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Conserved domains on  [gi|394273884|gb|EJE18311|]
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riboflavin biosynthesis protein RibD [Staphylococcus epidermidis NIHLM031]

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

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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 ...
 5-308 4.88e-101

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: 301.36  E-value: 4.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884    5 MDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPCVD 84
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   85 KIIEAGISKVIYAVKDTT-LVS-KGDEILREAGIEVEFQ-YNENAAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATDFN 161
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNpLVAgRGAERLKQAGIEVTFGiLKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  162 ESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDGK-HPIRVILSKTGQLDFNQQIFkDTASEIWIYTEN 240
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATeQPLRVVLDTQLRIPEFAKLI-PQIAPTWIFTTA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  241 EKLKT--DKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELILYIAPKLIGGS 308
Cdd:TIGR00326 240 RDKKKrlEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGT 309
 
Name Accession Description Interval E-value
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 5-308 4.88e-101

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: 301.36  E-value: 4.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884    5 MDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPCVD 84
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   85 KIIEAGISKVIYAVKDTT-LVS-KGDEILREAGIEVEFQ-YNENAAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATDFN 161
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNpLVAgRGAERLKQAGIEVTFGiLKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  162 ESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDGK-HPIRVILSKTGQLDFNQQIFkDTASEIWIYTEN 240
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATeQPLRVVLDTQLRIPEFAKLI-PQIAPTWIFTTA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  241 EKLKT--DKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELILYIAPKLIGGS 308
Cdd:TIGR00326 240 RDKKKrlEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGT 309
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 3-238 4.79e-97

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: 290.04  E-value: 4.79e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   3 RFMDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPC 82
Cdd:COG0117    2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  83 VDKIIEAGISKVIYAVKDTT-LVS-KGDEILREAGIEVEFQYNEN-AAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATD 159
Cdd:COG0117   82 ADALIEAGIKRVVIAMLDPNpLVAgKGIARLRAAGIEVEVGVLEEeARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394273884 160 FNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDGKHPIRVILSKTGQLDFNQQIFKDTASEIWIYT 238
Cdd:COG0117  162 NGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIV 240
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 4-347 8.63e-72

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 227.34  E-value: 8.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   4 FMDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPCV 83
Cdd:PRK10786   6 YMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTPPCC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  84 DKIIEAGISKVIYAVKDTT--LVSKGDEILREAGIEVE--FQYNEnAAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATD 159
Cdd:PRK10786  86 DALIAAGVARVVAAMQDPNpqVAGRGLYRLQQAGIDVShgLMMSE-AEALNKGFLKRMRTGFPYIQLKLGASLDGRTAMA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 160 FNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPD-------------GKHPIRVILSKTGQLDFNQQI 226
Cdd:PRK10786 165 SGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSEldaqtqalypqenLRQPVRIVIDSQNRVTPEHRI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 227 FKDTAsEIWIYTENEKLKTDKSFIKIINI----SKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELILYIAP 302
Cdd:PRK10786 245 VQQPG-ETWLARTQEDSREWPETVRTLLLpehnGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAP 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 394273884 303 KLIGGSGKHQFYKTdEVIDLPEATQFEIVDSKLINQNLKLKLRKK 347
Cdd:PRK10786 324 KLLGSDARGLCTLP-GLEKLADAPQFKFSEIRHVGPDVCLHLVPA 367
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 5-115 3.19e-53

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: 170.88  E-value: 3.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   5 MDDAIQLAKMVNGQTGVNPPVGSVVVK-NGRIVGLGAHLKKGDKHAEVQAIEMAG-LNAQGATIYVSLEPCTHHGSTPPC 82
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 394273884  83 VDKIIEAGISKVIYAVKDTTLV--SKGDEILREAG 115
Cdd:cd01284   81 VDAIIEAGIKRVVVGVRDPNPLvaGKGAERLRAAG 115
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
 142-310 2.08e-43

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: 148.68  E-value: 2.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  142 PEVTVKVSSSLDGKQATDFNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDG----KHPIRVILSKT 217
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGraaeRQPPRVVVDST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  218 GQLDFNQQIFKDTASEIWIYTENeklkTDKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELI 297
Cdd:pfam01872  81 LRVPLDARVLNDDAPTLVATTEP----ADKEKVEKLKVLRVDLKELLRELKERGIRSLLVEGGATLAGSLLRAGLVDELR 156

                         170
                  ....*....|...
gi 394273884  298 LYIAPKLIGGSGK 310
Cdd:pfam01872 157 LYIAPKLLGGGGR 169
 
Name Accession Description Interval E-value
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 5-308 4.88e-101

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: 301.36  E-value: 4.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884    5 MDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPCVD 84
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   85 KIIEAGISKVIYAVKDTT-LVS-KGDEILREAGIEVEFQ-YNENAAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATDFN 161
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNpLVAgRGAERLKQAGIEVTFGiLKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  162 ESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDGK-HPIRVILSKTGQLDFNQQIFkDTASEIWIYTEN 240
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATeQPLRVVLDTQLRIPEFAKLI-PQIAPTWIFTTA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  241 EKLKT--DKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELILYIAPKLIGGS 308
Cdd:TIGR00326 240 RDKKKrlEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPKLLGGT 309
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 3-238 4.79e-97

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: 290.04  E-value: 4.79e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   3 RFMDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPC 82
Cdd:COG0117    2 RYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  83 VDKIIEAGISKVIYAVKDTT-LVS-KGDEILREAGIEVEFQYNEN-AAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATD 159
Cdd:COG0117   82 ADALIEAGIKRVVIAMLDPNpLVAgKGIARLRAAGIEVEVGVLEEeARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394273884 160 FNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDGKHPIRVILSKTGQLDFNQQIFKDTASEIWIYT 238
Cdd:COG0117  162 NGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIV 240
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 4-347 8.63e-72

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 227.34  E-value: 8.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   4 FMDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPPCV 83
Cdd:PRK10786   6 YMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTPPCC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  84 DKIIEAGISKVIYAVKDTT--LVSKGDEILREAGIEVE--FQYNEnAAALYRDFFTAKRNEVPEVTVKVSSSLDGKQATD 159
Cdd:PRK10786  86 DALIAAGVARVVAAMQDPNpqVAGRGLYRLQQAGIDVShgLMMSE-AEALNKGFLKRMRTGFPYIQLKLGASLDGRTAMA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 160 FNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPD-------------GKHPIRVILSKTGQLDFNQQI 226
Cdd:PRK10786 165 SGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSEldaqtqalypqenLRQPVRIVIDSQNRVTPEHRI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 227 FKDTAsEIWIYTENEKLKTDKSFIKIINI----SKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELILYIAP 302
Cdd:PRK10786 245 VQQPG-ETWLARTQEDSREWPETVRTLLLpehnGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAP 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 394273884 303 KLIGGSGKHQFYKTdEVIDLPEATQFEIVDSKLINQNLKLKLRKK 347
Cdd:PRK10786 324 KLLGSDARGLCTLP-GLEKLADAPQFKFSEIRHVGPDVCLHLVPA 367
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
 142-347 8.65e-56

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: 181.13  E-value: 8.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 142 PEVTVKVSSSLDGKQATDFNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPD-GKHPIRVILSKTGQL 220
Cdd:COG1985    4 PYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGlGRQPLRVVVDSSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 221 DFNQQIFkDTASEIWIYTENEKLKTDKS--------FIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKH 292
Cdd:COG1985   84 PPDARLF-DDAAPTLVLTTEAADAERRAaleaagaeVIVLPGDGRVDLAALLAALAERGIRSVLVEGGPTLAGSFLAAGL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394273884 293 LNELILYIAPKLIGGSGKHqFYKTDEVIDLPEATQFEIVDSKLINQNLKLKLRKK 347
Cdd:COG1985  163 VDELILYIAPKLLGGDGPT-LVGGPGLETLADAPRLRLVSVRRLGDDLLLRYRPR 216
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 5-115 3.19e-53

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: 170.88  E-value: 3.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   5 MDDAIQLAKMVNGQTGVNPPVGSVVVK-NGRIVGLGAHLKKGDKHAEVQAIEMAG-LNAQGATIYVSLEPCTHHGSTPPC 82
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDdDGEIVGEGYHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 394273884  83 VDKIIEAGISKVIYAVKDTTLV--SKGDEILREAG 115
Cdd:cd01284   81 VDAIIEAGIKRVVVGVRDPNPLvaGKGAERLRAAG 115
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 2-309 1.01e-48

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 168.03  E-value: 1.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   2 SRFMDDAIQLAKMVNGQTGVNPPVGSVVVKNGRIVGLGAHLKKGDKHAEVQAIEMAGLNAQGATIYVSLEPCTHHGSTPP 81
Cdd:PLN02807  33 SFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGRTPP 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  82 CVDKIIEAGISKVIYAVKDTT--LVSKGDEILREAGIEVEFQYNE------NAAALYRdFFTAKrnevPEVTVKVSSSLD 153
Cdd:PLN02807 113 CTEALIKAKVKRVVVGMVDPNpiVASKGIERLRDAGIEVTVGVEEelcrklNEAFIHR-MLTGK----PFVTLRYSMSMN 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 154 GKQATDFNESkwitnKEVKEDVY-QLRHEHDAVITGRRTIEADnPLYTTRVPDGKHPIRVILSKTGQLDFNQQIFKDT-A 231
Cdd:PLN02807 188 GCLLNQIGEG-----ADDAGGYYsQLLQEYDAVILSSALADAD-PLPLSQEAGAKQPLRIIIARSESSPLQIPSLREEsA 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 232 SEIWIYTENEKL---KTDKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITS------QFLQSKHLNELILYIAP 302
Cdd:PLN02807 262 AKVLVLADKESSaepVLRRKGVEVVVLNQINLDSILDLCYQRGLCSVLLDLRGNVGGlesllkDALEDKLLQKVVVEVLP 341


                 ....*..
gi 394273884 303 KLIGGSG 309
Cdd:PLN02807 342 FWSGSQG 348
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
 142-310 2.08e-43

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: 148.68  E-value: 2.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  142 PEVTVKVSSSLDGKQATDFNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTRVPDG----KHPIRVILSKT 217
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGraaeRQPPRVVVDST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  218 GQLDFNQQIFKDTASEIWIYTENeklkTDKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSKHLNELI 297
Cdd:pfam01872  81 LRVPLDARVLNDDAPTLVATTEP----ADKEKVEKLKVLRVDLKELLRELKERGIRSLLVEGGATLAGSLLRAGLVDELR 156

                         170
                  ....*....|...
gi 394273884  298 LYIAPKLIGGSGK 310
Cdd:pfam01872 157 LYIAPKLLGGGGR 169
ribD_Cterm TIGR00227
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ...
 141-308 4.45e-40

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: 140.60  E-value: 4.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  141 VPEVTVKVSSSLDGKQATDFNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNPLYTTR---VPDGKHPIRVILSKT 217
Cdd:TIGR00227   2 RPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRwveLDELRNPVRVVLDSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  218 GQLDFNQQIFKDTAsEIWIYTENEKLKTDKSFIK--IINISKCDTTTI-----LQDLYQRGIGKLLVEAGPNITSQFLQS 290
Cdd:TIGR00227  82 LRVPPTARLLNDDA-PTWVATSEPADEEKVKELEdfGVEVLVLETKRVdlkklMEILYEEGIRSVMVEGGGTLNGSLLKE 160

                         170
                  ....*....|....*...
gi 394273884  291 KHLNELILYIAPKLIGGS 308
Cdd:TIGR00227 161 GLVDELIVYIAPKLLGGR 178
PRK05625 PRK05625
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
 142-347 6.43e-25

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


Pssm-ID: 180169  Cd Length: 217  Bit Score: 100.32  E-value: 6.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 142 PEVTVKVSSSLDGKQATDFNESKwITNKEVKEDVYQLRHEHDAVITGRRTIEADNP-LYTTRVPDGK--HPIRVILSKTG 218
Cdd:PRK05625   3 PYVIVNAAMSADGKLATKTRYSR-ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPsLTVHRYAAGKpeNPIRVVVDSSA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 219 QLDFNQQIFKDTASEIwIYTEN-------EKLKTDKSFIKIINISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFLQSK 291
Cdd:PRK05625  82 RTPPDARILDGPAKTI-VAVSEaapsekvEELEKKGAEVIVAGGERVDLPDLLEDLYERGIKRLMVEGGGTLIWSMFKEG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 394273884 292 HLNELILYIAPKLIGGSGKHQFYKTDEVIDLPEATQFEIVDSKLINQNLKLKLRKK 347
Cdd:PRK05625 161 LVDEVRVTVGPKIIGGKDAPTLADGEGFIEEEDPLKLELAKVCRCDEGVVLTYKVK 216
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-137 7.42e-21

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: 87.48  E-value: 7.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   1 MSRFMDDAIQLAK--MVNGqtGVnpPVGSVVVKNGRIVGLGAHLKKGDK----HAEVQAIEMAG--LNA---QGATIYVS 69
Cdd:COG0590    4 DEEFMRRALELARkaVAEG--EV--PVGAVLVKDGEIIARGHNRVETLNdptaHAEILAIRAAArkLGNwrlSGCTLYVT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394273884  70 LEPCthhgstPPCVDKIIEAGISKVIYAVKDT------TLVSKGDEILREAGIEVEFQ-YNENAAALYRDFFTAK 137
Cdd:COG0590   80 LEPC------PMCAGAIVWARIGRVVYGASDPkagaagSIYDLLADPRLNHRVEVVGGvLAEECAALLRDFFAAR 148
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
2-97 8.35e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 83.12  E-value: 8.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884    2 SRFMDDAIQLAKMvnGQTGVNPPVGSVVVK-NGRIVGLGAHLKKGDK----HAEVQAIEMAGLN-----AQGATIYVSLE 71
Cdd:pfam00383   3 EYFMRLALKAAKR--AYPYSNFPVGAVIVKkDGEIIATGYNGENAGYdptiHAERNAIRQAGKRgegvrLEGATLYVTLE 80

                          90       100
                  ....*....|....*....|....*.
gi 394273884   72 PCTHhgstppCVDKIIEAGISKVIYA 97
Cdd:pfam00383  81 PCGM------CAQAIIESGIKRVVFG 100
PRK14719 PRK14719
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
 141-345 1.63e-15

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


Pssm-ID: 237801 [Multi-domain]  Cd Length: 360  Bit Score: 76.52  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 141 VPEVTVKVSSSLDGKQATDFNESKWITNKEVKEdVYQLRHEHDAVITGRRTIEADNPLYTT-RVPDG--KHPIRVILSKT 217
Cdd:PRK14719 139 LPYVISNVGMTLDGKLATIENDSRISGENDLKR-VHEIRKDVDAIMVGIGTVLKDDPRLTVhKINASpkDNPLRIVVDSN 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 218 GQLDFNQQIFKDTASEIWIYT------ENEKLKTDKSFIKII---NISKCDTTTILQDLYQRGIGKLLVEAGPNITSQFL 288
Cdd:PRK14719 218 LKIPLNARVLNKDAKTVIATTtpisdeKEEKIRKLKEMGITVlqaGVQKVDLRKIMNEIYKMGINKILLEGGGTLNWGMF 297

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394273884 289 QSKHLNELILYIAPKLIGGSGKHQFYKTDEVIDLPEATQFEIVDSKLINQNLKLKLR 345
Cdd:PRK14719 298 KENLINEVRVYIAPKVFGGANSPTYVDGEGFKNVEECTKLELKNYYPLDDGIVLEYR 354
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 5-98 2.40e-15

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: 70.66  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   5 MDDAIQLAKMvNGQTGVNPPVGSVVVKN--GRIVGLGAHLK----KGDKHAEVQAIEMAGLNA--QGATIYVSLEPCTHh 76
Cdd:cd00786    1 MTEALKAADL-GYAKESNFQVGACLVNKkdGGKVGRGCNIEnaaySMCNHAERTALFNAGSEGdtKGQMLYVALSPCGA- 78

                         90       100
                 ....*....|....*....|..
gi 394273884  77 gstppCVDKIIEAGISKVIYAV 98
Cdd:cd00786   79 -----CAQLIIELGIKDVIVVL 95
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
25-119 5.75e-15

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 71.41  E-value: 5.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  25 VGSVVVKNGRIVGLG--------------------AHLKKGDK-------HAEVQAIEMA---GLNAQGATIYVSLEPCT 74
Cdd:COG2131   30 VGAVIVKDKRILATGyngapsglphcdevgclrekLGIPSGERgeccrtvHAEQNAILQAarhGVSTEGATLYVTHFPCL 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 394273884  75 HhgstppCVDKIIEAGISKVIYA--VKDttlvSKGDEILREAGIEVE 119
Cdd:COG2131  110 E------CAKMIIQAGIKRVVYLedYPD----ELAKELLKEAGVEVR 146
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 5-97 9.75e-13

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: 63.79  E-value: 9.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   5 MDDAIQLAKMVNGQTGVnpPVGSVVVKN-GRIVGLGaH---LKKGD--KHAEVQAIEMAGLNAQ-----GATIYVSLEPC 73
Cdd:cd01285    1 MRLAIELARKALAEGEV--PFGAVIVDDdGKVIARG-HnrvEQDGDptAHAEIVAIRNAARRLGsyllsGCTLYTTLEPC 77

                         90       100
                 ....*....|....*....|....
gi 394273884  74 thhgstPPCVDKIIEAGISKVIYA 97
Cdd:cd01285   78 ------PMCAGALLWARIKRVVYG 95
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 3-138 1.56e-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: 64.47  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884    3 RFMDDAIQLAKMVNGQTGVnpPVGSVVVKNGRIVGLGAHLKKGDK----HAEVQAIEMA-----GLNAQGATIYVSLEPC 73
Cdd:pfam14437   5 KWFRKALGLAEKAYDAGEV--PIGAVIVKDGKVIARGYNRKELNAdttaHAEILAIQQAakklgSWRLDDATLYVTLEPC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394273884   74 thhgstPPCVDKIIEAGISKVIYAVKDTTLVSKGDEILR----EAGIEVEFQYNENAAALyRDFFTAKR 138
Cdd:pfam14437  83 ------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKlvivLWNHRVELVEEDCSEIL-KGFFKKLR 144
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 25-97 1.66e-11

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: 61.14  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884  25 VGSVVVKNGRIVGLG--------------AHLKKGDK-----------HAEVQAIEMA---GLNAQGATIYVSLEPCTHh 76
Cdd:cd01286   22 VGAVIVKDKRIISTGyngspsglphcaevGCERDDLPsgedqkccrtvHAEQNAILQAarhGVSLEGATLYVTLFPCIE- 100

                         90       100
                 ....*....|....*....|.
gi 394273884  77 gstppCVDKIIEAGISKVIYA 97
Cdd:cd01286  101 -----CAKLIIQAGIKKVVYA 116
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 4-140 3.57e-11

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 60.98  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   4 FMDDAIQLAKMVNGQTGVnpPVGSVVVKNGRIVGLGAHLKKGDK----HAEVQAIEMAGLNAQG-----ATIYVSLEPCT 74
Cdd:PRK10860  16 WMRHALTLAKRAWDEREV--PVGAVLVHNNRVIGEGWNRPIGRHdptaHAEIMALRQGGLVLQNyrlldATLYVTLEPCV 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 394273884  75 HhgstppCVDKIIEAGISKVIYAVKDTTLVSKGD--EILREAG----IEV-EFQYNENAAALYRDFFTAKRNE 140
Cdd:PRK10860  94 M------CAGAMVHSRIGRLVFGARDAKTGAAGSlmDVLHHPGmnhrVEItEGVLADECAALLSDFFRMRRQE 160
cd PHA02588
deoxycytidylate deaminase; Provisional
 4-119 3.63e-11

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 60.93  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884   4 FMDDAIQLAKmvnGQTGVNPPVGSVVVKNGRIVGLGA------------HLKKGDK------------------------ 47
Cdd:PHA02588   6 YLQIAYLVSQ---ESKCVSWKVGAVIEKNGRIISTGYngtpaggvnccdHANEQGWlddegklkkehrpehsawssknei 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394273884  48 HAEVQAIEMA---GLNAQGATIYVSLEPCthhgstPPCVDKIIEAGISKVIYAVKDTTLVSKGDEILREAGIEVE 119
Cdd:PHA02588  83 HAELNAILFAarnGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYCEKYDRNGPGWDDILRKSGIEVI 151
PRK14059 PRK14059
pyrimidine reductase family protein;
127-307 7.99e-07

pyrimidine reductase family protein;


Pssm-ID: 184482  Cd Length: 251  Bit Score: 49.58  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 127 AALYRDFFTAKRnevPEVTVKVSSSLDGKqATDFNESKWITNKEVKEDVYQLRHEHDAVITGRRTIEADNplYT-TRVPD 205
Cdd:PRK14059  19 AELYAYPDGLDR---PWLRANFVTSLDGA-ATVDGRSGGLGGPADRRVFGLLRALADVVVVGAGTVRAEN--YGgVRLSA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273884 206 GK-----------HPIRVILSKTGQLDFNQQIFKDTASEIWIYTENEKLKTDKSFIK----IINISKCDTTTI-----LQ 265
Cdd:PRK14059  93 AArqqrqargqaeVPPIAVVSRSGDLDPDSRLFTETEVPPLVLTCAAAAADRRRRLAglaeVADVVVAGPDTVdlaaaVA 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 394273884 266 DLYQRGIGKLLVEAGPNITSQFLQSKHLNELILYIAPKLIGG 307
Cdd:PRK14059 173 ALAARGLRRILCEGGPTLLGQLLAADLVDELCLTIAPVLAGG 214
 
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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