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Conserved domains on  [gi|504233478|ref|WP_014420580|]
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MULTISPECIES: bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD [Marinobacter]

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 ...
6-368 7.44e-147

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: 419.94  E-value: 7.44e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   6 DRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTP 85
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  86 PCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTA 165
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 166 MASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDIGDATDPS---RQPLRVIADRDARTPATA 242
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQenlRQPVRIVIDSQNRVTPEH 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 243 RILQGGnvqvfcASSTLASGPAQDLA-ALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDE 321
Cdd:PRK10786 243 RIVQQP------GETWLARTQEDSREwPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDE 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 504233478 322 LWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLIL 368
Cdd:PRK10786 317 LIVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPDVCLHL 364
 
Name Accession Description Interval E-value
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
6-368 7.44e-147

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 419.94  E-value: 7.44e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   6 DRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTP 85
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  86 PCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTA 165
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 166 MASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDIGDATDPS---RQPLRVIADRDARTPATA 242
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQenlRQPVRIVIDSQNRVTPEH 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 243 RILQGGnvqvfcASSTLASGPAQDLA-ALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDE 321
Cdd:PRK10786 243 RIVQQP------GETWLARTQEDSREwPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDE 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 504233478 322 LWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLIL 368
Cdd:PRK10786 317 LIVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPDVCLHL 364
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
10-367 1.57e-143

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: 410.37  E-value: 1.57e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   10 MARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPPCAR 89
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   90 ALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAMASG 169
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  170 ESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMgdigdatdpSRQPLRVIADRDARTPATARILQGgn 249
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEA---------TEQPLRVVLDTQLRIPEFAKLIPQ-- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  250 vqvfcASSTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPV 329
Cdd:TIGR00326 230 -----IAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 504233478  330 FLGSTGRPT--AHLPLETMADKVQWKVLDRRQVGEDQRLI 367
Cdd:TIGR00326 305 LLGGTHAPGlcSEPGFQKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
7-328 1.72e-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: 388.65  E-value: 1.72e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   7 RAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPP 86
Cdd:COG0117    1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  87 CARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAM 166
Cdd:COG0117   81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 167 ASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGdigdatdpsRQPLRVIADRDARTPATARILQ 246
Cdd:COG0117  161 ANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGE---------NPPRRVVVDDLLLRPPPALLLV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 247 GGNVQVFCAssTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQ 326
Cdd:COG0117  232 ANDAALIIV--TVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDL 309

                 ..
gi 504233478 327 AP 328
Cdd:COG0117  310 LL 311
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
10-122 1.23e-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: 175.50  E-value: 1.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  10 MARAVQLAWRGRYSTHPNPRVGCVIAKGD-LIVGEGWHERAGEAHAEVRALSQAGHE-ARGATAYVTLEPCSHYGRTPPC 87
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504233478  88 ARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAG 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 ...
150-363 4.45e-52

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: 171.79  E-value: 4.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  150 PWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRdemgdiGDATDPSRQPLR 229
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRW------VKGRAAERQPPR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  230 VIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALgvsltgvawkdnGVDVAELLDALGELGINELLVEAGPTL 309
Cdd:pfam01872  75 VVVDSTLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL------------RVDLKELLRELKERGIRSLLVEGGATL 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504233478  310 AGTFIGENLVDELWLYQAPVFLGSTGRPtahLPLETMADKVQWKVLDRRQVGED 363
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRT---LFGGEGFLALKLKLVSSEAIGNG 193
 
Name Accession Description Interval E-value
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
6-368 7.44e-147

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 419.94  E-value: 7.44e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   6 DRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTP 85
Cdd:PRK10786   3 DEFYMARALKLAQRGRFTTHPNPNVGCVIVKDGEIVGEGYHQRAGEPHAEVHALRMAGEKAKGATAYVTLEPCSHHGRTP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  86 PCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTA 165
Cdd:PRK10786  83 PCCDALIAAGVARVVAAMQDPNPQVAGRGLYRLQQAGIDVSHGLMMSEAEALNKGFLKRMRTGFPYIQLKLGASLDGRTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 166 MASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDIGDATDPS---RQPLRVIADRDARTPATA 242
Cdd:PRK10786 163 MASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWSELDAQTQALYPQenlRQPVRIVIDSQNRVTPEH 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 243 RILQGGnvqvfcASSTLASGPAQDLA-ALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDE 321
Cdd:PRK10786 243 RIVQQP------GETWLARTQEDSREwPETVRTLLLPEHNGHLDLVVLMMQLGKQQINSIWVEAGPTLAGALLQAGLVDE 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 504233478 322 LWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLIL 368
Cdd:PRK10786 317 LIVYIAPKLLGSDARGLCTLPgLEKLADAPQFKFSEIRHVGPDVCLHL 364
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
10-367 1.57e-143

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: 410.37  E-value: 1.57e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   10 MARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPPCAR 89
Cdd:TIGR00326   1 MNRALDLAKKGQGTTHPNPLVGCVIVKNGEIVGEGAHQKAGEPHAEVHALRQAGENAKGATAYVTLEPCSHQGRTPPCAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   90 ALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAMASG 169
Cdd:TIGR00326  81 AIIEAGIKKVVVSMQDPNPLVAGRGAERLKQAGIEVTFGILKEEAERLNKGFLKRMRTGLPYVQLKLAASLDGKIATASG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  170 ESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMgdigdatdpSRQPLRVIADRDARTPATARILQGgn 249
Cdd:TIGR00326 161 ESKWITSEAARTDAQQLRAQSDAILVGGGTVKADNPALTARLDEA---------TEQPLRVVLDTQLRIPEFAKLIPQ-- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  250 vqvfcASSTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPV 329
Cdd:TIGR00326 230 -----IAPTWIFTTARDKKKRLEAFEVNIFPLEKVTIREVMTQLGKRGINSVLVEGGPNLLGSFLDEGLVDELIIYIAPK 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 504233478  330 FLGSTGRPT--AHLPLETMADKVQWKVLDRRQVGEDQRLI 367
Cdd:TIGR00326 305 LLGGTHAPGlcSEPGFQKMADALNFKFLEINQIGPDILLT 344
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
7-328 1.72e-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: 388.65  E-value: 1.72e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   7 RAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGRTPP 86
Cdd:COG0117    1 ERYMRRALELARRGLGTTSPNPLVGCVIVKDGRIVGEGYHQRAGGPHAEVNALAQAGEAARGATLYVTLEPCSHHGRTPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  87 CARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGRTAM 166
Cdd:COG0117   81 CADALIEAGIKRVVIAMLDPNPLVAGKGIARLRAAGIEVEVGVLEEEARALNRGFLKRMRTGRPFVTLKLAMSLDGKIAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 167 ASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGdigdatdpsRQPLRVIADRDARTPATARILQ 246
Cdd:COG0117  161 ANGESQWITGEEARADVHRLRARSDAILVGIGTVLADDPSLTVRLPGGE---------NPPRRVVVDDLLLRPPPALLLV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 247 GGNVQVFCAssTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQ 326
Cdd:COG0117  232 ANDAALIIV--TVTADAAAALAALAAEAGVVLLLVGGLLLLALLLLLLLLLLLLLLLLLLLGGGGGLAAAALLAALLLDL 309

                 ..
gi 504233478 327 AP 328
Cdd:COG0117  310 LL 311
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
147-371 3.34e-86

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: 259.71  E-value: 3.34e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 147 TGRPWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGdigdatdpsRQ 226
Cdd:COG1985    1 TGRPYVTLKLAMSLDGKIATADGESKWITGEAARRDVHRLRARADAILVGAGTVLADDPSLTVRLPGLG---------RQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 227 PLRVIADRDARTPATARILQ-GGNVQVFCASSTlASGPAQDLAALGVSLTgVAWKDNGVDVAELLDALGELGINELLVEA 305
Cdd:COG1985   72 PLRVVVDSSLRLPPDARLFDdAAPTLVLTTEAA-DAERRAALEAAGAEVI-VLPGDGRVDLAALLAALAERGIRSVLVEG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233478 306 GPTLAGTFIGENLVDELWLYQAPVFLGSTGRPTAHLP-LETMADKVQWKVLDRRQVGEDQRLILARH 371
Cdd:COG1985  150 GPTLAGSFLAAGLVDELILYIAPKLLGGDGPTLVGGPgLETLADAPRLRLVSVRRLGDDLLLRYRPR 216
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
4-363 6.68e-65

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 210.78  E-value: 6.68e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   4 DRDRAMMARAVQLAWRGRYSTHPNPRVGCVIAKGDLIVGEGWHERAGEAHAEVRALSQAGHEARGATAYVTLEPCSHYGR 83
Cdd:PLN02807  30 DDDSFYMRRCVELARKAIGCTSPNPMVGCVIVKDGRIVGEGFHPKAGQPHAEVFALRDAGDLAENATAYVSLEPCNHYGR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  84 TPPCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAGIRVTEGVMADEASRLNPGFMKRMNTGRPWVRLKMAASLDGR 163
Cdd:PLN02807 110 TPPCTEALIKAKVKRVVVGMVDPNPIVASKGIERLRDAGIEVTVGVEEELCRKLNEAFIHRMLTGKPFVTLRYSMSMNGC 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 164 TAMASGESqwitGPEARADVQRLRAISDAILTGvGTVLADDPSLTVRrdEMGdigdatdpSRQPLRVIADRDARTPATAR 243
Cdd:PLN02807 190 LLNQIGEG----ADDAGGYYSQLLQEYDAVILS-SALADADPLPLSQ--EAG--------AKQPLRIIIARSESSPLQIP 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 244 IL---QGGNVQVFCASSTLAsgpAQDLAALGVSLTGVawkdNGVDVAELLDALGELGINELLVEA-GPT-----LAGTFI 314
Cdd:PLN02807 255 SLreeSAAKVLVLADKESSA---EPVLRRKGVEVVVL----NQINLDSILDLCYQRGLCSVLLDLrGNVgglesLLKDAL 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 504233478 315 GENLVDELWLYQAPVFLGSTGRPTAhlpLETMADKVQWKVLDRRQVGED 363
Cdd:PLN02807 328 EDKLLQKVVVEVLPFWSGSQGQSIA---SFGGSQSFKLKRLTSREVGGS 373
ribD_Cterm TIGR00227
riboflavin-specific deaminase C-terminal domain; Eubacterial riboflavin-specific deaminases ...
148-363 1.23e-63

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: 202.23  E-value: 1.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  148 GRPWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMgdigdatDPSRQP 227
Cdd:TIGR00227   1 GRPYVILKYAMSLDGKIATASGESSWITSEEARRDVHQLRAQSDAILVGSGTVLADDPRLTVRWVEL-------DELRNP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  228 LRVIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALGVSLtgVAWKDNGVDVAELLDALGELGINELLVEAGP 307
Cdd:TIGR00227  74 VRVVLDSRLRVPPTARLLNDDAPTWVATSEPADEEKVKELEDFGVEV--LVLETKRVDLKKLMEILYEEGIRSVMVEGGG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504233478  308 TLAGTFIGENLVDELWLYQAPVFLGSTGRPT--AHLPLETMADKVQWKVLDRRQVGED 363
Cdd:TIGR00227 152 TLNGSLLKEGLVDELIVYIAPKLLGGRDAPTlvDGEGFQKMADAPNLELKEIYQIGED 209
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
10-122 1.23e-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: 175.50  E-value: 1.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  10 MARAVQLAWRGRYSTHPNPRVGCVIAKGD-LIVGEGWHERAGEAHAEVRALSQAGHE-ARGATAYVTLEPCSHYGRTPPC 87
Cdd:cd01284    1 MRRALELAEKGRGLTSPNPPVGCVIVDDDgEIVGEGYHRKAGGPHAEVNALASAGEKlARGATLYVTLEPCSHHGKTPPC 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504233478  88 ARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAG 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 ...
150-363 4.45e-52

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: 171.79  E-value: 4.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  150 PWVRLKMAASLDGRTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRdemgdiGDATDPSRQPLR 229
Cdd:pfam01872   1 PYVILKFAISLDGKIAAAGGSSQWITGEEARADVHQLRAEADAILVGRGTVRADNPSLTVRW------VKGRAAERQPPR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  230 VIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALgvsltgvawkdnGVDVAELLDALGELGINELLVEAGPTL 309
Cdd:pfam01872  75 VVVDSTLRVPLDARVLNDDAPTLVATTEPADKEKVEKLKVL------------RVDLKELLRELKERGIRSLLVEGGATL 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504233478  310 AGTFIGENLVDELWLYQAPVFLGSTGRPtahLPLETMADKVQWKVLDRRQVGED 363
Cdd:pfam01872 143 AGSLLRAGLVDELRLYIAPKLLGGGGRT---LFGGEGFLALKLKLVSSEAIGNG 193
PRK05625 PRK05625
5-amino-6-(5-phosphoribosylamino)uracil reductase; Validated
149-338 6.13e-38

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


Pssm-ID: 180169  Cd Length: 217  Bit Score: 135.37  E-value: 6.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 149 RPWVRLKMAASLDGRTAMASGESQwITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVRRDEMGDigdatdpSRQPL 228
Cdd:PRK05625   2 RPYVIVNAAMSADGKLATKTRYSR-ISGPEDFDRVHELRAEVDAVMVGIGTVLADDPSLTVHRYAAGK-------PENPI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 229 RVIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALGVSLtgVAWKDNGVDVAELLDALGELGINELLVEAGPT 308
Cdd:PRK05625  74 RVVVDSSARTPPDARILDGPAKTIVAVSEAAPSEKVEELEKKGAEV--IVAGGERVDLPDLLEDLYERGIKRLMVEGGGT 151
                        170       180       190
                 ....*....|....*....|....*....|
gi 504233478 309 LAGTFIGENLVDELWLYQAPVFLGSTGRPT 338
Cdd:PRK05625 152 LIWSMFKEGLVDEVRVTVGPKIIGGKDAPT 181
rib_reduct_arch TIGR01508
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 1'-reductase, archaeal; This model ...
150-338 1.22e-34

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: 126.84  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  150 PWVRLKMAASLDGRTAMASGESQwITGPEARADVQRLRAISDAILTGVGTVLADDPSLTVrrdemgdigDATDPSRQPLR 229
Cdd:TIGR01508   1 PYVIVNVAMSLDGKLATINRDSR-ISCEEDLIRVHEIRAEVDAIMVGIGTVLADDPRLTV---------KKIKSDRNPVR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  230 VIADRDARTPATARILQGGNVQVFCASSTLASGPAQDLAALGVSLtgVAWKDNGVDVAELLDALGELGINELLVEAGPTL 309
Cdd:TIGR01508  71 VVVDSKLRVPLNARILNKDAKTIIATSEDEPEEKVEELEDKGVEV--VKFGEGRVDLKKLLDILYDKGVRRLMVEGGGTL 148
                         170       180
                  ....*....|....*....|....*....
gi 504233478  310 AGTFIGENLVDELWLYQAPVFLGSTGRPT 338
Cdd:TIGR01508 149 IWSLFKENLVDEISVYIAPKIFGGRDAPT 177
PRK14719 PRK14719
bifunctional RNAse/5-amino-6-(5-phosphoribosylamino)uracil reductase; Provisional
113-338 4.11e-24

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


Pssm-ID: 237801 [Multi-domain]  Cd Length: 360  Bit Score: 101.55  E-value: 4.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 113 RGL---DMLREAGIRVTEGVMADEASrLNPGFMKRMNTGR-------PWVRLKMAASLDGRTAMASGESQwITGPEARAD 182
Cdd:PRK14719  94 RGIkvnNLIRKEIIKYSRGDLKDIES-LYPYISRRININSdlsdimlPYVISNVGMTLDGKLATIENDSR-ISGENDLKR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 183 VQRLRAISDAILTGVGTVLADDPSLTVRRDEmgdigdaTDPSRQPLRVIADRDARTPATARILQGgNVQVFCASSTLASG 262
Cdd:PRK14719 172 VHEIRKDVDAIMVGIGTVLKDDPRLTVHKIN-------ASPKDNPLRIVVDSNLKIPLNARVLNK-DAKTVIATTTPISD 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 263 PAQD----LAALGVSL--TGVawkdNGVDVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPVFLGSTGR 336
Cdd:PRK14719 244 EKEEkirkLKEMGITVlqAGV----QKVDLRKIMNEIYKMGINKILLEGGGTLNWGMFKENLINEVRVYIAPKVFGGANS 319

                 ..
gi 504233478 337 PT 338
Cdd:PRK14719 320 PT 321
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
4-137 4.06e-18

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: 80.16  E-value: 4.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   4 DRDRAMMARAVQLAWRGRYS-THPnprVGCVIAKGDLIVGEGWHERAGE----AHAEVRALSQAG-----HEARGATAYV 73
Cdd:COG0590    2 EDDEEFMRRALELARKAVAEgEVP---VGAVLVKDGEIIARGHNRVETLndptAHAEILAIRAAArklgnWRLSGCTLYV 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233478  74 TLEPCshygrtPPCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREA----GIRVTEGVMADEASRL 137
Cdd:COG0590   79 TLEPC------PMCAGAIVWARIGRVVYGASDPKAGAAGSIYDLLADPrlnhRVEVVGGVLAEECAAL 140
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-102 8.59e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 77.73  E-value: 8.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478    6 DRAMMARAVQLAWRGRysTHPNPRVGCVIAKGD-LIVGEGWH-ERAG---EAHAEVRALSQA-----GHEARGATAYVTL 75
Cdd:pfam00383   2 DEYFMRLALKAAKRAY--PYSNFPVGAVIVKKDgEIIATGYNgENAGydpTIHAERNAIRQAgkrgeGVRLEGATLYVTL 79
                          90       100
                  ....*....|....*....|....*..
gi 504233478   76 EPCSHygrtppCARALIDAGVAHVFAA 102
Cdd:pfam00383  80 EPCGM------CAQAIIESGIKRVVFG 100
PRK14059 PRK14059
pyrimidine reductase family protein;
144-339 8.59e-17

pyrimidine reductase family protein;


Pssm-ID: 184482  Cd Length: 251  Bit Score: 78.85  E-value: 8.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 144 RMNTGRPWVRLKMAASLDGrTAMASGESQWITGPEARADVQRLRAISDAILTGVGTVLADDPSLTV----RRDEMGDIGD 219
Cdd:PRK14059  25 PDGLDRPWLRANFVTSLDG-AATVDGRSGGLGGPADRRVFGLLRALADVVVVGAGTVRAENYGGVRlsaaARQQRQARGQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478 220 ATDPsrqPLRVIAdRDARTPATARILQGGNVQ-VFCASSTLASGPAQDLAALGVSLTGVAWKDNGVDVAELLDALGELGI 298
Cdd:PRK14059 104 AEVP---PIAVVS-RSGDLDPDSRLFTETEVPpLVLTCAAAAADRRRRLAGLAEVADVVVAGPDTVDLAAAVAALAARGL 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504233478 299 NELLVEAGPTLAGTFIGENLVDELWLYQAPVFLGSTGRPTA 339
Cdd:PRK14059 180 RRILCEGGPTLLGQLLAADLVDELCLTIAPVLAGGVARRIV 220
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
4-125 1.29e-14

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 70.64  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   4 DRDRAMMARAVQLAWRgrySTHPNPRVGCVIAKGDLIVG---------------EGW------------HERAGEAHAEV 56
Cdd:COG2131    7 SWDEYFMEIAKLVALR---STCLRRQVGAVIVKDKRILAtgyngapsglphcdeVGClreklgipsgerGECCRTVHAEQ 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233478  57 RALSQA---GHEARGATAYVTLEPCSHygrtppCARALIDAGVAHVFAATKDPNPsvsgRGLDMLREAGIRV 125
Cdd:COG2131   84 NAILQAarhGVSTEGATLYVTHFPCLE------CAKMIIQAGIKRVVYLEDYPDE----LAKELLKEAGVEV 145
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
10-119 1.77e-13

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: 66.91  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  10 MARAVQLAWRgrySTHPNPRVGCVIAKGDLIVG--------------EGWHERAGE-----------AHAEVRALSQA-- 62
Cdd:cd01286    5 MAIARLAALR---STCPRRQVGAVIVKDKRIIStgyngspsglphcaEVGCERDDLpsgedqkccrtVHAEQNAILQAar 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504233478  63 -GHEARGATAYVTLEPCSHygrtppCARALIDAGVAHVFAAtkDPNPSVSGRGLDMLR 119
Cdd:cd01286   82 hGVSLEGATLYVTLFPCIE------CAKLIIQAGIKKVVYA--EPYDDDDPAAAELLE 131
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
5-144 4.84e-13

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 66.75  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478   5 RDRAMMARAVQLAWRGrYSTHPNPrVGCVIAKGDLIVGEGWHERAGE----AHAEVRALSQAGHEARG-----ATAYVTL 75
Cdd:PRK10860  12 SHEYWMRHALTLAKRA-WDEREVP-VGAVLVHNNRVIGEGWNRPIGRhdptAHAEIMALRQGGLVLQNyrlldATLYVTL 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233478  76 EPCSHygrtppCARALIDAGVAHVFAATKDPNPSVSGRGLDMLREAG----IRVTEGVMADEASRLNPGFMKR 144
Cdd:PRK10860  90 EPCVM------CAGAMVHSRIGRLVFGARDAKTGAAGSLMDVLHHPGmnhrVEITEGVLADECAALLSDFFRM 156
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
10-102 9.50e-12

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 60.64  E-value: 9.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  10 MARAVQLAWRGrYSTHPNPRVGCVI--AKGDLIVGEGWHER----AGEAHAEVRALSQAGHEA--RGATAYVTLEPCSHy 81
Cdd:cd00786    1 MTEALKAADLG-YAKESNFQVGACLvnKKDGGKVGRGCNIEnaaySMCNHAERTALFNAGSEGdtKGQMLYVALSPCGA- 78
                         90       100
                 ....*....|....*....|.
gi 504233478  82 grtppCARALIDAGVAHVFAA 102
Cdd:cd00786   79 -----CAQLIIELGIKDVIVV 94
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
4-118 2.66e-11

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: 61.00  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478    4 DRDRAMMARAVQLawRGRYSTHPNPrVGCVIAKGDLIVGEGWHERAGE----AHAEVRALSQA-----GHEARGATAYVT 74
Cdd:pfam14437   2 NHEKWFRKALGLA--EKAYDAGEVP-IGAVIVKDGKVIARGYNRKELNadttAHAEILAIQQAakklgSWRLDDATLYVT 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 504233478   75 LEPCshygrtPPCARALIDAGVAHVFAATKDPNPSVSGRGLDML 118
Cdd:pfam14437  79 LEPC------PMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKL 116
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
10-112 2.00e-10

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 57.24  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  10 MARAVQLAWRGR-YSTHPnprVGCVIAKGDL-IVGEGWHERAGE----AHAEVRALSQAG-----HEARGATAYVTLEPC 78
Cdd:cd01285    1 MRLAIELARKALaEGEVP---FGAVIVDDDGkVIARGHNRVEQDgdptAHAEIVAIRNAArrlgsYLLSGCTLYTTLEPC 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 504233478  79 shygrtPPCARALIDAGVAHVFAATKDPNPSVSG 112
Cdd:cd01285   78 ------PMCAGALLWARIKRVVYGASDPKLGGIG 105
cd PHA02588
deoxycytidylate deaminase; Provisional
45-127 8.38e-07

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 48.60  E-value: 8.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233478  45 WHERaGEAHAEVRAL---SQAGHEARGATAYVTLEPCshygrtPPCARALIDAGVAHVFAATK-DPNPSvsgRGLDMLRE 120
Cdd:PHA02588  76 WSSK-NEIHAELNAIlfaARNGISIEGATMYVTASPC------PDCAKAIAQSGIKKLVYCEKyDRNGP---GWDDILRK 145

                 ....*..
gi 504233478 121 AGIRVTE 127
Cdd:PHA02588 146 SGIEVIQ 152
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
285-359 1.17e-05

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: 45.23  E-value: 1.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233478 285 DVAELLDALGELGINELLVEAGPTLAGTFIGENLVDELWLYQAPVFLGStGRPTahlpLETMADKVQWKVLDRRQ 359
Cdd:COG0262   90 DLEEALAALKAAGGKDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLGE-GDRL----FPELDAPSRLELVESEA 159
 
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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