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Conserved domains on  [gi|449441472|ref|XP_004138506|]
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riboflavin biosynthesis protein PYRD, chloroplastic [Cucumis sativus]

Protein Classification

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase( domain architecture ID 11477156)

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase catalyzes steps in the riboflavin biosynthesis pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 64-422 0e+00

diaminohydroxyphosphoribosylaminopyrimidine deaminase


:

Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 552.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  64 GGHSVRCvnviQGVHCDVDDEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLA 143
Cdd:PLN02807  17 RRTSVRC----SARAAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 144 ENATAYVTLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQIL 223
Cdd:PLN02807  93 ENATAYVSLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRML 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 224 TGKPLLTLRYTLSLNGCFLDQVGKGAAEAGGYYSQLLQEYNAVIISpPSSSEEFEIPSSNEHGAKQPLWIIL-SSPDGLI 302
Cdd:PLN02807 173 TGKPFVTLRYSMSMNGCLLNQIGEGADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQEAGAKQPLRIIIaRSESSPL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 303 TVPRITDP-TTKVVIFTNKEVVV----SEREIETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLGVHEELIKEGIEEKL 377
Cdd:PLN02807 252 QIPSLREEsAAKVLVLADKESSAepvlRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGLESLLKDALEDKL 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 449441472 378 LQKVVVEVLPQWSESQS-ETWFKSMAENLKLKCLEPRMCGPSVVLE 422
Cdd:PLN02807 332 LQKVVVEVLPFWSGSQGqSIASFGGSQSFKLKRLTSREVGGSVVLE 377
 
Name Accession Description Interval E-value
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 64-422 0e+00

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 552.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  64 GGHSVRCvnviQGVHCDVDDEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLA 143
Cdd:PLN02807  17 RRTSVRC----SARAAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 144 ENATAYVTLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQIL 223
Cdd:PLN02807  93 ENATAYVSLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRML 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 224 TGKPLLTLRYTLSLNGCFLDQVGKGAAEAGGYYSQLLQEYNAVIISpPSSSEEFEIPSSNEHGAKQPLWIIL-SSPDGLI 302
Cdd:PLN02807 173 TGKPFVTLRYSMSMNGCLLNQIGEGADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQEAGAKQPLRIIIaRSESSPL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 303 TVPRITDP-TTKVVIFTNKEVVV----SEREIETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLGVHEELIKEGIEEKL 377
Cdd:PLN02807 252 QIPSLREEsAAKVLVLADKESSAepvlRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGLESLLKDALEDKL 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 449441472 378 LQKVVVEVLPQWSESQS-ETWFKSMAENLKLKCLEPRMCGPSVVLE 422
Cdd:PLN02807 332 LQKVVVEVLPFWSGSQGqSIASFGGSQSFKLKRLTSREVGGSVVLE 377
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 84-240 1.45e-96

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: 291.96  E-value: 1.45e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  84 EVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPP 163
Cdd:COG0117    1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449441472 164 CTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGC 240
Cdd:COG0117   81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGK 157
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 87-421 2.70e-90

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: 277.10  E-value: 2.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472   87 MRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPPCTE 166
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  167 ALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGCFLDQVG 246
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  247 KG---AAEAGGYYSQLLQ-EYNAVIISppSSSEEFEIPSSNEHGAK---QPLWIILSSPDGLITVPRITDPTTKVVIFTN 319
Cdd:TIGR00326 161 ESkwiTSEAARTDAQQLRaQSDAILVG--GGTVKADNPALTARLDEateQPLRVVLDTQLRIPEFAKLIPQIAPTWIFTT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  320 KEVVVSERE---IETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLgvHEELIKEGieekLLQKVVVEVLPQWSESQ--- 393
Cdd:TIGR00326 239 ARDKKKRLEafeVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNL--LGSFLDEG----LVDELIIYIAPKLLGGThap 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 449441472  394 ---SETWFKSMAENLKLKCLEPRMCGPSVVL 421
Cdd:TIGR00326 313 glcSEPGFQKMADALNFKFLEINQIGPDILL 343
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 87-199 4.06e-64

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: 201.31  E-value: 4.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  87 MRRSLEIARKAIGHTSPNPMVGCVIVK-NGEIVGEGFHPKAGQPHAEVFALREAG-SLAENATAYVTLEPCNHYGRTPPC 164
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 449441472 165 TEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAG 199
Cdd:cd01284   81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
82-179 4.12e-25

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 98.53  E-value: 4.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472   82 DDEVYMRRSLEIARKAigHTSPNPMVGCVIVK-NGEIVGEGFHPK-AGQP---HAEVFALREAGSL-----AENATAYVT 151
Cdd:pfam00383   1 WDEYFMRLALKAAKRA--YPYSNFPVGAVIVKkDGEIIATGYNGEnAGYDptiHAERNAIRQAGKRgegvrLEGATLYVT 78

                          90       100
                  ....*....|....*....|....*...
gi 449441472  152 LEPCNHygrtppCTEALIKAKVKRVVVG 179
Cdd:pfam00383  79 LEPCGM------CAQAIIESGIKRVVFG 100
 
Name Accession Description Interval E-value
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 64-422 0e+00

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 552.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  64 GGHSVRCvnviQGVHCDVDDEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLA 143
Cdd:PLN02807  17 RRTSVRC----SARAAGDDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 144 ENATAYVTLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQIL 223
Cdd:PLN02807  93 ENATAYVSLEPCNHYGRTPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRML 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 224 TGKPLLTLRYTLSLNGCFLDQVGKGAAEAGGYYSQLLQEYNAVIISpPSSSEEFEIPSSNEHGAKQPLWIIL-SSPDGLI 302
Cdd:PLN02807 173 TGKPFVTLRYSMSMNGCLLNQIGEGADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQEAGAKQPLRIIIaRSESSPL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 303 TVPRITDP-TTKVVIFTNKEVVV----SEREIETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLGVHEELIKEGIEEKL 377
Cdd:PLN02807 252 QIPSLREEsAAKVLVLADKESSAepvlRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGLESLLKDALEDKL 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 449441472 378 LQKVVVEVLPQWSESQS-ETWFKSMAENLKLKCLEPRMCGPSVVLE 422
Cdd:PLN02807 332 LQKVVVEVLPFWSGSQGqSIASFGGSQSFKLKRLTSREVGGSVVLE 377
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 84-240 1.45e-96

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: 291.96  E-value: 1.45e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  84 EVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPP 163
Cdd:COG0117    1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449441472 164 CTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGC 240
Cdd:COG0117   81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGK 157
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 87-421 2.70e-90

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: 277.10  E-value: 2.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472   87 MRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTPPCTE 166
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  167 ALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNGCFLDQVG 246
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  247 KG---AAEAGGYYSQLLQ-EYNAVIISppSSSEEFEIPSSNEHGAK---QPLWIILSSPDGLITVPRITDPTTKVVIFTN 319
Cdd:TIGR00326 161 ESkwiTSEAARTDAQQLRaQSDAILVG--GGTVKADNPALTARLDEateQPLRVVLDTQLRIPEFAKLIPQIAPTWIFTT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  320 KEVVVSERE---IETVVLDQLNMNNILNYCQSQGLNSVMWDVRAKLgvHEELIKEGieekLLQKVVVEVLPQWSESQ--- 393
Cdd:TIGR00326 239 ARDKKKRLEafeVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNL--LGSFLDEG----LVDELIIYIAPKLLGGThap 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 449441472  394 ---SETWFKSMAENLKLKCLEPRMCGPSVVL 421
Cdd:TIGR00326 313 glcSEPGFQKMADALNFKFLEINQIGPDILL 343
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 83-239 9.67e-66

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 214.24  E-value: 9.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  83 DEVYMRRSLEIARKAIGHTSPNPMVGCVIVKNGEIVGEGFHPKAGQPHAEVFALREAGSLAENATAYVTLEPCNHYGRTP 162
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449441472 163 PCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQILTGKPLLTLRYTLSLNG 239
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDG 159
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 87-199 4.06e-64

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: 201.31  E-value: 4.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  87 MRRSLEIARKAIGHTSPNPMVGCVIVK-NGEIVGEGFHPKAGQPHAEVFALREAG-SLAENATAYVTLEPCNHYGRTPPC 164
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 449441472 165 TEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAG 199
Cdd:cd01284   81 VDAIIEAGIKRVVVGVRDPNPLVAGKGAERLRAAG 115
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
82-179 4.12e-25

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 98.53  E-value: 4.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472   82 DDEVYMRRSLEIARKAigHTSPNPMVGCVIVK-NGEIVGEGFHPK-AGQP---HAEVFALREAGSL-----AENATAYVT 151
Cdd:pfam00383   1 WDEYFMRLALKAAKRA--YPYSNFPVGAVIVKkDGEIIATGYNGEnAGYDptiHAERNAIRQAGKRgegvrLEGATLYVT 78

                          90       100
                  ....*....|....*....|....*...
gi 449441472  152 LEPCNHygrtppCTEALIKAKVKRVVVG 179
Cdd:pfam00383  79 LEPCGM------CAQAIIESGIKRVVFG 100
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 82-214 5.07e-20

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: 85.94  E-value: 5.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  82 DDEVYMRRSLEIARKAI---GHtspnPmVGCVIVKNGEIVGEGF-------HPKAgqpHAEVFALREAGSLAEN-----A 146
Cdd:COG0590    3 DDEEFMRRALELARKAVaegEV----P-VGAVLVKDGEIIARGHnrvetlnDPTA---HAEILAIRAAARKLGNwrlsgC 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449441472 147 TAYVTLEPCnhygrtPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDA----GIDVTVSIEEDSCKKL 214
Cdd:COG0590   75 TLYVTLEPC------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPrlnhRVEVVGGVLAEECAAL 140
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 82-221 2.29e-17

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: 78.33  E-value: 2.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472   82 DDEVYMRRSLEIARKAIGHTSPNpmVGCVIVKNGEIVGEGFHPKAGQ----PHAEVFALREA-----GSLAENATAYVTL 152
Cdd:pfam14437   2 NHEKWFRKALGLAEKAYDAGEVP--IGAVIVKDGKVIARGYNRKELNadttAHAEILAIQQAakklgSWRLDDATLYVTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449441472  153 EPCnhygrtPPCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAGIDVTVSIEEDSCKKLNEAYIHQ 221
Cdd:pfam14437  80 EPC------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGFFKK 142
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 76-221 4.33e-17

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 78.31  E-value: 4.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  76 GVHCDVD----DEVYMRRSLEIARKAIGHTS-PnpmVGCVIVKNGEIVGEGFHPKAGQ----PHAEVFALREAGSLAEN- 145
Cdd:PRK10860   2 GVFFLSEvefsHEYWMRHALTLAKRAWDEREvP---VGAVLVHNNRVIGEGWNRPIGRhdptAHAEIMALRQGGLVLQNy 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 146 ----ATAYVTLEPCNHygrtppCTEALIKAKVKRVVVGMVDPNPIVASKGVQRLRDAG----IDVTVSIEEDSCKKLNEA 217
Cdd:PRK10860  79 rlldATLYVTLEPCVM------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGmnhrVEITEGVLADECAALLSD 152


                 ....
gi 449441472 218 YIHQ 221
Cdd:PRK10860 153 FFRM 156
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 87-184 9.81e-17

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: 75.35  E-value: 9.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  87 MRRSLEIARKAIGHTSpNPmVGCVIVKN-GEIVGEGfHPKAGQP-----HAEVFALREAGS-----LAENATAYVTLEPC 155
Cdd:cd01285    1 MRLAIELARKALAEGE-VP-FGAVIVDDdGKVIARG-HNRVEQDgdptaHAEIVAIRNAARrlgsyLLSGCTLYTTLEPC 77

                         90       100
                 ....*....|....*....|....*....
gi 449441472 156 nhygrtPPCTEALIKAKVKRVVVGMVDPN 184
Cdd:cd01285   78 ------PMCAGALLWARIKRVVYGASDPK 100
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 94-180 9.15e-12

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: 61.03  E-value: 9.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  94 ARKAIGHTSPNPMVGCVIVKN--GEIVGEG----FHPKAGQPHAEVFALREAGSLA--ENATAYVTLEPCNHygrtppCT 165
Cdd:cd00786    7 AADLGYAKESNFQVGACLVNKkdGGKVGRGcnieNAAYSMCNHAERTALFNAGSEGdtKGQMLYVALSPCGA------CA 80

                         90
                 ....*....|....*
gi 449441472 166 EALIKAKVKRVVVGM 180
Cdd:cd00786   81 QLIIELGIKDVIVVL 95
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
83-202 1.10e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 62.55  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  83 DEVYMRRSLEIARKAighTSPNPMVGCVIVKNGEIVGEGF--HPKaGQP--------------------------HAEVF 134
Cdd:COG2131    9 DEYFMEIAKLVALRS---TCLRRQVGAVIVKDKRILATGYngAPS-GLPhcdevgclreklgipsgergeccrtvHAEQN 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449441472 135 AL----REAGSLaENATAYVTLEPCNHygrtppCTEALIKAKVKRVVVgmVDPNPivASKGVQRLRDAGIDV 202
Cdd:COG2131   85 AIlqaaRHGVST-EGATLYVTHFPCLE------CAKMIIQAGIKRVVY--LEDYP--DELAKELLKEAGVEV 145
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 83-177 4.24e-10

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: 57.28  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  83 DEVYMRRSLEIARKAighTSPNPMVGCVIVKNGEIVGEGF--------------HPKAGQP-----------HAEVFALR 137
Cdd:cd01286    1 DEYFMAIARLAALRS---TCPRRQVGAVIVKDKRIISTGYngspsglphcaevgCERDDLPsgedqkccrtvHAEQNAIL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 449441472 138 EAGSL---AENATAYVTLEPCNHygrtppCTEALIKAKVKRVV 177
Cdd:cd01286   78 QAARHgvsLEGATLYVTLFPCIE------CAKLIIQAGIKKVV 114
cd PHA02588
deoxycytidylate deaminase; Provisional
 82-215 2.03e-07

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 50.53  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472  82 DDEVYMRRSLEIARKAighTSPNPMVGCVIVKNGEIVGEGFH-PKAGQP------------------------------- 129
Cdd:PHA02588   2 KDSTYLQIAYLVSQES---KCVSWKVGAVIEKNGRIISTGYNgTPAGGVnccdhaneqgwlddegklkkehrpehsawss 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449441472 130 ----HAE----VFALReAGSLAENATAYVTLEPCnhygrtPPCTEALIKAKVKRVVVG-MVDPNPIvasKGVQRLRDAGI 200
Cdd:PHA02588  79 kneiHAElnaiLFAAR-NGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYCeKYDRNGP---GWDDILRKSGI 148

                        170
                 ....*....|....*
gi 449441472 201 DVtVSIEEDSCKKLN 215
Cdd:PHA02588 149 EV-IQIPKEELNKLN 162
 
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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