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Conserved domains on  [gi|512682427|ref|WP_016474710|]
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MULTISPECIES: deaminase [Sutterella]

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];
8-138 3.64e-40

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 131.50  E-value: 3.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   8 QMYMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE-----MEVDGKLVTRPE---VQHAELNAIAKL 79
Cdd:COG2131   10 EYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEvgclrEKLGIPSGERGEccrTVHAEQNAILQA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 512682427  80 AENGYSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELYRSREGLDFLERAGIKVTQL 138
Cdd:COG2131   90 ARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQL 148
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
8-138 3.64e-40

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 131.50  E-value: 3.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   8 QMYMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE-----MEVDGKLVTRPE---VQHAELNAIAKL 79
Cdd:COG2131   10 EYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEvgclrEKLGIPSGERGEccrTVHAEQNAILQA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 512682427  80 AENGYSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELYRSREGLDFLERAGIKVTQL 138
Cdd:COG2131   90 ARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQL 148
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-129 1.84e-37

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: 123.92  E-value: 1.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  10 YMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE------MEVDGKLVTRPEVQHAELNAIAKLAENG 83
Cdd:cd01286    4 FMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEvgcerdDLPSGEDQKCCRTVHAEQNAILQAARHG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 512682427  84 YSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELYRS--REGLDFLE 129
Cdd:cd01286   84 VSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDddPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 6-138 4.36e-30

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 106.38  E-value: 4.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   6 DNQMYMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE-------MEVDGKL--VTRPE--------V 68
Cdd:PHA02588   2 KDSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhaneqgwLDDEGKLkkEHRPEhsawssknE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512682427  69 QHAELNAIAKLAENGYSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELY-RSREG-LDFLERAGIKVTQL 138
Cdd:PHA02588  82 IHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdRNGPGwDDILRKSGIEVIQI 153
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-116 3.27e-25

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 91.98  E-value: 3.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   10 YMRIAQIAAERSYAK-RLKVGCVIVK-NHSIISFGWNGMPTGYDNCCemevdgklvtrpevqHAELNAIAKLAENGYSSK 87
Cdd:pfam00383   5 FMRLALKAAKRAYPYsNFPVGAVIVKkDGEIIATGYNGENAGYDPTI---------------HAERNAIRQAGKRGEGVR 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 512682427   88 --DAAIFITHSPCIHCALLIQKCGISQVFYH 116
Cdd:pfam00383  70 leGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 28-136 1.79e-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: 62.92  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   28 VGCVIVKNHSIISFGWNgmptgydnccemevdgklvTRPEVQHAELNAiakLAENGYSSKDAAIFITHSPCIH------C 101
Cdd:TIGR00326  21 VGCVIVKNGEIVGEGAH-------------------QKAGEPHAEVHA---LRQAGENAKGATAYVTLEPCSHqgrtppC 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 512682427  102 ALLIQKCGISQVFY-----HELYRSReGLDFLERAGIKVT 136
Cdd:TIGR00326  79 AEAIIEAGIKKVVVsmqdpNPLVAGR-GAERLKQAGIEVT 117
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
8-138 3.64e-40

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 131.50  E-value: 3.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   8 QMYMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE-----MEVDGKLVTRPE---VQHAELNAIAKL 79
Cdd:COG2131   10 EYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEvgclrEKLGIPSGERGEccrTVHAEQNAILQA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 512682427  80 AENGYSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELYRSREGLDFLERAGIKVTQL 138
Cdd:COG2131   90 ARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQL 148
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 10-129 1.84e-37

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: 123.92  E-value: 1.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  10 YMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE------MEVDGKLVTRPEVQHAELNAIAKLAENG 83
Cdd:cd01286    4 FMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEvgcerdDLPSGEDQKCCRTVHAEQNAILQAARHG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 512682427  84 YSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELYRS--REGLDFLE 129
Cdd:cd01286   84 VSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDddPAAAELLE 131
cd PHA02588
deoxycytidylate deaminase; Provisional
 6-138 4.36e-30

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 106.38  E-value: 4.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   6 DNQMYMRIAQIAAERSYAKRLKVGCVIVKNHSIISFGWNGMPTGYDNCCE-------MEVDGKL--VTRPE--------V 68
Cdd:PHA02588   2 KDSTYLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDhaneqgwLDDEGKLkkEHRPEhsawssknE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512682427  69 QHAELNAIAKLAENGYSSKDAAIFITHSPCIHCALLIQKCGISQVFYHELY-RSREG-LDFLERAGIKVTQL 138
Cdd:PHA02588  82 IHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYdRNGPGwDDILRKSGIEVIQI 153
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-116 3.27e-25

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 91.98  E-value: 3.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   10 YMRIAQIAAERSYAK-RLKVGCVIVK-NHSIISFGWNGMPTGYDNCCemevdgklvtrpevqHAELNAIAKLAENGYSSK 87
Cdd:pfam00383   5 FMRLALKAAKRAYPYsNFPVGAVIVKkDGEIIATGYNGENAGYDPTI---------------HAERNAIRQAGKRGEGVR 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 512682427   88 --DAAIFITHSPCIHCALLIQKCGISQVFYH 116
Cdd:pfam00383  70 leGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 28-136 1.79e-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: 62.92  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   28 VGCVIVKNHSIISFGWNgmptgydnccemevdgklvTRPEVQHAELNAiakLAENGYSSKDAAIFITHSPCIH------C 101
Cdd:TIGR00326  21 VGCVIVKNGEIVGEGAH-------------------QKAGEPHAEVHA---LRQAGENAKGATAYVTLEPCSHqgrtppC 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 512682427  102 ALLIQKCGISQVFY-----HELYRSReGLDFLERAGIKVT 136
Cdd:TIGR00326  79 AEAIIEAGIKKVVVsmqdpNPLVAGR-GAERLKQAGIEVT 117
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 28-136 3.67e-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: 61.61  E-value: 3.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  28 VGCVIVKNHSIISFGW---NGMPtgydnccemevdgklvtrpevqHAELNAIAKLAEngySSKDAAIFITHSPCIH---- 100
Cdd:COG0117   24 VGCVIVKDGRIVGEGYhqrAGGP----------------------HAEVNALAQAGE---AARGATLYVTLEPCSHhgrt 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 512682427 101 --CALLIQKCGISQVFY-----HELYRSReGLDFLERAGIKVT 136
Cdd:COG0117   79 ppCADALIEAGIKRVVIamldpNPLVAGK-GIARLRAAGIEVE 120
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 28-132 7.77e-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: 55.32  E-value: 7.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  28 VGCVIVK-NHSIISFGWN---GMPtgydnccemevdgklvtrpevqHAELNAIAKLAENgySSKDAAIFITHSPCIH--- 100
Cdd:cd01284   21 VGCVIVDdDGEIVGEGYHrkaGGP----------------------HAEVNALASAGEK--LARGATLYVTLEPCSHhgk 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 512682427 101 ---CALLIQKCGISQVFYH----ELYRSREGLDFLERAG 132
Cdd:cd01284   77 tppCVDAIIEAGIKRVVVGvrdpNPLVAGKGAERLRAAG 115
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 11-115 9.46e-09

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: 49.92  E-value: 9.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  11 MRIAQIAAERSYAK-RLKVGCVIVKNH-SIISFGWNgmptgydncceMEVDGKLVTRpevqHAELNAIAKLAEN--GYSS 86
Cdd:cd01285    1 MRLAIELARKALAEgEVPFGAVIVDDDgKVIARGHN-----------RVEQDGDPTA----HAEIVAIRNAARRlgSYLL 65

                         90       100
                 ....*....|....*....|....*....
gi 512682427  87 KDAAIFITHSPCIHCALLIQKCGISQVFY 115
Cdd:cd01285   66 SGCTLYTTLEPCPMCAGALLWARIKRVVY 94
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 10-115 4.21e-08

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: 48.96  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  10 YMRIAQIAAERSYAKR-LKVGCVIVKNHSIISFGWNGM-----PTGydnccemevdgklvtrpevqHAELNAIAKLAE-- 81
Cdd:COG0590    7 FMRRALELARKAVAEGeVPVGAVLVKDGEIIARGHNRVetlndPTA--------------------HAEILAIRAAARkl 66

                         90       100       110
                 ....*....|....*....|....*....|....
gi 512682427  82 NGYSSKDAAIFITHSPCIHCALLIQKCGISQVFY 115
Cdd:COG0590   67 GNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVY 100
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 11-114 4.06e-07

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 45.23  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  11 MRIAQIAAERSYAK--RLKVGCVIVKNHsiisfGWNGMPTGydncCEMEVdgklVTRPEVQHAELNAIAKL-AENGYssK 87
Cdd:cd00786    1 MTEALKAADLGYAKesNFQVGACLVNKK-----DGGKVGRG----CNIEN----AAYSMCNHAERTALFNAgSEGDT--K 65

                         90       100
                 ....*....|....*....|....*..
gi 512682427  88 DAAIFITHSPCIHCALLIQKCGISQVF 114
Cdd:cd00786   66 GQMLYVALSPCGACAQLIIELGIKDVI 92
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 14-106 7.92e-06

Cytidine deaminase zinc-binding domain. These enzymes 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. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes.


Pssm-ID: 238610 [Multi-domain]  Cd Length: 112  Bit Score: 41.94  E-value: 7.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427  14 AQIAAERSYAK--RLKVGCVIVKNHSIISFGWNGMPTGYDNCCemevdgklvtrpevqHAELNAIAKLAENGYSSKDAAI 91
Cdd:cd01283    4 ALAAAEFAYAPysNFTVGAALLTKDGRIFTGVNVENASYGLTL---------------CAERTAIGKAVSEGLRRYLVTW 68

                         90       100
                 ....*....|....*....|
gi 512682427  92 FITH-----SPCIHCALLIQ 106
Cdd:cd01283   69 AVSDeggvwSPCGACRQVLA 88
APOBEC_N pfam08210
APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. ...
 70-135 2.59e-03

APOBEC-like N-terminal domain; A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC-1 like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalyitc domain. More specifically, the catalytic domain is a zinc dependent deaminases domain and is essential for cytidine deamination.APOBEC-3 like members contain two copies of this domain. RNA editing by APOBEC-1 requires homodimerization and this complex interacts with RNA binding proteins to from the editosome (and references therein). This family also includes the functionally homologous activation induced deaminase (AID), which is essential for the development of antibody diversity in B lymphocytes, and the sea lamprey PmCDA1 and PmCDA2, which are predicted to play an AID-like role in the adaptive immune response of jawless vertebrates. Divergent members of this family are present in various eukaryotes such as Nematostella, C. elegans, Micromonas and Emiliania, and prokaryotes such as Wolbachia and Pseudomonas brassicacearum.


Pssm-ID: 462396 [Multi-domain]  Cd Length: 170  Bit Score: 36.19  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512682427   70 HAE---LNAIAKLAENGYSSKDAAIFITHSPCIHCA-----LLIQKCGI------SQVFYHE--LYRSREGLDFLERAGI 133
Cdd:pfam08210  47 HAEerfLRWIHDLALDPGSNYEVTWYVSWSPCNECAselaaFLSKHPNVrlrifvSRLYYWEepDYWNREGLRSLAQAGV 126


                  ..
gi 512682427  134 KV 135
Cdd:pfam08210 127 QL 128
 
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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