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Conserved domains on  [gi|577236046|gb|EUE53157|]
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ComE operon protein 2 [Staphylococcus aureus M0671]

Protein Classification

cytidine/deoxycytidylate deaminase family protein( domain architecture ID 923)

cytidine/deoxycytidylate deaminase family protein similar to Bacillus subtilis cytidine deaminase that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytidine_deaminase-like super family cl00269
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 1-142 8.00e-95

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.


The actual alignment was detected with superfamily member TIGR02571:

Pssm-ID: 444801 [Multi-domain]  Cd Length: 151  Bit Score: 270.19  E-value: 8.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046    1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLIEDGHCIRTIHAEMNALLQCAKQGVSTEGAT 80
Cdd:TIGR02571  10 MAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAKFGVSTEGAE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577236046   81 IYVTHFPCLNCTKSIIQAGIKRIYYAEDYHNHEYATKLLKQSGIEFKKIPFSPEYVAKYLTK 142
Cdd:TIGR02571  90 IYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPFDPSYLAQYNTQ 151
 
Name Accession Description Interval E-value
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 1-142 8.00e-95

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: 270.19  E-value: 8.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046    1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLIEDGHCIRTIHAEMNALLQCAKQGVSTEGAT 80
Cdd:TIGR02571  10 MAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAKFGVSTEGAE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577236046   81 IYVTHFPCLNCTKSIIQAGIKRIYYAEDYHNHEYATKLLKQSGIEFKKIPFSPEYVAKYLTK 142
Cdd:TIGR02571  90 IYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPFDPSYLAQYNTQ 151
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-134 2.29e-77

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 225.88  E-value: 2.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLI--------EDGHCIRTIHAEMNALLQCAKQ 72
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLReklgipsgERGECCRTVHAEQNAILQAARH 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577236046  73 GVSTEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDYHnHEYATKLLKQSGIEFKKIPFSPE 134
Cdd:COG2131   93 GVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYP-DELAKELLKEAGVEVRQLELEEE 153
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 1-120 4.86e-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: 181.32  E-value: 4.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLI------EDGHCIRTIHAEMNALLQCAKQGV 74
Cdd:cd01286    5 MAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERddlpsgEDQKCCRTVHAEQNAILQAARHGV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 577236046  75 STEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDYHNH-EYATKLLK 120
Cdd:cd01286   85 SLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDdPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 1-138 3.15e-38

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 127.57  E-value: 3.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCID----------EGCLIED---GHC----IRTIHAEM 63
Cdd:PHA02588   7 LQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhaneqgwlddEGKLKKEhrpEHSawssKNEIHAEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577236046  64 NALLQCAKQGVSTEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDY--HNHEYAtKLLKQSGIEFKKIPfsPEYVAK 138
Cdd:PHA02588  87 NAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdrNGPGWD-DILRKSGIEVIQIP--KEELNK 160
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
1-106 7.09e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 93.91  E-value: 7.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046    1 MAQSHLLALRS-TCQRLSVGATIVK-DNRIIAGGYNGSVAGEVhcidegcliedghciRTIHAEMNALLQCAKQG--VST 76
Cdd:pfam00383   6 MRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGENAGYD---------------PTIHAERNAIRQAGKRGegVRL 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 577236046   77 EGATIYVTHFPCLNCTKSIIQAGIKRIYYA 106
Cdd:pfam00383  71 EGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 49-109 9.52e-25

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: 97.63  E-value: 9.52e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577236046  49 LIEDGhciRTIHAEMNALLQCAKQGVSTEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDY 109
Cdd:NF041025 331 LIEFG---RAVHAEMNAILSAARLGGSTKGGTLYTTTFPCHNCAKHIVAAGIKRVVYIEPY 388
 
Name Accession Description Interval E-value
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 1-142 8.00e-95

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: 270.19  E-value: 8.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046    1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLIEDGHCIRTIHAEMNALLQCAKQGVSTEGAT 80
Cdd:TIGR02571  10 MAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAKFGVSTEGAE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577236046   81 IYVTHFPCLNCTKSIIQAGIKRIYYAEDYHNHEYATKLLKQSGIEFKKIPFSPEYVAKYLTK 142
Cdd:TIGR02571  90 IYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPFDPSYLAQYNTQ 151
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-134 2.29e-77

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 225.88  E-value: 2.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLI--------EDGHCIRTIHAEMNALLQCAKQ 72
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLReklgipsgERGECCRTVHAEQNAILQAARH 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577236046  73 GVSTEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDYHnHEYATKLLKQSGIEFKKIPFSPE 134
Cdd:COG2131   93 GVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYP-DELAKELLKEAGVEVRQLELEEE 153
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 1-120 4.86e-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: 181.32  E-value: 4.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCIDEGCLI------EDGHCIRTIHAEMNALLQCAKQGV 74
Cdd:cd01286    5 MAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERddlpsgEDQKCCRTVHAEQNAILQAARHGV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 577236046  75 STEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDYHNH-EYATKLLK 120
Cdd:cd01286   85 SLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDdPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 1-138 3.15e-38

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 127.57  E-value: 3.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQRLSVGATIVKDNRIIAGGYNGSVAGEVHCID----------EGCLIED---GHC----IRTIHAEM 63
Cdd:PHA02588   7 LQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhaneqgwlddEGKLKKEhrpEHSawssKNEIHAEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577236046  64 NALLQCAKQGVSTEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDY--HNHEYAtKLLKQSGIEFKKIPfsPEYVAK 138
Cdd:PHA02588  87 NAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdrNGPGWD-DILRKSGIEVIQIP--KEELNK 160
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
1-106 7.09e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 93.91  E-value: 7.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046    1 MAQSHLLALRS-TCQRLSVGATIVK-DNRIIAGGYNGSVAGEVhcidegcliedghciRTIHAEMNALLQCAKQG--VST 76
Cdd:pfam00383   6 MRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGENAGYD---------------PTIHAERNAIRQAGKRGegVRL 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 577236046   77 EGATIYVTHFPCLNCTKSIIQAGIKRIYYA 106
Cdd:pfam00383  71 EGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 49-109 9.52e-25

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: 97.63  E-value: 9.52e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577236046  49 LIEDGhciRTIHAEMNALLQCAKQGVSTEGATIYVTHFPCLNCTKSIIQAGIKRIYYAEDY 109
Cdd:NF041025 331 LIEFG---RAVHAEMNAILSAARLGGSTKGGTLYTTTFPCHNCAKHIVAAGIKRVVYIEPY 388
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 18-108 1.98e-16

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: 70.92  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046  18 VGATIVKDNRIIAGGYNGSVAgevhcidegcliedgHCIRTIHAEMNALLQ-CAKQG-VSTEGATIYVTHFPCLNCTKSI 95
Cdd:COG0590   26 VGAVLVKDGEIIARGHNRVET---------------LNDPTAHAEILAIRAaARKLGnWRLSGCTLYVTLEPCPMCAGAI 90

                         90
                 ....*....|...
gi 577236046  96 IQAGIKRIYYAED 108
Cdd:COG0590   91 VWARIGRVVYGAS 103
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 6-109 7.58e-15

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


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 66.78  E-value: 7.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046    6 LLALRSTCQRLSVGATIVKDNRIIAGGYNGsvagevhcidegcliEDGHCIRTIHAEMNALLQCAKQGVST--EGATIYV 83
Cdd:pfam14437  13 LAEKAYDAGEVPIGAVIVKDGKVIARGYNR---------------KELNADTTAHAEILAIQQAAKKLGSWrlDDATLYV 77

                          90       100
                  ....*....|....*....|....*.
gi 577236046   84 THFPCLNCTKSIIQAGIKRIYYAEDY 109
Cdd:pfam14437  78 TLEPCPMCAGAIVQAGLKSLVYGAGN 103
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 18-108 2.12e-14

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


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 64.56  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046  18 VGATIVKDN-RIIAGGYNgsvagevhcidegCLIEDGHciRTIHAEMNALLQCAKQGVST--EGATIYVTHFPCLNCTKS 94
Cdd:cd01285   19 FGAVIVDDDgKVIARGHN-------------RVEQDGD--PTAHAEIVAIRNAARRLGSYllSGCTLYTTLEPCPMCAGA 83

                         90
                 ....*....|....
gi 577236046  95 IIQAGIKRIYYAED 108
Cdd:cd01285   84 LLWARIKRVVYGAS 97
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 17-125 1.25e-13

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: 66.24  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046  17 SVGATIVKDNRIIAGGYNgSVAGEVhcidegcliedghcirtiHAEMNALLQCakqGVSTEGATIYVT-----HF----P 87
Cdd:COG0117   23 LVGCVIVKDGRIVGEGYH-QRAGGP------------------HAEVNALAQA---GEAARGATLYVTlepcsHHgrtpP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 577236046  88 clnCTKSIIQAGIKRIYYA-EDyhNHEYA----TKLLKQSGIE 125
Cdd:COG0117   81 ---CADALIEAGIKRVVIAmLD--PNPLVagkgIARLRAAGIE 118
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 17-127 2.72e-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: 62.54  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   17 SVGATIVKDNRIIAGGYNGSvAGEVHcidegcliedghcirtihAEMNALlqcAKQGVSTEGATIYVTHFPCLN------ 90
Cdd:TIGR00326  20 LVGCVIVKNGEIVGEGAHQK-AGEPH------------------AEVHAL---RQAGENAKGATAYVTLEPCSHqgrtpp 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 577236046   91 CTKSIIQAGIKRIYYAEDYHNHEYATK---LLKQSGIEFK 127
Cdd:TIGR00326  78 CAEAIIEAGIKKVVVSMQDPNPLVAGRgaeRLKQAGIEVT 117
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 17-106 1.19e-11

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: 57.63  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046  17 SVGATIVKDN-RIIAGGYNgSVAGEVHcidegcliedghcirtihAEMNALLQCAKQgvSTEGATIYVTHFPCLN----- 90
Cdd:cd01284   20 PVGCVIVDDDgEIVGEGYH-RKAGGPH------------------AEVNALASAGEK--LARGATLYVTLEPCSHhgktp 78

                         90
                 ....*....|....*..
gi 577236046  91 -CTKSIIQAGIKRIYYA 106
Cdd:cd01284   79 pCVDAIIEAGIKRVVVG 95
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 18-108 8.28e-10

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: 52.55  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046  18 VGATIVKDNriiaggyNGSVAGEvhcideGCLIEDGHCIRTIHAEMNALLQCAKQGvSTEGATIYVTHFPCLNCTKSIIQ 97
Cdd:cd00786   20 VGACLVNKK-------DGGKVGR------GCNIENAAYSMCNHAERTALFNAGSEG-DTKGQMLYVALSPCGACAQLIIE 85

                         90
                 ....*....|.
gi 577236046  98 AGIKRIYYAED 108
Cdd:cd00786   86 LGIKDVIVVLT 96
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-105 8.37e-09

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 51.35  E-value: 8.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALRSTCQR-LSVGATIVKDNRIIAGGYNGSVagevhcidegcliedGHCIRTIHAEMNALLQ--CAKQGVSTE 77
Cdd:PRK10860  17 MRHALTLAKRAWDEReVPVGAVLVHNNRVIGEGWNRPI---------------GRHDPTAHAEIMALRQggLVLQNYRLL 81

                         90       100
                 ....*....|....*....|....*...
gi 577236046  78 GATIYVTHFPCLNCTKSIIQAGIKRIYY 105
Cdd:PRK10860  82 DATLYVTLEPCVMCAGAMVHSRIGRLVF 109
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 1-125 7.31e-08

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 49.76  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046   1 MAQSHLLALR---STCQRLSVGATIVKDNRIIAGGYNGSvAGEVhcidegcliedghcirtiHAEMNALLQCakqGVSTE 77
Cdd:PRK10786   7 MARALKLAQRgrfTTHPNPNVGCVIVKDGEIVGEGYHQR-AGEP------------------HAEVHALRMA---GEKAK 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 577236046  78 GATIYVTHFPCLN------CTKSIIQAGIKRIYYAEDYHNHEYATK---LLKQSGIE 125
Cdd:PRK10786  65 GATAYVTLEPCSHhgrtppCCDALIAAGVARVVAAMQDPNPQVAGRglyRLQQAGID 121
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 18-103 4.62e-04

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 38.99  E-value: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577236046  18 VGATIVKDNRIIAGGYNGSvAGEVHcidegcliedghcirtihAEMNALLQCakqGVSTEGATIYVTHFPCLN------C 91
Cdd:PLN02807  56 VGCVIVKDGRIVGEGFHPK-AGQPH------------------AEVFALRDA---GDLAENATAYVSLEPCNHygrtppC 113

                         90
                 ....*....|..
gi 577236046  92 TKSIIQAGIKRI 103
Cdd:PLN02807 114 TEALIKAKVKRV 125
 
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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