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Conserved domains on  [gi|2049391977|gb|QWG82781|]
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ComE operon protein 2 [Bacillus mycoides]

Protein Classification

cytidine/deoxycytidylate deaminase family protein; cytidine deaminase( domain architecture ID 10798262)

cytidine/deoxycytidylate deaminase family protein similar to Bacillus subtilis cytidine deaminase that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis| cytidine deaminase catalyzes the deamination of cytidine to uridine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 2-152 2.90e-105

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: 298.31  E-value: 2.90e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   2 ERISWDQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYVIDNHCVRTIHAEMNALLQCAK 81
Cdd:TIGR02571   1 ERIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049391977  82 FGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYKNHPYAVELFEQASVTVKHVPLEYDITSLEEQE 152
Cdd:TIGR02571  81 FGVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPFDPSYLAQYNTQ 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 ...
 2-152 2.90e-105

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: 298.31  E-value: 2.90e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   2 ERISWDQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYVIDNHCVRTIHAEMNALLQCAK 81
Cdd:TIGR02571   1 ERIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049391977  82 FGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYKNHPYAVELFEQASVTVKHVPLEYDITSLEEQE 152
Cdd:TIGR02571  81 FGVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPFDPSYLAQYNTQ 151
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-145 3.15e-78

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 230.11  E-value: 3.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   1 MERISWDQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYVI--------DNHCVRTIHAE 72
Cdd:COG2131     3 MERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREklgipsgeRGECCRTVHAE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049391977  73 MNALLQCAKFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYkNHPYAVELFEQASVTVKHVPLEYDI 145
Cdd:COG2131    83 QNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDY-PDELAKELLKEAGVEVRQLELEEEE 154
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 7-130 2.18e-55

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: 171.30  E-value: 2.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   7 DQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYV------IDNHCVRTIHAEMNALLQCA 80
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERddlpsgEDQKCCRTVHAEQNAILQAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049391977  81 KFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYKNH-PYAVELFE 130
Cdd:cd01286    81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDdPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 7-143 2.10e-31

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 111.39  E-value: 2.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   7 DQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCID---DGCYVIDNHCVRT--------------I 69
Cdd:PHA02588    3 DSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhanEQGWLDDEGKLKKehrpehsawsskneI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2049391977  70 HAEMNALLQCAKFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDY-KNHPYAVELFEQASVTVKHVPLEY 143
Cdd:PHA02588   83 HAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdRNGPGWDDILRKSGIEVIQIPKEE 157
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-116 3.65e-28

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 101.22  E-value: 3.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   6 WDQYFMTQSHLLSLRS-TCTRLAVGATIVR-DKRIIAGGYNGSIKGGVhciddgcyvidnhcvRTIHAEMNALLQCAKFG 83
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGENAGYD---------------PTIHAERNAIRQAGKRG 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2049391977  84 --AKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYA 116
Cdd:pfam00383  66 egVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 67-115 1.73e-14

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: 70.28  E-value: 1.73e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2049391977  67 RTIHAEMNALLQCAKFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYY 115
Cdd:NF041025  336 RAVHAEMNAILSAARLGGSTKGGTLYTTTFPCHNCAKHIVAAGIKRVVY 384
 
Name Accession Description Interval E-value
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 2-152 2.90e-105

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: 298.31  E-value: 2.90e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   2 ERISWDQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYVIDNHCVRTIHAEMNALLQCAK 81
Cdd:TIGR02571   1 ERIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049391977  82 FGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYKNHPYAVELFEQASVTVKHVPLEYDITSLEEQE 152
Cdd:TIGR02571  81 FGVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHPYAIELFEQAGVELKKVPFDPSYLAQYNTQ 151
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-145 3.15e-78

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 230.11  E-value: 3.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   1 MERISWDQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYVI--------DNHCVRTIHAE 72
Cdd:COG2131     3 MERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREklgipsgeRGECCRTVHAE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049391977  73 MNALLQCAKFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYkNHPYAVELFEQASVTVKHVPLEYDI 145
Cdd:COG2131    83 QNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDY-PDELAKELLKEAGVEVRQLELEEEE 154
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 7-130 2.18e-55

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: 171.30  E-value: 2.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   7 DQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCIDDGCYV------IDNHCVRTIHAEMNALLQCA 80
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERddlpsgEDQKCCRTVHAEQNAILQAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049391977  81 KFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDYKNH-PYAVELFE 130
Cdd:cd01286    81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDdPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 7-143 2.10e-31

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 111.39  E-value: 2.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   7 DQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGSIKGGVHCID---DGCYVIDNHCVRT--------------I 69
Cdd:PHA02588    3 DSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhanEQGWLDDEGKLKKehrpehsawsskneI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2049391977  70 HAEMNALLQCAKFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDY-KNHPYAVELFEQASVTVKHVPLEY 143
Cdd:PHA02588   83 HAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdRNGPGWDDILRKSGIEVIQIPKEE 157
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
6-116 3.65e-28

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 101.22  E-value: 3.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   6 WDQYFMTQSHLLSLRS-TCTRLAVGATIVR-DKRIIAGGYNGSIKGGVhciddgcyvidnhcvRTIHAEMNALLQCAKFG 83
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGENAGYD---------------PTIHAERNAIRQAGKRG 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2049391977  84 --AKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYYA 116
Cdd:pfam00383  66 egVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 4-119 5.00e-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: 68.32  E-value: 5.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   4 ISWDQYFMTQSHLLSLRSTCTRLAVGATIVRDKRIIAGGYNGsikggvhciddgcyvIDNHCVRTIHAEMNALLQCAKFG 83
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNR---------------KELNADTTAHAEILAIQQAAKKL 65

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2049391977  84 AKT--EEAEIYVTHFPCLQCCKAIIQSGVTAVYYAQDY 119
Cdd:pfam14437  66 GSWrlDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGN 103
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 67-115 1.73e-14

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: 70.28  E-value: 1.73e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2049391977  67 RTIHAEMNALLQCAKFGAKTEEAEIYVTHFPCLQCCKAIIQSGVTAVYY 115
Cdd:NF041025  336 RAVHAEMNAILSAARLGGSTKGGTLYTTTFPCHNCAKHIVAAGIKRVVY 384
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 28-116 3.72e-12

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: 60.90  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977  28 VGATIVRDKRIIAGGYNGsikggvhciddgcyVIDNHCVrTIHAEMNALLQ-CAKFGAK-TEEAEIYVTHFPCLQCCKAI 105
Cdd:COG0590    26 VGAVLVKDGEIIARGHNR--------------VETLNDP-TAHAEILAIRAaARKLGNWrLSGCTLYVTLEPCPMCAGAI 90

                          90
                  ....*....|.
gi 2049391977 106 IQSGVTAVYYA 116
Cdd:COG0590    91 VWARIGRVVYG 101
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 28-116 8.10e-11

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: 56.47  E-value: 8.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977  28 VGATIVRDK-RIIAGGYNGSIKGGvhciddgcyviDnhcvRTIHAEMNALLQ-CAKFGAKT-EEAEIYVTHFPCLQCCKA 104
Cdd:cd01285    19 FGAVIVDDDgKVIARGHNRVEQDG-----------D----PTAHAEIVAIRNaARRLGSYLlSGCTLYTTLEPCPMCAGA 83

                          90
                  ....*....|..
gi 2049391977 105 IIQSGVTAVYYA 116
Cdd:cd01285    84 LLWARIKRVVYG 95
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 28-116 3.34e-07

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: 46.84  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977  28 VGATIVRD-KRIIAGGYngSIKGGVHciddgcyvidnhcvrtiHAEMNALLQCAKfgAKTEEAEIYVTHFPCLQ------ 100
Cdd:cd01284    21 VGCVIVDDdGEIVGEGY--HRKAGGP-----------------HAEVNALASAGE--KLARGATLYVTLEPCSHhgktpp 79

                          90
                  ....*....|....*.
gi 2049391977 101 CCKAIIQSGVTAVYYA 116
Cdd:cd01284    80 CVDAIIEAGIKRVVVG 95
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-120 8.61e-07

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 46.72  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   1 MERISWDQYFMTQSHLLSLRSTCTR-LAVGATIVRDKRIIAGGYNGSIkgGVHciDDgcyvidnhcvrTIHAEMNALLQC 79
Cdd:PRK10860    7 SEVEFSHEYWMRHALTLAKRAWDEReVPVGAVLVHNNRVIGEGWNRPI--GRH--DP-----------TAHAEIMALRQG 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2049391977  80 AKF--GAKTEEAEIYVTHFPCLQCCKAIIQSGV-TAVYYAQDYK 120
Cdd:PRK10860   72 GLVlqNYRLLDATLYVTLEPCVMCAGAMVHSRIgRLVFGARDAK 115
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 28-118 1.77e-06

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: 44.46  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977  28 VGATIVRDKriiaggyNGSIKGGVHCIDDGCYVIDNHcvrtihAEMNALLQCAKFGAkTEEAEIYVTHFPCLQCCKAIIQ 107
Cdd:cd00786    20 VGACLVNKK-------DGGKVGRGCNIENAAYSMCNH------AERTALFNAGSEGD-TKGQMLYVALSPCGACAQLIIE 85

                          90
                  ....*....|.
gi 2049391977 108 SGVTAVYYAQD 118
Cdd:cd00786    86 LGIKDVIVVLT 96
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 7-138 9.29e-06

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 44.76  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049391977   7 DQYFMTQSHLLSLR---STCTRLAVGATIVRDKRIIAGGYngsikggvhciddgcyvidNHCVRTIHAEMNALLQCakfG 83
Cdd:PRK10786    3 DEFYMARALKLAQRgrfTTHPNPNVGCVIVKDGEIVGEGY-------------------HQRAGEPHAEVHALRMA---G 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2049391977  84 AKTEEAEIYVTHFPCLQ------CCKAIIQSGVTAVYYAQDYKNHPYA---VELFEQASVTVKH 138
Cdd:PRK10786   61 EKAKGATAYVTLEPCSHhgrtppCCDALIAAGVARVVAAMQDPNPQVAgrgLYRLQQAGIDVSH 124
 
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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