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Conserved domains on  [gi|17557019|ref|NP_498980|]
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putative deoxycytidylate deaminase [Caenorhabditis elegans]

Protein Classification

dCMP deaminase family protein( domain architecture ID 10101269)

dCMP deaminase family protein such as deoxycytidylate deaminase, which catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 51-177 1.28e-52

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: 164.76  E-value: 1.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  51 HQRFLRIAKVTSLRSKDPNTQVGCVIVDKDNCIvSVGYNGFPIGVDDDVFRWDKED----PEDNKHLYVVHAEMNAIIN- 125
Cdd:cd01286   1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRII-STGYNGSPSGLPHCAEVGCERDdlpsGEDQKCCRTVHAEQNAILQa 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17557019 126 -KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRDELaFRASKKMLD 177
Cdd:cd01286  80 aRHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDD-DPAAAELLE 131
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 51-177 1.28e-52

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: 164.76  E-value: 1.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  51 HQRFLRIAKVTSLRSKDPNTQVGCVIVDKDNCIvSVGYNGFPIGVDDDVFRWDKED----PEDNKHLYVVHAEMNAIIN- 125
Cdd:cd01286   1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRII-STGYNGSPSGLPHCAEVGCERDdlpsGEDQKCCRTVHAEQNAILQa 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17557019 126 -KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRDELaFRASKKMLD 177
Cdd:cd01286  80 aRHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDD-DPAAAELLE 131
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
51-191 4.96e-51

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 161.55  E-value: 4.96e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  51 HQRFLRIAKVTSLRSKDPNTQVGCVIVdKDNCIVSVGYNGFPIGVDDDVFR-WDKE-----DPEDNKHLYVVHAEMNAII 124
Cdd:COG2131   9 DEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREklgipSGERGECCRTVHAEQNAIL 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019 125 N--KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLEN-RDELAfrasKKMLDHARLPYEQIVMPQE 191
Cdd:COG2131  88 QaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDyPDELA----KELLKEAGVEVRQLELEEE 153
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
50-161 7.08e-34

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 116.25  E-value: 7.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019    50 KHQRFLRIAKVTSLRS-KDPNTQVGCVIVDKDNCIVSVGYNGFPIGVDddvfrwdkedpednkhlYVVHAEMNAIIN--- 125
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAGYD-----------------PTIHAERNAIRQagk 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17557019   126 -KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFL 161
Cdd:pfam00383  64 rGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 50-165 3.23e-17

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 75.18  E-value: 3.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019   50 KHQRFLRIAKVTSLRSKDPNTQVGCVIVdKDNCIVSVGYNGFP------------IGVDDDVFRWDKED-PE----DNKH 112
Cdd:PHA02588   2 KDSTYLQIAYLVSQESKCVSWKVGAVIE-KNGRIISTGYNGTPaggvnccdhaneQGWLDDEGKLKKEHrPEhsawSSKN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17557019  113 lyVVHAEMNAII--NKRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRD 165
Cdd:PHA02588  81 --EIHAELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYD 133
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 68-192 1.59e-06

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: 47.52  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019    68 PNTQVGCVIVdKDNCIVSVGYNgFPIGVdddvfrwdkedpednkhlyvVHAEMNAIiNKRCTTLHDCTVYVTLFPCNK-- 145
Cdd:TIGR00326  17 PNPLVGCVIV-KNGEIVGEGAH-QKAGE--------------------PHAEVHAL-RQAGENAKGATAYVTLEPCSHqg 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17557019   146 ----CAQMLIQSRVKKVyFLENRDELAFRASK--KMLDHARLPYEQIVMPQEA 192
Cdd:TIGR00326  74 rtppCAEAIIEAGIKKV-VVSMQDPNPLVAGRgaERLKQAGIEVTFGILKEEA 125
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 51-177 1.28e-52

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: 164.76  E-value: 1.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  51 HQRFLRIAKVTSLRSKDPNTQVGCVIVDKDNCIvSVGYNGFPIGVDDDVFRWDKED----PEDNKHLYVVHAEMNAIIN- 125
Cdd:cd01286   1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRII-STGYNGSPSGLPHCAEVGCERDdlpsGEDQKCCRTVHAEQNAILQa 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17557019 126 -KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRDELaFRASKKMLD 177
Cdd:cd01286  80 aRHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDD-DPAAAELLE 131
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
51-191 4.96e-51

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 161.55  E-value: 4.96e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  51 HQRFLRIAKVTSLRSKDPNTQVGCVIVdKDNCIVSVGYNGFPIGVDDDVFR-WDKE-----DPEDNKHLYVVHAEMNAII 124
Cdd:COG2131   9 DEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREklgipSGERGECCRTVHAEQNAIL 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019 125 N--KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLEN-RDELAfrasKKMLDHARLPYEQIVMPQE 191
Cdd:COG2131  88 QaaRHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDyPDELA----KELLKEAGVEVRQLELEEE 153
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
50-161 7.08e-34

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 116.25  E-value: 7.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019    50 KHQRFLRIAKVTSLRS-KDPNTQVGCVIVDKDNCIVSVGYNGFPIGVDddvfrwdkedpednkhlYVVHAEMNAIIN--- 125
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAGYD-----------------PTIHAERNAIRQagk 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17557019   126 -KRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFL 161
Cdd:pfam00383  64 rGEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 50-165 3.23e-17

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 75.18  E-value: 3.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019   50 KHQRFLRIAKVTSLRSKDPNTQVGCVIVdKDNCIVSVGYNGFP------------IGVDDDVFRWDKED-PE----DNKH 112
Cdd:PHA02588   2 KDSTYLQIAYLVSQESKCVSWKVGAVIE-KNGRIISTGYNGTPaggvnccdhaneQGWLDDEGKLKKEHrPEhsawSSKN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17557019  113 lyVVHAEMNAII--NKRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRD 165
Cdd:PHA02588  81 --EIHAELNAILfaARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYD 133
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 52-165 2.10e-16

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: 71.49  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  52 QRFLRIAKVTSLRSKDPntqVGCVIVDKDNCIVSVGYNgfpigvdddvfrwdkEDPEDNKHLyvVHAEMNAI--INKRCT 129
Cdd:cd01285   2 RLAIELARKALAEGEVP---FGAVIVDDDGKVIARGHN---------------RVEQDGDPT--AHAEIVAIrnAARRLG 61

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17557019 130 T--LHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRD 165
Cdd:cd01285  62 SylLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDP 99
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 67-173 2.83e-16

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: 71.11  E-value: 2.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  67 DPNTQVGCVIVDKDNCIVSVGYNgfpigvdddvfrwdKEDPEDnkhlyvvHAEMNAIINKRCTTLHDCTVYVTLFPCNK- 145
Cdd:cd01284  16 SPNPPVGCVIVDDDGEIVGEGYH--------------RKAGGP-------HAEVNALASAGEKLARGATLYVTLEPCSHh 74

                        90       100       110
                ....*....|....*....|....*....|...
gi 17557019 146 -----CAQMLIQSRVKKVYFLeNRDELAFRASK 173
Cdd:cd01284  75 gktppCVDAIIEAGIKRVVVG-VRDPNPLVAGK 106
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 72-192 5.58e-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: 71.30  E-value: 5.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  72 VGCVIVdKDNCIVSVGYNGfpigvdddvfRWDKEDPednkhlyVVHAEMNAII-------NKRcttLHDCTVYVTLFPCN 144
Cdd:COG0590  26 VGAVLV-KDGEIIARGHNR----------VETLNDP-------TAHAEILAIRaaarklgNWR---LSGCTLYVTLEPCP 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17557019 145 KCAQMLIQSRVKKVYFLENRDELAFRAS------KKMLDHaRLPYEQIVMPQEA 192
Cdd:COG0590  85 MCAGAIVWARIGRVVYGASDPKAGAAGSiydllaDPRLNH-RVEVVGGVLAEEC 137
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 65-161 1.42e-14

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: 66.42  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  65 SKDPNTQVGCVIVDKDncivsvGYNGFPIGVDDDVfrwdkedpedNKHLYVVHAEMNAIINK-RCTTLHDCTVYVTLFPC 143
Cdd:cd00786  13 AKESNFQVGACLVNKK------DGGKVGRGCNIEN----------AAYSMCNHAERTALFNAgSEGDTKGQMLYVALSPC 76

                        90
                ....*....|....*...
gi 17557019 144 NKCAQMLIQSRVKKVYFL 161
Cdd:cd00786  77 GACAQLIIELGIKDVIVV 94
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 68-160 1.09e-11

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: 62.38  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019  68 PNTQVGCVIVdKDNCIVSVGY---NGFPigvdddvfrwdkedpednkhlyvvHAEMNAIINKRCTtLHDCTVYVTLFPCN 144
Cdd:COG0117  20 PNPLVGCVIV-KDGRIVGEGYhqrAGGP------------------------HAEVNALAQAGEA-ARGATLYVTLEPCS 73

                        90       100
                ....*....|....*....|..
gi 17557019 145 K------CAQMLIQSRVKKVYF 160
Cdd:COG0117  74 HhgrtppCADALIEAGIKRVVI 95
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 51-177 7.89e-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: 57.53  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019    51 HQRFLR-IAKVTSLRSKDPNTQVGCVIVdKDNCIVSVGYNgfpigvdddvfrwdkEDPEDNKHLYvvHAEMNAIiNKRC- 128
Cdd:pfam14437   3 HEKWFRkALGLAEKAYDAGEVPIGAVIV-KDGKVIARGYN---------------RKELNADTTA--HAEILAI-QQAAk 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 17557019   129 ----TTLHDCTVYVTLFPCNKCAQMLIQSRVKK-VYFLENRDELAFRASKKMLD 177
Cdd:pfam14437  64 klgsWRLDDATLYVTLEPCPMCAGAIVQAGLKSlVYGAGNPKGGAVGSVLNKLV 117
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 68-192 1.59e-06

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: 47.52  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019    68 PNTQVGCVIVdKDNCIVSVGYNgFPIGVdddvfrwdkedpednkhlyvVHAEMNAIiNKRCTTLHDCTVYVTLFPCNK-- 145
Cdd:TIGR00326  17 PNPLVGCVIV-KNGEIVGEGAH-QKAGE--------------------PHAEVHAL-RQAGENAKGATAYVTLEPCSHqg 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17557019   146 ----CAQMLIQSRVKKVyFLENRDELAFRASK--KMLDHARLPYEQIVMPQEA 192
Cdd:TIGR00326  74 rtppCAEAIIEAGIKKV-VVSMQDPNPLVAGRgaERLKQAGIEVTFGILKEEA 125
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 51-160 1.13e-05

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 44.03  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019   51 HQRFLRIAKVTSLRSKDP-NTQVGCVIVdKDNCIVSVGYNGfPIGvdddvfrwdKEDPednkhlyVVHAEMNAI------ 123
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDErEVPVGAVLV-HNNRVIGEGWNR-PIG---------RHDP-------TAHAEIMALrqgglv 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17557019  124 -INKRcttLHDCTVYVTLFPCNKCAQMLIQSRVKKVYF 160
Cdd:PRK10860  75 lQNYR---LLDATLYVTLEPCVMCAGAMVHSRIGRLVF 109
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 68-158 1.03e-03

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 38.98  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557019   68 PNTQVGCVIVdKDNCIVSVGYNgfpigvdddvFRWDKEDPEdnkhlyvVHAEMNAIINKRCTtlhdcTVYVTLFPCNK-- 145
Cdd:PRK10786  23 PNPNVGCVIV-KDGEIVGEGYH----------QRAGEPHAE-------VHALRMAGEKAKGA-----TAYVTLEPCSHhg 79

                         90
                 ....*....|....*..
gi 17557019  146 ----CAQMLIQSRVKKV 158
Cdd:PRK10786  80 rtppCCDALIAAGVARV 96
 
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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