVKEN-RIIGRGFYEKYGGSHAEINAINDVKEKykknylsKLSGSDLFVTLEPCSKKGK 88
Cdd:cd01284    4 ALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEK-------LARGATLYVTLEPCSHHGK 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 291334222  89 TGACVNELKKYDFKRIVVGTKDPTQ----NGINNLQSAG 123
Cdd:cd01284   77 TPPCVDAIIEAGIKRVVVGVRDPNPlvagKGAERLRAAG 115
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 3-161 1.88e-29

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 116.41  E-value: 1.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   3 DSFFISEAISLGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEKYGGSHAEINAINDVKEKYKknylsklsGSDLFVTLEP 82
Cdd:PLN02807  32 DSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAE--------NATAYVSLEP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  83 CSKKGKTGACVNELKKYDFKRIVVGTKDPT----QNGINNLQSAGYELK-NLNNQQCQALNESFFHKVKSNKPFVRAKVA 157
Cdd:PLN02807 104 CNHYGRTPPCTEALIKAKVKRVVVGMVDPNpivaSKGIERLRDAGIEVTvGVEEELCRKLNEAFIHRMLTGKPFVTLRYS 183


                 ....
gi 291334222 158 MSSD 161
Cdd:PLN02807 184 MSMN 187
ribD_Cterm TIGR00227
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ...
 149-329 7.32e-28

riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases have a zinc-binding domain recognized by the dCMP_cyt_deam model toward the N-terminus and this domain toward the C-terminus. Yeast HTP reductase, a riboflavin-biosynthetic enzyme, and several archaeal proteins believed related to riboflavin biosynthesis consist only of this domain and lack the dCMP_cyt_deam domain.


Pssm-ID: 129330 [Multi-domain]  Cd Length: 216  Bit Score: 108.24  E-value: 7.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  149 KPFVRAKVAMSSDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKIIANKNfvqPERYVF 228
Cdd:TIGR00227   2 RPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRWVELDELRN---PVRVVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  229 SNSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGINDISLMSLKKNSNSLSSEDFIKRISKLNVNNILIEAGPRLLGSFG 308
Cdd:TIGR00227  79 DSRLRVPPTARLLNDDAPTWVATSEPADEEKVKELEDFGVEVLVLETKRVDLKKLMEILYEEGIRSVMVEGGGTLNGSLL 158

                         170       180
                  ....*....|....*....|.
gi 291334222  309 DYGLIDEYIFYISPEKLGTKA 329
Cdd:TIGR00227 159 KEGLVDELIVYIAPKLLGGRD 179
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
 150-326 2.60e-27

RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.


Pssm-ID: 396444  Cd Length: 196  Bit Score: 106.31  E-value: 2.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  150 PFVRAKVAMSSDHKSVFASKQRKWITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKiiANKNFVQPERYVFS 229
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVK--GRAAERQPPRVVVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  230 NSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGINDIslmslkknsnSLSSEDFIKRISKLNVNNILIEAGPRLLGSFGD 309
Cdd:pfam01872  79 STLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL----------RVDLKELLRELKERGIRSLLVEGGATLAGSLLR 148

                         170
                  ....*....|....*..
gi 291334222  310 YGLIDEYIFYISPEKLG 326
Cdd:pfam01872 149 AGLVDELRLYIAPKLLG 165
PRK05625 PRK05625
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
 149-328 1.80e-16

5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated


Pssm-ID: 180169  Cd Length: 217  Bit Score: 77.21  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 149 KPFVRAKVAMSSDHKsvFASKQRKW-ITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVrsKKIIANKNfVQPERYV 227
Cdd:PRK05625   2 RPYVIVNAAMSADGK--LATKTRYSrISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTV--HRYAAGKP-ENPIRVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 228 FSNSLNLNWSAPFFKLPGKKVVVTSKKNLPKlpqgindiSLMSLKK--------NSNSLSSEDFIKRISKLNVNNILIEA 299
Cdd:PRK05625  77 VDSSARTPPDARILDGPAKTIVAVSEAAPSE--------KVEELEKkgaevivaGGERVDLPDLLEDLYERGIKRLMVEG 148

                        170       180
                 ....*....|....*....|....*....
gi 291334222 300 GPRLLGSFGDYGLIDEYIFYISPEKLGTK 328
Cdd:PRK05625 149 GGTLIWSMFKEGLVDEVRVTVGPKIIGGK 177
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
3-107 4.06e-15

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 70.02  E-value: 4.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222    3 DSFFISEAISLGLKGRftAKPGVKVGCVIVKEN-RIIGRGFYEKYGGS----HAEINAINDVKekyKKNYLSKLSGSDLF 77
Cdd:pfam00383   2 DEYFMRLALKAAKRAY--PYSNFPVGAVIVKKDgEIIATGYNGENAGYdptiHAERNAIRQAG---KRGEGVRLEGATLY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 291334222   78 VTLEPCskkgktGACVNELKKYDFKRIVVG 107
Cdd:pfam00383  77 VTLEPC------GMCAQAIIESGIKRVVFG 100
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-111 4.40e-14

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: 68.61  E-value: 4.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   1 MSDSFFISEAISLGLKGRftAKPGVKVGCVIVKENRIIGRGFYEKYGGS----HAEINAINDVkEKYKKNYlsKLSGSDL 76
Cdd:COG0590    2 EDDEEFMRRALELARKAV--AEGEVPVGAVLVKDGEIIARGHNRVETLNdptaHAEILAIRAA-ARKLGNW--RLSGCTL 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 291334222  77 FVTLEP---CSkkgktGACVNelkkYDFKRIVVGTKDP 111
Cdd:COG0590   77 YVTLEPcpmCA-----GAIVW----ARIGRVVYGASDP 105
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 13-111 3.66e-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: 63.31  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   13 LGLKGRFTAKPGVKVGCVIVKENRIIGRGFYEK----YGGSHAEINAINdvkEKYKKNYLSKLSGSDLFVTLEPCskkgk 88
Cdd:pfam14437  11 LGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKelnaDTTAHAEILAIQ---QAAKKLGSWRLDDATLYVTLEPC----- 82

                          90       100
                  ....*....|....*....|...
gi 291334222   89 tGACVNELKKYDFKRIVVGTKDP 111
Cdd:pfam14437  83 -PMCAGAIVQAGLKSLVYGAGNP 104
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 24-119 2.24e-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: 57.24  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  24 GVKVGCVIV-KENRIIGRGFYEKYGGS----HAEINAINDVKEKYKKNYLSklsGSDLFVTLEPCSKkgKTGACVnelkK 98
Cdd:cd01285   16 EVPFGAVIVdDDGKVIARGHNRVEQDGdptaHAEIVAIRNAARRLGSYLLS---GCTLYTTLEPCPM--CAGALL----W 86

                         90       100
                 ....*....|....*....|.
gi 291334222  99 YDFKRIVVGTKDPTQNGINNL 119
Cdd:cd01285   87 ARIKRVVYGASDPKLGGIGFL 107
PRK14719 PRK14719
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
 150-326 5.63e-10

bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional


Pssm-ID: 237801 [Multi-domain]  Cd Length: 360  Bit Score: 59.95  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 150 PFVRAKVAMSSDHKSVFASKQRKwITGIPARNNVQTLRAEADIILTGAGTINEDNPSMNVRSKKIIANKNfvqPERYVFS 229
Cdd:PRK14719 140 PYVISNVGMTLDGKLATIENDSR-ISGENDLKRVHEIRKDVDAIMVGIGTVLKDDPRLTVHKINASPKDN---PLRIVVD 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222 230 NSLNLNWSAPFFKLPGKKVVVTSKKNLPKLPQGI---NDISLMSLKKNSNSLSSEDFIKRISKLNVNNILIEAGPRL-LG 305
Cdd:PRK14719 216 SNLKIPLNARVLNKDAKTVIATTTPISDEKEEKIrklKEMGITVLQAGVQKVDLRKIMNEIYKMGINKILLEGGGTLnWG 295

                        170       180
                 ....*....|....*....|.
gi 291334222 306 SFGDyGLIDEYIFYISPEKLG 326
Cdd:PRK14719 296 MFKE-NLINEVRVYIAPKVFG 315
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 23-84 3.99e-07

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: 48.42  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  23 PGVKVGCVIVKENRIIGRGfyekYGGS-----------------------------HAEINAI-NDVKEKykknylSKLS 72
Cdd:cd01286   18 PRRQVGAVIVKDKRIISTG----YNGSpsglphcaevgcerddlpsgedqkccrtvHAEQNAIlQAARHG------VSLE 87

                         90
                 ....*....|..
gi 291334222  73 GSDLFVTLEPCS 84
Cdd:cd01286   88 GATLYVTLFPCI 99
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 2-110 1.17e-05

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 45.18  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222   2 SDSFFISEAISLGLKGRftAKPGVKVGCVIVKENRIIGRGFYEKYG----GSHAEINAINDVKEKYKkNYlsKLSGSDLF 77
Cdd:PRK10860  12 SHEYWMRHALTLAKRAW--DEREVPVGAVLVHNNRVIGEGWNRPIGrhdpTAHAEIMALRQGGLVLQ-NY--RLLDATLY 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 291334222  78 VTLEPCSkkgktgACVNELKKYDFKRIVVGTKD 110
Cdd:PRK10860  87 VTLEPCV------MCAGAMVHSRIGRLVFGARD 113
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 23-106 1.61e-05

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: 42.92  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291334222  23 PGVKVGCVIVKENR--IIGRGF---YEKYGGS-HAEINAIndvkekYKKNYLSKLSGSDLFVTLEPCskkgktGACVNEL 96
Cdd:cd00786   16 SNFQVGACLVNKKDggKVGRGCnieNAAYSMCnHAERTAL------FNAGSEGDTKGQMLYVALSPC------GACAQLI 83

                         90
                 ....*....|
gi 291334222  97 KKYDFKRIVV 106
Cdd:cd00786   84 IELGIKDVIV 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH