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Conserved domains on  [gi|499536768|ref|WP_011217551|]
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bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD [Photobacterium profundum]

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 ...
 6-367 0e+00

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: 515.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   6 DHSMMLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTP 85
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  86 PCAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTA 165
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 166 LSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEPVKAEYPETALRQPTRVIIDSKNRVTPDF 245
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQENLRQPVRIVIDSQNRVTPEH 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 246 KLFSLEGETLLARAEMGQETWPDSVTQVLIPKQDDseQLNLTSLMLELAKQDINHIWVEAGAELAGGLLAAGLVDELILY 325
Cdd:PRK10786 243 RIVQQPGETWLARTQEDSREWPETVRTLLLPEHNG--HLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 499536768 326 QAPKLMGCDSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRI 367
Cdd:PRK10786 321 IAPKLLGSDARGLCTLPGLEKLADAPQFKFSEIRHVGPDVCL 362
 
Name Accession Description Interval E-value
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 6-367 0e+00

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 515.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   6 DHSMMLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTP 85
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  86 PCAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTA 165
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 166 LSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEPVKAEYPETALRQPTRVIIDSKNRVTPDF 245
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQENLRQPVRIVIDSQNRVTPEH 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 246 KLFSLEGETLLARAEMGQETWPDSVTQVLIPKQDDseQLNLTSLMLELAKQDINHIWVEAGAELAGGLLAAGLVDELILY 325
Cdd:PRK10786 243 RIVQQPGETWLARTQEDSREWPETVRTLLLPEHNG--HLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 499536768 326 QAPKLMGCDSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRI 367
Cdd:PRK10786 321 IAPKLLGSDARGLCTLPGLEKLADAPQFKFSEIRHVGPDVCL 362
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 10-368 2.38e-147

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: 420.39  E-value: 2.38e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   10 MLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTPPCAQ 89
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   90 ALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTALSNG 169
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  170 ESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEpvkaeypetalrQPTRVIIDSKNRVTPDFKLFS 249
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATE------------QPLRVVLDTQLRIPEFAKLIP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  250 LEGETLLARAEMGQETWPDSVTQVLIPKqddsEQLNLTSLMLELAKQDINHIWVEAGAELAGGLLAAGLVDELILYQAPK 329
Cdd:TIGR00326 229 QIAPTWIFTTARDKKKRLEAFEVNIFPL----EKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 499536768  330 LMGC-DSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRII 368
Cdd:TIGR00326 305 LLGGtHAPGLCSEPGFQKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 7-294 2.57e-135

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: 388.26  E-value: 2.57e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   7 HSMMLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTPP 86
Cdd:COG0117    1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  87 CAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTAL 166
Cdd:COG0117   81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 167 SNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEPVKAEYPETALRQPTRVIIDSKNRVTPDFK 246
Cdd:COG0117  161 ANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499536768 247 LFSLEGETLLARAEMGQETWPDSVTQVLIPKQDDSEQLNLTSLMLELA 294
Cdd:COG0117  241 TVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLL 288
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 10-122 2.21e-57

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: 182.43  E-value: 2.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  10 MLRAIELAKRGRFTTAPNPNVGCIIAQGA-TIVGEGFHYQAGQPHAEVFALRAAGEQ-AKGATAYVTLEPCSHFGRTPPC 87
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499536768  88 AQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAG 122
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 ...
 150-365 7.43e-45

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: 152.92  E-value: 7.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  150 PYVQLKLAASLDGRTALSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEpvkaeypetALRQ 229
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGRA---------AERQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  230 PTRVIIDSKNRVTPDFKLFSLEGETLLARAEMGQETWPDSVTQVlipkqddseQLNLTSLMLELAKQDINHIWVEAGAEL 309
Cdd:pfam01872  72 PPRVVVDSTLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL---------RVDLKELLRELKERGIRSLLVEGGATL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499536768  310 AGGLLAAGLVDELILYQAPKLMGCDSRSLINLKGLtsmsQVLNLEITDVRMIGPDL 365
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRTLFGGEGF----LALKLKLVSSEAIGNGV 194
 
Name Accession Description Interval E-value
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 6-367 0e+00

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 515.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   6 DHSMMLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTP 85
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  86 PCAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTA 165
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 166 LSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEPVKAEYPETALRQPTRVIIDSKNRVTPDF 245
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQENLRQPVRIVIDSQNRVTPEH 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 246 KLFSLEGETLLARAEMGQETWPDSVTQVLIPKQDDseQLNLTSLMLELAKQDINHIWVEAGAELAGGLLAAGLVDELILY 325
Cdd:PRK10786 243 RIVQQPGETWLARTQEDSREWPETVRTLLLPEHNG--HLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 499536768 326 QAPKLMGCDSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRI 367
Cdd:PRK10786 321 IAPKLLGSDARGLCTLPGLEKLADAPQFKFSEIRHVGPDVCL 362
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 10-368 2.38e-147

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: 420.39  E-value: 2.38e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   10 MLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTPPCAQ 89
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   90 ALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTALSNG 169
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  170 ESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEpvkaeypetalrQPTRVIIDSKNRVTPDFKLFS 249
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEATE------------QPLRVVLDTQLRIPEFAKLIP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  250 LEGETLLARAEMGQETWPDSVTQVLIPKqddsEQLNLTSLMLELAKQDINHIWVEAGAELAGGLLAAGLVDELILYQAPK 329
Cdd:TIGR00326 229 QIAPTWIFTTARDKKKRLEAFEVNIFPL----EKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 499536768  330 LMGC-DSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRII 368
Cdd:TIGR00326 305 LLGGtHAPGLCSEPGFQKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 7-294 2.57e-135

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: 388.26  E-value: 2.57e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   7 HSMMLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTPP 86
Cdd:COG0117    1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  87 CAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTAL 166
Cdd:COG0117   81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 167 SNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEPVKAEYPETALRQPTRVIIDSKNRVTPDFK 246
Cdd:COG0117  161 ANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGENPPRRVVVDDLLLRPPPALLLVANDAALIIV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499536768 247 LFSLEGETLLARAEMGQETWPDSVTQVLIPKQDDSEQLNLTSLMLELA 294
Cdd:COG0117  241 TVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLL 288
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 6-235 3.94e-70

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 224.27  E-value: 3.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   6 DHSMMLRAIELAKRGRFTTAPNPNVGCIIAQGATIVGEGFHYQAGQPHAEVFALRAAGEQAKGATAYVTLEPCSHFGRTP 85
Cdd:PLN02807  32 DSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGRTP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  86 PCAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMKTGLPYVQLKLAASLDGRTA 165
Cdd:PLN02807 112 PCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGCLL 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 166 LSNGESKWITGPEARADVQRFRAragAILSTSSTviADDPSLNVRwselgepvkaeypETALRQPTRVII 235
Cdd:PLN02807 192 NQIGEGADDAGGYYSQLLQEYDA---VILSSALA--DADPLPLSQ-------------EAGAKQPLRIII 243
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
 147-371 2.35e-69

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: 216.95  E-value: 2.35e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 147 TGLPYVQLKLAASLDGRTALSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGepvkaeypeta 226
Cdd:COG1985    1 TGRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGLG----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 227 lRQPTRVIIDSKNRVTPDFKLFSLEGETLL-----ARAEMGQETWPDSVTQVLIPkqdDSEQLNLTSLMLELAKQDINHI 301
Cdd:COG1985   70 -RQPLRVVVDSSLRLPPDARLFDDAAPTLVltteaADAERRAALEAAGAEVIVLP---GDGRVDLAALLAALAERGIRSV 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 302 WVeagaelaggllaaglVDELILYQAPKLMGCDSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRIIARV 371
Cdd:COG1985  146 LVeggptlagsflaaglVDELILYIAPKLLGGDGPTLVGGPGLETLADAPRLRLVSVRRLGDDLLLRYRP 215
ribD_Cterm TIGR00227
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ...
 148-371 1.74e-65

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: 206.85  E-value: 1.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  148 GLPYVQLKLAASLDGRTALSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELgepvkaeypeTAL 227
Cdd:TIGR00227   1 GRPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRWVEL----------DEL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  228 RQPTRVIIDSKNRVTPDFKLFSLEGETLLARAEMGQET----WPDSVTQVLIPKQddsEQLNLTSLMLELAKQDINHIWV 303
Cdd:TIGR00227  71 RNPVRVVLDSRLRVPPTARLLNDDAPTWVATSEPADEEkvkeLEDFGVEVLVLET---KRVDLKKLMEILYEEGIRSVMV 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499536768  304 EAGAELAGGLLAAGLVDELILYQAPKLMGC-DSRSLINLKGLTSMSQVLNLEITDVRMIGPDLRIIARV 371
Cdd:TIGR00227 148 EGGGTLNGSLLKEGLVDELIVYIAPKLLGGrDAPTLVDGEGFQKMADAPNLELKEIYQIGEDIVLTAKL 216
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 10-122 2.21e-57

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: 182.43  E-value: 2.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  10 MLRAIELAKRGRFTTAPNPNVGCIIAQGA-TIVGEGFHYQAGQPHAEVFALRAAGEQ-AKGATAYVTLEPCSHFGRTPPC 87
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499536768  88 AQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAG 122
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 ...
 150-365 7.43e-45

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: 152.92  E-value: 7.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  150 PYVQLKLAASLDGRTALSNGESKWITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEpvkaeypetALRQ 229
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRWVKGRA---------AERQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  230 PTRVIIDSKNRVTPDFKLFSLEGETLLARAEMGQETWPDSVTQVlipkqddseQLNLTSLMLELAKQDINHIWVEAGAEL 309
Cdd:pfam01872  72 PPRVVVDSTLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL---------RVDLKELLRELKERGIRSLLVEGGATL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499536768  310 AGGLLAAGLVDELILYQAPKLMGCDSRSLINLKGLtsmsQVLNLEITDVRMIGPDL 365
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRTLFGGEGF----LALKLKLVSSEAIGNGV 194
PRK05625 PRK05625
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
 150-362 4.17e-22

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


Pssm-ID: 180169  Cd Length: 217  Bit Score: 93.00  E-value: 4.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 150 PYVQLKLAASLDGRTALSNGESKwITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSELGEPvkaeypetalRQ 229
Cdd:PRK05625   3 PYVIVNAAMSADGKLATKTRYSR-ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAAGKP----------EN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 230 PTRVIIDSKNRVTPDFKLFSLEGETLLARAEmgqETWPDSVTQ-----VLIPKQDDsEQLNLTSLMLELAKQDINHIWVE 304
Cdd:PRK05625  72 PIRVVVDSSARTPPDARILDGPAKTIVAVSE---AAPSEKVEElekkgAEVIVAGG-ERVDLPDLLEDLYERGIKRLMVE 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499536768 305 AGAELAGGLLAAGLVDELILYQAPKLMGC-DSRSLINLKGLTSMSQVLNLEITDVRMIG 362
Cdd:PRK05625 148 GGGTLIWSMFKEGLVDEVRVTVGPKIIGGkDAPTLADGEGFIEEEDPLKLELAKVCRCD 206
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-102 1.42e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 85.43  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768    6 DHSMMLRAIELAKRGRftTAPNPNVGCII-AQGATIVGEGFH-YQAGQP---HAEVFALRAA-----GEQAKGATAYVTL 75
Cdd:pfam00383   2 DEYFMRLALKAAKRAY--PYSNFPVGAVIvKKDGEIIATGYNgENAGYDptiHAERNAIRQAgkrgeGVRLEGATLYVTL 79

                          90       100
                  ....*....|....*....|....*..
gi 499536768   76 EPCSHfgrtppCAQALINANVSRVVCA 102
Cdd:pfam00383  80 EPCGM------CAQAIIESGIKRVVFG 100
rib_reduct_arch TIGR01508
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ...
 150-362 9.60e-18

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: 81.01  E-value: 9.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  150 PYVQLKLAASLDGRTALSNGESKwITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRWSelgepvKAEypetalRQ 229
Cdd:TIGR01508   1 PYVIVNVAMSLDGKLATINRDSR-ISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTVKKI------KSD------RN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  230 PTRVIIDSKNRVTPDFKLFSLEGETLLARAEMGQETWPDSVTQ-VLIPKQDDSEQLNLTSLMLELAKQDINHIWVEAGAE 308
Cdd:TIGR01508  68 PVRVVVDSKLRVPLNARILNKDAKTIIATSEDEPEEKVEELEDkGVEVVKFGEGRVDLKKLLDILYDKGVRRLMVEGGGT 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499536768  309 LAGGLLAAGLVDELILYQAPKLMGC-DSRSLINLKGLTSMSQVlNLEITDVRMIG 362
Cdd:TIGR01508 148 LIWSLFKENLVDEISVYIAPKIFGGrDAPTYVDGEGFKTEDCP-KLELKNFYRLG 201
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 6-137 6.65e-17

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: 76.70  E-value: 6.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   6 DHSMMLRAIELAKRGRfttAPN--PnVGCIIAQGATIVGEGF--HYQAGQP--HAEVFALRAAGEQAK-----GATAYVT 74
Cdd:COG0590    4 DEEFMRRALELARKAV---AEGevP-VGAVLVKDGEIIARGHnrVETLNDPtaHAEILAIRAAARKLGnwrlsGCTLYVT 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499536768  75 LEPCshfgrtPPCAQALINANVSRVVCAmvDPNPKVGGRG--IEMLKIA----GIEVQTGLLAADAQAL 137
Cdd:COG0590   80 LEPC------PMCAGAIVWARIGRVVYG--ASDPKAGAAGsiYDLLADPrlnhRVEVVGGVLAEECAAL 140
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
30-126 3.81e-14

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 69.10  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  30 VGCIIAQGATIVGEGFHYQAGQpHAEVFA-LRAA--GEQAKGATAYVTLEPCSHfgrtppCAQALINANVSRVVCAmvdp 106
Cdd:COG2131   58 VGCLREKLGIPSGERGECCRTV-HAEQNAiLQAArhGVSTEGATLYVTHFPCLE------CAKMIIQAGIKRVVYL---- 126

                         90       100
                 ....*....|....*....|
gi 499536768 107 NPKVGGRGIEMLKIAGIEVQ 126
Cdd:COG2131  127 EDYPDELAKELLKEAGVEVR 146
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 10-116 1.03e-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: 66.87  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  10 MLRAIELAKRGR-FTTAPnpnVGCIIAQGA-TIVGEGfH---YQAGQP--HAEVFALRAAGEQ-----AKGATAYVTLEP 77
Cdd:cd01285    1 MRLAIELARKALaEGEVP---FGAVIVDDDgKVIARG-HnrvEQDGDPtaHAEIVAIRNAARRlgsylLSGCTLYTTLEP 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499536768  78 CshfgrtPPCAQALINANVSRVVCAMVDPNPKVGGRGIE 116
Cdd:cd01285   77 C------PMCAGALLWARIKRVVYGASDPKLGGIGFLIE 109
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-146 1.23e-13

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: 67.55  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768    5 IDH--SMMLRAIELAKRGRFTTAPnpnVGCIIAQGATIVGEGFHYQAGQ----PHAEVFALRAAGEQ-----AKGATAYV 73
Cdd:pfam14437   1 ENHekWFRKALGLAEKAYDAGEVP---IGAVIVKDGKVIARGYNRKELNadttAHAEILAIQQAAKKlgswrLDDATLYV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499536768   74 TLEPCshfgrtPPCAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAGIEVQTGLLAADAQALNFGFIKRMK 146
Cdd:pfam14437  78 TLEPC------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVLWNHRVELVEEDCSEILKGFFKKLR 144
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 10-103 1.74e-11

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: 60.26  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  10 MLRAIELAKRGrFTTAPNPNVG-CII-AQGATIVGEGFH--YQAGQP--HAEVFALRAAG--EQAKGATAYVTLEPCSHf 81
Cdd:cd00786    1 MTEALKAADLG-YAKESNFQVGaCLVnKKDGGKVGRGCNieNAAYSMcnHAERTALFNAGseGDTKGQMLYVALSPCGA- 78

                         90       100
                 ....*....|....*....|..
gi 499536768  82 grtppCAQALINANVSRVVCAM 103
Cdd:cd00786   79 -----CAQLIIELGIKDVIVVL 95
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 10-144 6.27e-11

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 60.59  E-value: 6.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768  10 MLRAIELAKRGrFTTAPNPnVGCIIAQGATIVGEGFHYQAGQ----PHAEVFALRAAGEQAKG-----ATAYVTLEPCSH 80
Cdd:PRK10860  17 MRHALTLAKRA-WDEREVP-VGAVLVHNNRVIGEGWNRPIGRhdptAHAEIMALRQGGLVLQNyrlldATLYVTLEPCVM 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499536768  81 fgrtppCAQALINANVSRVVCAMVDPNPKVGGRGIEMLKIAG----IEVQTGLLAADAQALNFGFIKR 144
Cdd:PRK10860  95 ------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGmnhrVEITEGVLADECAALLSDFFRM 156
PRK14719 PRK14719
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
 149-357 2.31e-10

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


Pssm-ID: 237801 [Multi-domain]  Cd Length: 360  Bit Score: 61.49  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 149 LPYVQLKLAASLDGRTALSNGESKwITGPEARADVQRFRARAGAILSTSSTVIADDPSLNVRwselgepvkaEYPETALR 228
Cdd:PRK14719 139 LPYVISNVGMTLDGKLATIENDSR-ISGENDLKRVHEIRKDVDAIMVGIGTVLKDDPRLTVH----------KINASPKD 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768 229 QPTRVIIDSKNRVTPDFKLFSLEGETLLARAEMGQETWPDSVTQV----LIPKQDDSEQLNLTSLMLELAKQDINHIWVE 304
Cdd:PRK14719 208 NPLRIVVDSNLKIPLNARVLNKDAKTVIATTTPISDEKEEKIRKLkemgITVLQAGVQKVDLRKIMNEIYKMGINKILLE 287

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499536768 305 AGAELAGGLLAAGLVDELILYQAPKLM-GCDSRSLINLKGLTSMSQVLNLEITD 357
Cdd:PRK14719 288 GGGTLNWGMFKENLINEVRVYIAPKVFgGANSPTYVDGEGFKNVEECTKLELKN 341
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 6-119 7.50e-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: 56.51  E-value: 7.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499536768   6 DHSMMLrAIELAKRgrfTTAPNPNVGCIIAQGATIVGEGF--------------HYQAGQP-----------HAEVFALR 60
Cdd:cd01286    2 EYFMAI-ARLAALR---STCPRRQVGAVIVKDKRIISTGYngspsglphcaevgCERDDLPsgedqkccrtvHAEQNAIL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499536768  61 AA---GEQAKGATAYVTLEPCSHfgrtppCAQALINANVSRVVCAmvDPNPKVGGRGIEMLK 119
Cdd:cd01286   78 QAarhGVSLEGATLYVTLFPCIE------CAKLIIQAGIKKVVYA--EPYDDDDPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 53-125 9.08e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 45.52  E-value: 9.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499536768  53 HAEVFALRAA---GEQAKGATAYVTLEPCshfgrtPPCAQALINANVSRVV-CAMVDPNPKvggRGIEMLKIAGIEV 125
Cdd:PHA02588  83 HAELNAILFAarnGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVyCEKYDRNGP---GWDDILRKSGIEV 150
 
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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