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Conserved domains on  [gi|1491308488|gb|RLI72215|]
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MAG: cytidine deaminase [Candidatus Gerdarchaeota archaeon]

Protein Classification

deoxycytidylate deaminase( domain architecture ID 10788416)

deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase

CATH:  3.40.140.10
EC:  3.5.4.12
Gene Ontology:  GO:0004132|GO:0008270|GO:0009972|GO:0006220
PubMed:  2247612
SCOP:  4000564

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-150 6.70e-85

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 245.91  E-value: 6.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   1 MRPTVDEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELHIPSGTKHEICRGVHSEQ 80
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRTVHAEQ 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  81 NAIIQCAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSYSDTEGIDLLREAGVEVTILEQKAK 150
Cdd:COG2131    84 NAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQLELEEE 153
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-150 6.70e-85

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 245.91  E-value: 6.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   1 MRPTVDEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELHIPSGTKHEICRGVHSEQ 80
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRTVHAEQ 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  81 NAIIQCAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSYSDTEGIDLLREAGVEVTILEQKAK 150
Cdd:COG2131    84 NAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQLELEEE 153
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 6-136 1.03e-60

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: 184.02  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELhiPSGTKHEICRGVHSEQNAIIQ 85
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL--PSGEDQKCCRTVHAEQNAILQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491308488  86 CAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSYSDTE--GIDLLR 136
Cdd:cd01286    79 AARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDpaAAELLE 131
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 6-142 2.59e-36

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 123.05  E-value: 2.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELHipsgtkheICRGVHSEQNAIIQ 85
Cdd:TIGR02571   6 DQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGH--------CVRTIHAEMNALLQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491308488  86 CAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSY-SDTEGIDLLREAGVEV 142
Cdd:TIGR02571  78 CAKFGVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYhNHPYAIELFEQAGVEL 135
cd PHA02588
deoxycytidylate deaminase; Provisional
 13-148 2.27e-33

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 116.01  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  13 AELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCID----IGCLRDEL---------HIPSGTKHEIcrgvHSE 79
Cdd:PHA02588   10 AYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhaneQGWLDDEGklkkehrpeHSAWSSKNEI----HAE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308488  80 QNAIIQCAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSY--SDTEGIDLLREAGVEVTILEQK 148
Cdd:PHA02588   86 LNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdrNGPGWDDILRKSGIEVIQIPKE 156
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-123 1.26e-22

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 86.20  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRS-TCLRRQFGTVIVQDNH-VISTGYNGAPRGMPHCIdigclrdelhipsgtkheicrgvHSEQNAI 83
Cdd:pfam00383   2 DEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGeIIATGYNGENAGYDPTI-----------------------HAERNAI 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491308488  84 IQCAI--HGESTAGATLYVTGYPCKICAKMIINAMIKRVVVS 123
Cdd:pfam00383  59 RQAGKrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 2-121 2.38e-21

anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase.


Pssm-ID: 468954 [Multi-domain]  Cd Length: 435  Bit Score: 89.15  E-value: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   2 RPTVDEY--FTAMAelVSTRSTCLRRQFGTVIV-QDNHVISTGYNGAPR---GMPHCIDIGCLRD--------------- 60
Cdd:NF041025  215 TPTRDERgmYAAFS--AALRSACLSRQVGAAITdKDGEIISTGWNDVPKaggGLYWPGDEPDHRDyslgydrndeekrki 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  61 -------------ELHIPSGTKHEIC-----------------RGVHSEQNAIIQCAIHGESTAGATLYVTGYPCKICAK 110
Cdd:NF041025  293 iedilkrladagsESLKKKGRNASECfklilkksrikdliefgRAVHAEMNAILSAARLGGSTKGGTLYTTTFPCHNCAK 372

                         170
                  ....*....|.
gi 1491308488 111 MIINAMIKRVV 121
Cdd:NF041025  373 HIVAAGIKRVV 383
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-150 6.70e-85

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 245.91  E-value: 6.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   1 MRPTVDEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELHIPSGTKHEICRGVHSEQ 80
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRTVHAEQ 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  81 NAIIQCAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSYSDTEGIDLLREAGVEVTILEQKAK 150
Cdd:COG2131    84 NAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQLELEEE 153
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 6-136 1.03e-60

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: 184.02  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELhiPSGTKHEICRGVHSEQNAIIQ 85
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL--PSGEDQKCCRTVHAEQNAILQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491308488  86 CAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSYSDTE--GIDLLR 136
Cdd:cd01286    79 AARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDpaAAELLE 131
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 6-142 2.59e-36

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 123.05  E-value: 2.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCIDIGCLRDELHipsgtkheICRGVHSEQNAIIQ 85
Cdd:TIGR02571   6 DQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGH--------CVRTIHAEMNALLQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491308488  86 CAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSY-SDTEGIDLLREAGVEV 142
Cdd:TIGR02571  78 CAKFGVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYhNHPYAIELFEQAGVEL 135
cd PHA02588
deoxycytidylate deaminase; Provisional
 13-148 2.27e-33

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 116.01  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  13 AELVSTRSTCLRRQFGTVIVQDNHVISTGYNGAPRGMPHCID----IGCLRDEL---------HIPSGTKHEIcrgvHSE 79
Cdd:PHA02588   10 AYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhaneQGWLDDEGklkkehrpeHSAWSSKNEI----HAE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308488  80 QNAIIQCAIHGESTAGATLYVTGYPCKICAKMIINAMIKRVVVSGSY--SDTEGIDLLREAGVEVTILEQK 148
Cdd:PHA02588   86 LNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdrNGPGWDDILRKSGIEVIQIPKE 156
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-123 1.26e-22

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 86.20  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRS-TCLRRQFGTVIVQDNH-VISTGYNGAPRGMPHCIdigclrdelhipsgtkheicrgvHSEQNAI 83
Cdd:pfam00383   2 DEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGeIIATGYNGENAGYDPTI-----------------------HAERNAI 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491308488  84 IQCAI--HGESTAGATLYVTGYPCKICAKMIINAMIKRVVVS 123
Cdd:pfam00383  59 RQAGKrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 2-121 2.38e-21

anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase.


Pssm-ID: 468954 [Multi-domain]  Cd Length: 435  Bit Score: 89.15  E-value: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   2 RPTVDEY--FTAMAelVSTRSTCLRRQFGTVIV-QDNHVISTGYNGAPR---GMPHCIDIGCLRD--------------- 60
Cdd:NF041025  215 TPTRDERgmYAAFS--AALRSACLSRQVGAAITdKDGEIISTGWNDVPKaggGLYWPGDEPDHRDyslgydrndeekrki 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  61 -------------ELHIPSGTKHEIC-----------------RGVHSEQNAIIQCAIHGESTAGATLYVTGYPCKICAK 110
Cdd:NF041025  293 iedilkrladagsESLKKKGRNASECfklilkksrikdliefgRAVHAEMNAILSAARLGGSTKGGTLYTTTFPCHNCAK 372

                         170
                  ....*....|.
gi 1491308488 111 MIINAMIKRVV 121
Cdd:NF041025  373 HIVAAGIKRVV 383
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 28-153 2.79e-16

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: 74.33  E-value: 2.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  28 GTVIVQDNHVISTGYngaprgmphcidigclrdelHIPSGtkheicrGVHSEQNAIIQCaihGESTAGATLYVTGYPCKI 107
Cdd:COG0117    25 GCVIVKDGRIVGEGY--------------------HQRAG-------GPHAEVNALAQA---GEAARGATLYVTLEPCSH 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491308488 108 ------CAKMIINAMIKRVV---------VSGsysdtEGIDLLREAGVEVT--ILEQKAKDVL 153
Cdd:COG0117    75 hgrtppCADALIEAGIKRVViamldpnplVAG-----KGIARLRAAGIEVEvgVLEEEARALN 132
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 28-164 1.22e-12

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: 64.08  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  28 GTVIVQDNHVISTGYngaprgmphcidigclrdelHIPSGtkheicrGVHSEQNAIIQCaihGESTAGATLYVTGYPCK- 106
Cdd:TIGR00326  22 GCVIVKNGEIVGEGA--------------------HQKAG-------EPHAEVHALRQA---GENAKGATAYVTLEPCSh 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488 107 -----ICAKMIINAMIKRVVVS----GSYSDTEGIDLLREAGVEVT--ILEQKAKDVLLKVIK-MKESRQ 164
Cdd:TIGR00326  72 qgrtpPCAEAIIEAGIKKVVVSmqdpNPLVAGRGAERLKQAGIEVTfgILKEEAERLNKGFLKrMRTGLP 141
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 6-128 6.05e-12

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 59.84  E-value: 6.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTRSTCLRRQFGTVIVQDNHVISTGYNgaprgmphcidigclRDELHIPSGTkheicrgvHSEQNAIIQ 85
Cdd:pfam14437   4 EKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYN---------------RKELNADTTA--------HAEILAIQQ 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1491308488  86 CAIHGEST--AGATLYVTGYPCKICAKMIINAMIKRVVVSGSYSD 128
Cdd:pfam14437  61 AAKKLGSWrlDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGNPK 105
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 27-139 8.15e-12

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: 58.79  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  27 FGTVIVQDNH-VISTGYngaprgmphcidigclrdelHIPSGTKHeicrgvhSEQNAIIQCAihGESTAGATLYVTGYPC 105
Cdd:cd01284    21 VGCVIVDDDGeIVGEGY--------------------HRKAGGPH-------AEVNALASAG--EKLARGATLYVTLEPC 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1491308488 106 K------ICAKMIINAMIKRVVVSGSYSDT----EGIDLLREAG 139
Cdd:cd01284    72 ShhgktpPCVDAIIEAGIKRVVVGVRDPNPlvagKGAERLRAAG 115
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 27-153 1.01e-11

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: 59.36  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  27 FGTVIVQDNHVISTGYNgaprgmphcidigcLRDELHIPSGtkheicrgvHSEQNAIIQ-CAIHG-ESTAGATLYVTGYP 104
Cdd:COG0590    26 VGAVLVKDGEIIARGHN--------------RVETLNDPTA---------HAEILAIRAaARKLGnWRLSGCTLYVTLEP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1491308488 105 CKICAKMIINAMIKRVVVSGSYSDTEGI----DLLREA----GVEVT--ILEQKAKDVL 153
Cdd:COG0590    83 CPMCAGAIVWARIGRVVYGASDPKAGAAgsiyDLLADPrlnhRVEVVggVLAEECAALL 141
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 27-137 2.13e-07

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: 46.84  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  27 FGTVIVQDNH-VISTGYNgaprgmphcidigcLRDELHIPSGtkheicrgvHSEQNAI--IQCAIHGESTAGATLYVTGY 103
Cdd:cd01285    19 FGAVIVDDDGkVIARGHN--------------RVEQDGDPTA---------HAEIVAIrnAARRLGSYLLSGCTLYTTLE 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1491308488 104 PCKICAKMIINAMIKRVVVSGSYSDTEGIDLLRE 137
Cdd:cd01285    76 PCPMCAGALLWARIKRVVYGASDPKLGGIGFLIE 109
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 77-122 2.93e-07

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: 46.39  E-value: 2.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1491308488  77 HSEQNAIIQCAIHGEsTAGATLYVTGYPCKICAKMIINAMIKRVVV 122
Cdd:cd00786    49 HAERTALFNAGSEGD-TKGQMLYVALSPCGACAQLIIELGIKDVIV 93
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 28-144 2.31e-06

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 46.30  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  28 GTVIVQDNHVISTGYNgaPR-GMPHCiDIGCLRDElhipsgtkheicrgvhseqnaiiqcaihGESTAGATLYVTGYPCK 106
Cdd:PLN02807   57 GCVIVKDGRIVGEGFH--PKaGQPHA-EVFALRDA----------------------------GDLAENATAYVSLEPCN 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1491308488 107 ------ICAKMIINAMIKRVVVSGSYSD----TEGIDLLREAGVEVTI 144
Cdd:PLN02807  106 hygrtpPCTEALIKAKVKRVVVGMVDPNpivaSKGIERLRDAGIEVTV 153
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 6-142 3.23e-05

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 42.83  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488   6 DEYFTAMAELVSTR---STCLRRQFGTVIVQDNHVISTGYngaprgmphcidigclrdelHIPSGTKHEicrGVHSEQNA 82
Cdd:PRK10786    3 DEFYMARALKLAQRgrfTTHPNPNVGCVIVKDGEIVGEGY--------------------HQRAGEPHA---EVHALRMA 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  83 iiqcaihGESTAGATLYVTGYPCK------ICAKMIINAMIKRVVVSGSYSDTE----GIDLLREAGVEV 142
Cdd:PRK10786   60 -------GEKAKGATAYVTLEPCShhgrtpPCCDALIAAGVARVVAAMQDPNPQvagrGLYRLQQAGIDV 122
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 28-165 2.75e-04

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 39.40  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488  28 GTVIVQDNHVISTGYNgapRGMPHcidigclrdelHIPSGtkheicrgvHSEQNAIIQ--CAIHGESTAGATLYVTGYPC 105
Cdd:PRK10860   36 GAVLVHNNRVIGEGWN---RPIGR-----------HDPTA---------HAEIMALRQggLVLQNYRLLDATLYVTLEPC 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308488 106 KICAKMIINAMIKRVVVSGSYSDTEG----IDLLREAG----VEVT--ILEQKAKDVLLKVIKMKESRQR 165
Cdd:PRK10860   93 VMCAGAMVHSRIGRLVFGARDAKTGAagslMDVLHHPGmnhrVEITegVLADECAALLSDFFRMRRQEIK 162
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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