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Conserved domains on  [gi|15599251|ref|NP_252745|]
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riboflavin-specific deaminase/reductase [Pseudomonas aeruginosa PAO1]

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 ...
 5-373 1.55e-157

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 PRK10786:

Pssm-ID: 473077 [Multi-domain]  Cd Length: 367  Bit Score: 446.91  E-value: 1.55e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    5 DPLYMARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTP 84
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   85 PCADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTA 164
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  165 MASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDElgLNAELTAL---AAARQPLRVLVDGRLRV-P 240
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSE--LDAQTQALypqENLRQPVRIVIDSQNRVtP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  241 LESAFYQAGPALVATcaaASARERFQDAGHELLALPSAEGHVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEY 320
Cdd:PRK10786 241 EHRIVQQPGETWLAR---TQEDSREWPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDEL 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599251  321 RLFVAPKFLGSSARPLLDWP-LARMADAAQLRIDDIRAVGDDwlvtARPHLRDA 373
Cdd:PRK10786 318 IVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPD----VCLHLVPA 367
 
Name Accession Description Interval E-value
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 5-373 1.55e-157

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 446.91  E-value: 1.55e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    5 DPLYMARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTP 84
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   85 PCADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTA 164
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  165 MASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDElgLNAELTAL---AAARQPLRVLVDGRLRV-P 240
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSE--LDAQTQALypqENLRQPVRIVIDSQNRVtP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  241 LESAFYQAGPALVATcaaASARERFQDAGHELLALPSAEGHVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEY 320
Cdd:PRK10786 241 EHRIVQQPGETWLAR---TQEDSREWPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDEL 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599251  321 RLFVAPKFLGSSARPLLDWP-LARMADAAQLRIDDIRAVGDDwlvtARPHLRDA 373
Cdd:PRK10786 318 IVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPD----VCLHLVPA 367
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 9-365 8.05e-135

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: 388.42  E-value: 8.05e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251     9 MARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTPPCAD 88
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    89 ALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTAMASG 168
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   169 ESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDElglnaeltalaAARQPLRVLVDGRLRVPLESA-FYQ 247
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDE-----------ATEQPLRVVLDTQLRIPEFAKlIPQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   248 AGPALVATCAAASaRERFQDAGHELLALPSaeghVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEYRLFVAPK 327
Cdd:TIGR00326 230 IAPTWIFTTARDK-KKRLEAFEVNIFPLEK----VTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 15599251   328 FLGSSARPLLDWPLA--RMADAAQLRIDDIRAVGDDWLVT 365
Cdd:TIGR00326 305 LLGGTHAPGLCSEPGfqKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 8-320 9.44e-132

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: 379.40  E-value: 9.44e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   8 YMARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTPPCA 87
Cdd:COG0117   3 YMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPCA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  88 DALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTAMAS 167
Cdd:COG0117  83 DALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATAN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251 168 GESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDELGlnaeltalaaaRQPLRVLVDGRLRVPLESAFYQ 247
Cdd:COG0117 163 GESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGE-----------NPPRRVVVDDLLLRPPPALLLV 231

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599251 248 AGPALVATC------AAASARERFQDAGHELLALPSAEGHVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEY 320
Cdd:COG0117 232 ANDAALIIVtvtadaAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDLL 310
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 9-121 2.14e-54

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: 174.73  E-value: 2.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   9 MARALELARQGLYSTQPNPRVGCVLVKD-GQVVGEGWHVRAGEPHAEVHALRQAGEN-ARGATAYVTLEPCSHFGRTPPC 86
Cdd:cd01284   1 MRRALELAEKGRGLTSPNPPVGCVIVDDdGEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599251  87 ADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAG 121
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 ...
 149-364 3.90e-49

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: 164.09  E-value: 3.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   149 PFVRVKLAMSLDGRTAMASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDELGlnaeltalAAARQP 228
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGR--------AAERQP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   229 LRVLVDGRLRVPLESA-FYQAGPALVATCAAAsARERFQDAghellalpsAEGHVDLHKLLLELAARGANEVLVEAGPRL 307
Cdd:pfam01872  73 PRVVVDSTLRVPLDARvLNDDAPTLVATTEPA-DKEKVEKL---------KVLRVDLKELLRELKERGIRSLLVEGGATL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15599251   308 AGAFARLGLVDEYRLFVAPKFLGSSARPLLDWPLARmadAAQLRIDDIRAVGDDWLV 364
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRTLFGGEGFL---ALKLKLVSSEAIGNGVVL 196
 
Name Accession Description Interval E-value
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 5-373 1.55e-157

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 446.91  E-value: 1.55e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    5 DPLYMARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTP 84
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   85 PCADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTA 164
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  165 MASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDElgLNAELTAL---AAARQPLRVLVDGRLRV-P 240
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSE--LDAQTQALypqENLRQPVRIVIDSQNRVtP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  241 LESAFYQAGPALVATcaaASARERFQDAGHELLALPSAEGHVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEY 320
Cdd:PRK10786 241 EHRIVQQPGETWLAR---TQEDSREWPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDEL 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599251  321 RLFVAPKFLGSSARPLLDWP-LARMADAAQLRIDDIRAVGDDwlvtARPHLRDA 373
Cdd:PRK10786 318 IVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPD----VCLHLVPA 367
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 9-365 8.05e-135

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: 388.42  E-value: 8.05e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251     9 MARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTPPCAD 88
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    89 ALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTAMASG 168
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   169 ESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDElglnaeltalaAARQPLRVLVDGRLRVPLESA-FYQ 247
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDE-----------ATEQPLRVVLDTQLRIPEFAKlIPQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   248 AGPALVATCAAASaRERFQDAGHELLALPSaeghVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEYRLFVAPK 327
Cdd:TIGR00326 230 IAPTWIFTTARDK-KKRLEAFEVNIFPLEK----VTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 15599251   328 FLGSSARPLLDWPLA--RMADAAQLRIDDIRAVGDDWLVT 365
Cdd:TIGR00326 305 LLGGTHAPGLCSEPGfqKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 8-320 9.44e-132

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: 379.40  E-value: 9.44e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   8 YMARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTPPCA 87
Cdd:COG0117   3 YMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPPCA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  88 DALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGRTAMAS 167
Cdd:COG0117  83 DALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIATAN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251 168 GESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDELGlnaeltalaaaRQPLRVLVDGRLRVPLESAFYQ 247
Cdd:COG0117 163 GESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGE-----------NPPRRVVVDDLLLRPPPALLLV 231

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599251 248 AGPALVATC------AAASARERFQDAGHELLALPSAEGHVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEY 320
Cdd:COG0117 232 ANDAALIIVtvtadaAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDLL 310
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
 146-369 4.74e-83

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: 252.00  E-value: 4.74e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251 146 HGLPFVRVKLAMSLDGRTAMASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDELGlnaeltalaaa 225
Cdd:COG1985   1 TGRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGLG----------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251 226 RQPLRVLVDGRLRVPLESAFYQ-AGPALVATCAAASA--RERFQDAGHELLALPSaEGHVDLHKLLLELAARGANEVLVE 302
Cdd:COG1985  70 RQPLRVVVDSSLRLPPDARLFDdAAPTLVLTTEAADAerRAALEAAGAEVIVLPG-DGRVDLAALLAALAERGIRSVLVE 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599251 303 AGPRLAGAFARLGLVDEYRLFVAPKFLGSSARPLLDWP-LARMADAAQLRIDDIRAVGDDWLVTARPH 369
Cdd:COG1985 149 GGPTLAGSFLAAGLVDELILYIAPKLLGGDGPTLVGGPgLETLADAPRLRLVSVRRLGDDLLLRYRPR 216
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 5-337 1.02e-76

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 241.60  E-value: 1.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    5 DPLYMARALELARQGLYSTQPNPRVGCVLVKDGQVVGEGWHVRAGEPHAEVHALRQAGENARGATAYVTLEPCSHFGRTP 84
Cdd:PLN02807  32 DSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGRTP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   85 PCADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRMEHGLPFVRVKLAMSLDGR-- 162
Cdd:PLN02807 112 PCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGCll 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  163 TAMASGESQwitgpSARSAVQRLRARSSVVLSGAdtlLADDarlnvrpDELGLNAEltalAAARQPLRVLVDGRLRVPLE 242
Cdd:PLN02807 192 NQIGEGADD-----AGGYYSQLLQEYDAVILSSA---LADA-------DPLPLSQE----AGAKQPLRIIIARSESSPLQ 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  243 SAFY---QAGPALVATCAAASARERFQDAGHELLALpsaeGHVDLHKLLLELAARGANEVLVEAGPRLAGaFARLG---- 315
Cdd:PLN02807 253 IPSLreeSAAKVLVLADKESSAEPVLRRKGVEVVVL----NQINLDSILDLCYQRGLCSVLLDLRGNVGG-LESLLkdal 327

                        330       340
                 ....*....|....*....|....*
gi 15599251  316 ---LVDEYRLFVAPKFLGSSARPLL 337
Cdd:PLN02807 328 edkLLQKVVVEVLPFWSGSQGQSIA 352
ribD_Cterm TIGR00227
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ...
 147-368 2.34e-64

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: 204.16  E-value: 2.34e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   147 GLPFVRVKLAMSLDGRTAMASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDElglnaeltaLAAAR 226
Cdd:TIGR00227   1 GRPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRWVE---------LDELR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   227 QPLRVLVDGRLRVPLES-AFYQAGPALVATCAAASARE--RFQDAGHELLALpsAEGHVDLHKLLLELAARGANEVLVEA 303
Cdd:TIGR00227  72 NPVRVVLDSRLRVPPTArLLNDDAPTWVATSEPADEEKvkELEDFGVEVLVL--ETKRVDLKKLMEILYEEGIRSVMVEG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599251   304 GPRLAGAFARLGLVDEYRLFVAPKFLG-SSARPLLDWP-LARMADAAQLRIDDIRAVGDDWLVTARP 368
Cdd:TIGR00227 150 GGTLNGSLLKEGLVDELIVYIAPKLLGgRDAPTLVDGEgFQKMADAPNLELKEIYQIGEDIVLTAKL 216
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 9-121 2.14e-54

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: 174.73  E-value: 2.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   9 MARALELARQGLYSTQPNPRVGCVLVKD-GQVVGEGWHVRAGEPHAEVHALRQAGEN-ARGATAYVTLEPCSHFGRTPPC 86
Cdd:cd01284   1 MRRALELAEKGRGLTSPNPPVGCVIVDDdGEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599251  87 ADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAG 121
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 ...
 149-364 3.90e-49

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: 164.09  E-value: 3.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   149 PFVRVKLAMSLDGRTAMASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDELGlnaeltalAAARQP 228
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGR--------AAERQP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   229 LRVLVDGRLRVPLESA-FYQAGPALVATCAAAsARERFQDAghellalpsAEGHVDLHKLLLELAARGANEVLVEAGPRL 307
Cdd:pfam01872  73 PRVVVDSTLRVPLDARvLNDDAPTLVATTEPA-DKEKVEKL---------KVLRVDLKELLRELKERGIRSLLVEGGATL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15599251   308 AGAFARLGLVDEYRLFVAPKFLGSSARPLLDWPLARmadAAQLRIDDIRAVGDDWLV 364
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRTLFGGEGFL---ALKLKLVSSEAIGNGVVL 196
PRK05625 PRK05625
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
 149-365 4.72e-30

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


Pssm-ID: 180169  Cd Length: 217  Bit Score: 114.57  E-value: 4.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  149 PFVRVKLAMSLDGRTAMASGESQwITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPDELGLNaeltalaaaRQP 228
Cdd:PRK05625   3 PYVIVNAAMSADGKLATKTRYSR-ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAAGKP---------ENP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  229 LRVLVDGRLRVPLESA-FYQAGPALVATCAAA--SARERFQDAGHELLAlpSAEGHVDLHKLLLELAARGANEVLVEAGP 305
Cdd:PRK05625  73 IRVVVDSSARTPPDARiLDGPAKTIVAVSEAApsEKVEELEKKGAEVIV--AGGERVDLPDLLEDLYERGIKRLMVEGGG 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599251  306 RLAGAFARLGLVDEYRLFVAPK-FLGSSARPLLDWP-LARMADAAQLRIDDIRAVGDDWLVT 365
Cdd:PRK05625 151 TLIWSMFKEGLVDEVRVTVGPKiIGGKDAPTLADGEgFIEEEDPLKLELAKVCRCDEGVVLT 212
rib_reduct_arch TIGR01508
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ...
 149-367 7.00e-27

2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model represents a specific reductase of riboflavin biosynthesis in the Archaea, diaminohydroxyphosphoribosylaminopyrimidine reductase. It should not be confused with bacterial 5-amino-6-(5-phosphoribosylamino)uracil reductase. The intermediate 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine in riboflavin biosynthesis is reduced first, and then deaminated, in both Archaea and Fungi, opposite the order in Bacteria. The subsequent deaminase is not presently known and is not closely homologous to the deaminase domain (3.5.4.26) fused to the reductase domain (1.1.1.193) similar to this protein but found in most bacteria.


Pssm-ID: 130572  Cd Length: 210  Bit Score: 106.04  E-value: 7.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   149 PFVRVKLAMSLDGRTAMASGESQwITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRpdelglnaeltALAAARQP 228
Cdd:TIGR01508   1 PYVIVNVAMSLDGKLATINRDSR-ISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTVK-----------KIKSDRNP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   229 LRVLVDGRLRVPLESAFYQAGP-ALVATCAAASA--RERFQDAGHELLALpsAEGHVDLHKLLLELAARGANEVLVEAGP 305
Cdd:TIGR01508  69 VRVVVDSKLRVPLNARILNKDAkTIIATSEDEPEekVEELEDKGVEVVKF--GEGRVDLKKLLDILYDKGVRRLMVEGGG 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599251   306 RLAGAFARLGLVDEYRLFVAPKFLGSSARP-LLDWPLARMADAAQLRIDDIRAVGDDWLVTAR 367
Cdd:TIGR01508 147 TLIWSLFKENLVDEISVYIAPKIFGGRDAPtYVDGEGFKTEDCPKLELKNFYRLGEGIVLEFK 209
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 5-143 7.81e-22

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: 90.56  E-value: 7.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   5 DPLYMARALELARQGLYS-TQPnprVGCVLVKDGQVVGEGW--HVRAGEP--HAEVHALRQAGENA-----RGATAYVTL 74
Cdd:COG0590   4 DEEFMRRALELARKAVAEgEVP---VGAVLVKDGEIIARGHnrVETLNDPtaHAEILAIRAAARKLgnwrlSGCTLYVTL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599251  75 EPCshfgrtPPCADALVGAGVARVVAAMQDPNPEVAGRGL----LRLMQAGIAVQSGVLEAEARELNIGFIKR 143
Cdd:COG0590  81 EPC------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYdllaDPRLNHRVEVVGGVLAEECAALLRDFFAA 147
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
8-101 1.33e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 88.13  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251     8 YMARALELARQGlySTQPNPRVGCVLVK-DGQVVGEGWHVR-AGEP---HAEVHALRQA-----GENARGATAYVTLEPC 77
Cdd:pfam00383   5 FMRLALKAAKRA--YPYSNFPVGAVIVKkDGEIIATGYNGEnAGYDptiHAERNAIRQAgkrgeGVRLEGATLYVTLEPC 82

                          90       100
                  ....*....|....*....|....
gi 15599251    78 SHfgrtppCADALVGAGVARVVAA 101
Cdd:pfam00383  83 GM------CAQAIIESGIKRVVFG 100
PRK14719 PRK14719
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
 148-335 2.74e-18

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


Pssm-ID: 237801 [Multi-domain]  Cd Length: 360  Bit Score: 84.99  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  148 LPFVRVKLAMSLDGRTAMASGESQwITGPSARSAVQRLRARSSVVLSGADTLLADDARLNVRPdelgLNAeltalAAARQ 227
Cdd:PRK14719 139 LPYVISNVGMTLDGKLATIENDSR-ISGENDLKRVHEIRKDVDAIMVGIGTVLKDDPRLTVHK----INA-----SPKDN 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  228 PLRVLVDGRLRVPLES-AFYQAGPALVATCAAASARE-----RFQDAGheLLALPSAEGHVDLHKLLLELAARGANEVLV 301
Cdd:PRK14719 209 PLRIVVDSNLKIPLNArVLNKDAKTVIATTTPISDEKeekirKLKEMG--ITVLQAGVQKVDLRKIMNEIYKMGINKILL 286

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15599251  302 EAGPRLAGAFARLGLVDEYRLFVAPKFLGSSARP 335
Cdd:PRK14719 287 EGGGTLNWGMFKENLINEVRVYIAPKVFGGANSP 320
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 9-102 9.37e-16

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: 72.20  E-value: 9.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   9 MARALELARQGlYSTQPNPRVGCVLV--KDGQVVGEGWHVR----AGEPHAEVHALRQAG--ENARGATAYVTLEPCSHf 80
Cdd:cd00786   1 MTEALKAADLG-YAKESNFQVGACLVnkKDGGKVGRGCNIEnaaySMCNHAERTALFNAGseGDTKGQMLYVALSPCGA- 78

                        90       100
                ....*....|....*....|..
gi 15599251  81 grtppCADALVGAGVARVVAAM 102
Cdd:cd00786  79 -----CAQLIIELGIKDVIVVL 95
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
8-125 2.06e-15

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 72.95  E-value: 2.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   8 YMARALELArqgLYSTQPNPRVGCVLVKDGQVVG---------------EGWH-----VRAGEP-------HAEVHALRQ 60
Cdd:COG2131  12 FMEIAKLVA---LRSTCLRRQVGAVIVKDKRILAtgyngapsglphcdeVGCLreklgIPSGERgeccrtvHAEQNAILQ 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599251  61 A---GENARGATAYVTLEPCSHfgrtppCADALVGAGVARVVAAmqDPNPEVAGRGLLRlmQAGIAVQ 125
Cdd:COG2131  89 AarhGVSTEGATLYVTHFPCLE------CAKMIIQAGIKRVVYL--EDYPDELAKELLK--EAGVEVR 146
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 8-145 2.97e-15

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: 72.17  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251     8 YMARALELARQGlYSTQPNPrVGCVLVKDGQVVGEGWHVRAGE----PHAEVHALRQAGE-----NARGATAYVTLEPCs 78
Cdd:pfam14437   6 WFRKALGLAEKA-YDAGEVP-IGAVIVKDGKVIARGYNRKELNadttAHAEILAIQQAAKklgswRLDDATLYVTLEPC- 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599251    79 hfgrtPPCADALVGAGVARVVAAMQDPNPEVAGRGLLRLMQAGIAVQSGVLEAEARELNIGFIKRME 145
Cdd:pfam14437  83 -----PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGFFKKLR 144
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 5-101 4.14e-15

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: 71.15  E-value: 4.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   5 DPLYMARALELArqgLYSTQPNPRVGCVLVKDGQVVG--------------EGWHVRAGEP-----------HAEVHALR 59
Cdd:cd01286   1 DEYFMAIARLAA---LRSTCPRRQVGAVIVKDKRIIStgyngspsglphcaEVGCERDDLPsgedqkccrtvHAEQNAIL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15599251  60 QAGENAR---GATAYVTLEPCSHfgrtppCADALVGAGVARVVAA 101
Cdd:cd01286  78 QAARHGVsleGATLYVTLFPCIE------CAKLIIQAGIKKVVYA 116
PRK14059 PRK14059
pyrimidine reductase family protein;
149-336 2.07e-14

pyrimidine reductase family protein;


Pssm-ID: 184482  Cd Length: 251  Bit Score: 72.31  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  149 PFVRVKLAMSLDGrTAMASGESQWITGPSARSAVQRLRARSSVVLSGADTLLADDARlNVRPDELGLNAELTALAAARQP 228
Cdd:PRK14059  31 PWLRANFVTSLDG-AATVDGRSGGLGGPADRRVFGLLRALADVVVVGAGTVRAENYG-GVRLSAAARQQRQARGQAEVPP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251  229 LRVlVDGRLRVPLESAFYQ--AGPALVATCAAA--SARERFQDAGHELLALPSAEGHVDLHKLLLELAARGANEVLVEAG 304
Cdd:PRK14059 109 IAV-VSRSGDLDPDSRLFTetEVPPLVLTCAAAaaDRRRRLAGLAEVADVVVAGPDTVDLAAAVAALAARGLRRILCEGG 187

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15599251  305 PRLAGAFARLGLVDEYRLFVAPKFLGSSARPL 336
Cdd:PRK14059 188 PTLLGQLLAADLVDELCLTIAPVLAGGVARRI 219
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 9-111 4.53e-14

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: 67.64  E-value: 4.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251   9 MARALELARQGL-YSTQPnprVGCVLV-KDGQVVGEGWH--VRAGEP--HAEVHALRQAGENAR-----GATAYVTLEPC 77
Cdd:cd01285   1 MRLAIELARKALaEGEVP---FGAVIVdDDGKVIARGHNrvEQDGDPtaHAEIVAIRNAARRLGsyllsGCTLYTTLEPC 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 15599251  78 shfgrtPPCADALVGAGVARVVAAMQDPNPEVAG 111
Cdd:cd01285  78 ------PMCAGALLWARIKRVVYGASDPKLGGIG 105
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 5-146 1.09e-13

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 68.29  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    5 DPLYMARALELARQGlySTQPNPRVGCVLVKDGQVVGEGWH--VRAGEP--HAEVHALRQAGE---NAR--GATAYVTLE 75
Cdd:PRK10860  13 HEYWMRHALTLAKRA--WDEREVPVGAVLVHNNRVIGEGWNrpIGRHDPtaHAEIMALRQGGLvlqNYRllDATLYVTLE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599251   76 PCSHfgrtppCADALVGAGVARVVAAMQDPNPEVAGRGLLRL----MQAGIAVQSGVLEAEARELNIGFIK--RMEH 146
Cdd:PRK10860  91 PCVM------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLhhpgMNHRVEITEGVLADECAALLSDFFRmrRQEI 161
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
 281-338 1.72e-06

Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 47.54  E-value: 1.72e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599251 281 HVDLHKLLLELAARGANEVLVEAGPRLAGAFARLGLVDEYRLFVAPKFLGsSARPLLD 338
Cdd:COG0262  88 SGDLEEALAALKAAGGKDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLG-EGDRLFP 144
cd PHA02588
deoxycytidylate deaminase; Provisional
 5-99 1.47e-05

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 44.75  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599251    5 DPLYMARALELARQglySTQPNPRVGCVLVKDGQVVGEG-------------------WHVRAG---------------- 49
Cdd:PHA02588   3 DSTYLQIAYLVSQE---SKCVSWKVGAVIEKNGRIISTGyngtpaggvnccdhaneqgWLDDEGklkkehrpehsawssk 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599251   50 -EPHAEVHALRQA---GENARGATAYVTLEPCshfgrtPPCADALVGAGVARVV 99
Cdd:PHA02588  80 nEIHAELNAILFAarnGISIEGATMYVTASPC------PDCAKAIAQSGIKKLV 127
 
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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