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Conserved domains on  [gi|492558561|ref|WP_005885735|]
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MULTISPECIES: dCMP deaminase family protein [Fusobacterium]

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];
2-150 4.62e-66

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 198.14  E-value: 4.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561   2 KRKDYIEWDEYFMGVALLSGKRSKDPNTQVGACIVnEEKKIVGVGYNGLPIGCSDDEYP-WEREGEFL----ETKYPFVC 76
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIpsgeRGECCRTV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492558561  77 HAELNAILNSTK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDGtesniASKKMLTSAGVKFRQLKSK 150
Cdd:COG2131   80 HAEQNAILQAARhgvSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
2-150 4.62e-66

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 198.14  E-value: 4.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561   2 KRKDYIEWDEYFMGVALLSGKRSKDPNTQVGACIVnEEKKIVGVGYNGLPIGCSDDEYP-WEREGEFL----ETKYPFVC 76
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIpsgeRGECCRTV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492558561  77 HAELNAILNSTK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDGtesniASKKMLTSAGVKFRQLKSK 150
Cdd:COG2131   80 HAEQNAILQAARhgvSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-137 2.26e-54

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: 167.84  E-value: 2.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  10 DEYFMGVALLSGKRSKDPNTQVGACIVNEeKKIVGVGYNGLPIGCSDDEYPWEREGEF---LETKYPFVCHAELNAILNS 86
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKD-KRIISTGYNGSPSGLPHCAEVGCERDDLpsgEDQKCCRTVHAEQNAILQA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492558561  87 TK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDgteSNIASKKML 137
Cdd:cd01286   80 ARhgvSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDD---DDPAAAELL 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-120 7.31e-32

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 109.70  E-value: 7.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561    9 WDEYFMGVALLSGKRS-KDPNTQVGACIVNEEKKIVGVGYNGLPIGcsddeypweregefletkYPFVCHAELNAILN-- 85
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG------------------YDPTIHAERNAIRQag 62

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 492558561   86 ---STKSLKNCTIYVALFPCHECSKAIIQSGIRELVYL 120
Cdd:pfam00383  63 krgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 13-151 3.55e-24

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 92.13  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  13 FMGVALLSGKRSKDPNTQVGACIVNEEKkIVGVGYNGLPIG---CSD--DEYPW-EREGEFLETKYPF--------VCHA 78
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEKNGR-IISTGYNGTPAGgvnCCDhaNEQGWlDDEGKLKKEHRPEhsawssknEIHA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492558561  79 ELNAIL---NSTKSLKNCTIYVALFPCHECSKAIIQSGIRELVYLsDKYDGTESNIASkkMLTSAGVKFRQLKSKI 151
Cdd:PHA02588  85 ELNAILfaaRNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC-EKYDRNGPGWDD--ILRKSGIEVIQIPKEE 157
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 7-147 1.86e-21

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: 84.53  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561    7 IEWDEYFMGVALLSGKRSKDPNTQVGACIVnEEKKIVGVGYNGLPIG---CSDdeypwerEGEFLETKYPF-VCHAELNA 82
Cdd:TIGR02571   3 IKWDQYFMAQSHLLALRSTCTRLSVGATIV-RDKRIIAGGYNGSVAGgvhCID-------EGCYVVDGHCVrTIHAEMNA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492558561   83 ILNSTK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDgtesNIASKKMLTSAGVKFRQL 147
Cdd:TIGR02571  75 LLQCAKfgvSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHN----HPYAIELFEQAGVELKKV 138
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
2-150 4.62e-66

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 198.14  E-value: 4.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561   2 KRKDYIEWDEYFMGVALLSGKRSKDPNTQVGACIVnEEKKIVGVGYNGLPIGCSDDEYP-WEREGEFL----ETKYPFVC 76
Cdd:COG2131    1 KRMERPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVgCLREKLGIpsgeRGECCRTV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492558561  77 HAELNAILNSTK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDGtesniASKKMLTSAGVKFRQLKSK 150
Cdd:COG2131   80 HAEQNAILQAARhgvSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDE-----LAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-137 2.26e-54

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: 167.84  E-value: 2.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  10 DEYFMGVALLSGKRSKDPNTQVGACIVNEeKKIVGVGYNGLPIGCSDDEYPWEREGEF---LETKYPFVCHAELNAILNS 86
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKD-KRIISTGYNGSPSGLPHCAEVGCERDDLpsgEDQKCCRTVHAEQNAILQA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492558561  87 TK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDgteSNIASKKML 137
Cdd:cd01286   80 ARhgvSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDD---DDPAAAELL 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-120 7.31e-32

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 109.70  E-value: 7.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561    9 WDEYFMGVALLSGKRS-KDPNTQVGACIVNEEKKIVGVGYNGLPIGcsddeypweregefletkYPFVCHAELNAILN-- 85
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAG------------------YDPTIHAERNAIRQag 62

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 492558561   86 ---STKSLKNCTIYVALFPCHECSKAIIQSGIRELVYL 120
Cdd:pfam00383  63 krgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 11-122 5.51e-26

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: 94.54  E-value: 5.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  11 EYFMGVALLSgkRSKDPNTQVGACIVNEEkkivgvGYNGLPIGCSDDEYPweregefletkYPFVCHAELNAILN--STK 88
Cdd:cd00786    2 TEALKAADLG--YAKESNFQVGACLVNKK------DGGKVGRGCNIENAA-----------YSMCNHAERTALFNagSEG 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 492558561  89 SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSD 122
Cdd:cd00786   63 DTKGQMLYVALSPCGACAQLIIELGIKDVIVVLT 96
cd PHA02588
deoxycytidylate deaminase; Provisional
 13-151 3.55e-24

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 92.13  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  13 FMGVALLSGKRSKDPNTQVGACIVNEEKkIVGVGYNGLPIG---CSD--DEYPW-EREGEFLETKYPF--------VCHA 78
Cdd:PHA02588   6 YLQIAYLVSQESKCVSWKVGAVIEKNGR-IISTGYNGTPAGgvnCCDhaNEQGWlDDEGKLKKEHRPEhsawssknEIHA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492558561  79 ELNAIL---NSTKSLKNCTIYVALFPCHECSKAIIQSGIRELVYLsDKYDGTESNIASkkMLTSAGVKFRQLKSKI 151
Cdd:PHA02588  85 ELNAILfaaRNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYC-EKYDRNGPGWDD--ILRKSGIEVIQIPKEE 157
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 7-147 1.86e-21

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: 84.53  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561    7 IEWDEYFMGVALLSGKRSKDPNTQVGACIVnEEKKIVGVGYNGLPIG---CSDdeypwerEGEFLETKYPF-VCHAELNA 82
Cdd:TIGR02571   3 IKWDQYFMAQSHLLALRSTCTRLSVGATIV-RDKRIIAGGYNGSVAGgvhCID-------EGCYVVDGHCVrTIHAEMNA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492558561   83 ILNSTK---SLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDgtesNIASKKMLTSAGVKFRQL 147
Cdd:TIGR02571  75 LLQCAKfgvSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHN----HPYAIELFEQAGVELKKV 138
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 31-120 7.67e-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: 63.79  E-value: 7.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  31 VGACIVNEEKKIVGVGYNglpigcsddeypweregEFLETKYPfVCHAELNAILN-----STKSLKNCTIYVALFPCHEC 105
Cdd:cd01285   19 FGAVIVDDDGKVIARGHN-----------------RVEQDGDP-TAHAEIVAIRNaarrlGSYLLSGCTLYTTLEPCPMC 80

                         90
                 ....*....|....*
gi 492558561 106 SKAIIQSGIRELVYL 120
Cdd:cd01285   81 AGALLWARIKRVVYG 95
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 7-136 5.02e-13

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: 62.54  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561    7 IEWDEYFMGVALLSGKRSKDPNTQVGACIVnEEKKIVGVGYNglpigcsddeypwEREGEFLETKypfvcHAELNAIL-- 84
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIV-KDGKVIARGYN-------------RKELNADTTA-----HAEILAIQqa 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 492558561   85 ---NSTKSLKNCTIYVALFPCHECSKAIIQSGIRELVYLSDKYDGTESNIASKKM 136
Cdd:pfam14437  62 akkLGSWRLDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKL 116
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 10-119 7.94e-13

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: 62.06  E-value: 7.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  10 DEYFMGVAL----LSGKRSKDPntqVGACIVNEEKkIVGVGYNglpigcsddeypwEREGEFLETkypfvCHAELNAILN 85
Cdd:COG0590    4 DEEFMRRALelarKAVAEGEVP---VGAVLVKDGE-IIARGHN-------------RVETLNDPT-----AHAEILAIRA 61

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492558561  86 -----STKSLKNCTIYVALFPCHECSKAIIQSGIRELVY 119
Cdd:COG0590   62 aarklGNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVY 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 11-119 5.45e-12

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: 62.00  E-value: 5.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  11 EYFMGVALLSGKRSK---DPNTQVGACIVNEEKkIVGVGY---NGLPigcsddeypweregefletkypfvcHAELNAIL 84
Cdd:COG0117    1 ERYMRRALELARRGLgttSPNPLVGCVIVKDGR-IVGEGYhqrAGGP-------------------------HAEVNALA 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 492558561  85 NSTKSLKNCTIYVALFPC-HE-----CSKAIIQSGIRELVY 119
Cdd:COG0117   55 QAGEAARGATLYVTLEPCsHHgrtppCADALIEAGIKRVVI 95
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 26-119 2.70e-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: 57.24  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  26 DPNTQVGACIVNEEKKIVGVGYN---GLPigcsddeypweregefletkypfvcHAELNAILN-STKSLKNCTIYVALFP 101
Cdd:cd01284   16 SPNPPVGCVIVDDDGEIVGEGYHrkaGGP-------------------------HAEVNALASaGEKLARGATLYVTLEP 70

                         90       100
                 ....*....|....*....|....
gi 492558561 102 C------HECSKAIIQSGIRELVY 119
Cdd:cd01284   71 CshhgktPPCVDAIIEAGIKRVVV 94
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 14-161 7.47e-11

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: 59.07  E-value: 7.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561   14 MGVALLSGKRSK---DPNTQVGACIVNEEKkIVGVGYNglpigcsddeypwEREGEfletkypfvCHAELNAILNSTKSL 90
Cdd:TIGR00326   1 MNRALDLAKKGQgttHPNPLVGCVIVKNGE-IVGEGAH-------------QKAGE---------PHAEVHALRQAGENA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561   91 KNCTIYVALFPC-HE-----CSKAIIQSGIRELVYLSDKydgTESNIASK--KMLTSAG--VKFRQLKSKIGKLELSFDE 160
Cdd:TIGR00326  58 KGATAYVTLEPCsHQgrtppCAEAIIEAGIKKVVVSMQD---PNPLVAGRgaERLKQAGieVTFGILKEEAERLNKGFLK 134


                  .
gi 492558561  161 R 161
Cdd:TIGR00326 135 R 135
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 10-119 5.42e-09

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 52.50  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  10 DEYFMGVALLSGKRSKDP-NTQVGACIVNEeKKIVGVGYNgLPIGCSDDeypweregefletkypfVCHAELNAILNSTK 88
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDErEVPVGAVLVHN-NRVIGEGWN-RPIGRHDP-----------------TAHAEIMALRQGGL 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 492558561  89 SLKN-----CTIYVALFPCHECSKAIIQSGIRELVY 119
Cdd:PRK10860  74 VLQNyrlldATLYVTLEPCVMCAGAMVHSRIGRLVF 109
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 10-118 5.03e-06

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 45.14  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  10 DEYFMGVAL---LSGKRSKDPNTQVGACIVNEEKkIVGVGYNglpigcsddeypwEREGEfletkyPfvcHAELNAILNS 86
Cdd:PRK10786   3 DEFYMARALklaQRGRFTTHPNPNVGCVIVKDGE-IVGEGYH-------------QRAGE------P---HAEVHALRMA 59

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 492558561  87 TKSLKNCTIYVALFPC-HE-----CSKAIIQSGIRELV 118
Cdd:PRK10786  60 GEKAKGATAYVTLEPCsHHgrtppCCDALIAAGVARVV 97
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 27-118 9.45e-04

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 38.60  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492558561  27 PNTQVGaCIVNEEKKIVGVGYnglpigcsddeYPweREGEfletkyPfvcHAELNAILNSTKSLKNCTIYVALFPCHE-- 104
Cdd:PLN02807  52 PNPMVG-CVIVKDGRIVGEGF-----------HP--KAGQ------P---HAEVFALRDAGDLAENATAYVSLEPCNHyg 108

                         90
                 ....*....|....*...
gi 492558561 105 ----CSKAIIQSGIRELV 118
Cdd:PLN02807 109 rtppCTEALIKAKVKRVV 126
 
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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