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Conserved domains on  [gi|30750134|pdb|1UAQ|A]
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Chain A, cytosine deaminase

Protein Classification

nucleoside deaminase( domain architecture ID 10001752)

nucleoside deaminase such as adenosine, guanine, or cytosine deaminase is a Zn-dependent enzyme which catalyzes 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

EC:  3.5.4.-
Gene Ontology:  GO:0008270|GO:0019239|GO:0009116
PubMed:  38524700
SCOP:  3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 15-109 1.69e-41

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: 133.83  E-value: 1.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       15 MDIAYEEAALGY-KEGGVPIGGCLINNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGkvYKDTTLYTTLSPCDM 93
Cdd:cd00786   1 MTEALKAADLGYaKESNFQVGACLVNKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGD--TKGQMLYVALSPCGA 78

                        90
                ....*....|....*...
1UAQ_A       94 CTGAIIMYGI--PRCVVG 109
Cdd:cd00786  79 CAQLIIELGIkdVIVVLT 96
 
Name Accession Description Interval E-value
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 15-109 1.69e-41

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: 133.83  E-value: 1.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       15 MDIAYEEAALGY-KEGGVPIGGCLINNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGkvYKDTTLYTTLSPCDM 93
Cdd:cd00786   1 MTEALKAADLGYaKESNFQVGACLVNKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGD--TKGQMLYVALSPCGA 78

                        90
                ....*....|....*...
1UAQ_A       94 CTGAIIMYGI--PRCVVG 109
Cdd:cd00786  79 CAQLIIELGIkdVIVVLT 96
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 11-148 4.79e-39

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: 129.47  E-value: 4.79e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       11 DQKGMDIAYEEAALGYKEGGVPIGGCLInnKDGSVLGRGHNMRFQKGSATLHGEISTLEN-CGRLEGKVYKDTTLYTTLS 89
Cdd:COG0590   4 DEEFMRRALELARKAVAEGEVPVGAVLV--KDGEIIARGHNRVETLNDPTAHAEILAIRAaARKLGNWRLSGCTLYVTLE 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1UAQ_A       90 PCDMCTGAIIMYGIPRCVVGENvNFKSKGEKYL------QTRGHEVVV---VDDERCKKIMKQFIDER 148
Cdd:COG0590  82 PCPMCAGAIVWARIGRVVYGAS-DPKAGAAGSIydlladPRLNHRVEVvggVLAEECAALLRDFFAAR 148
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-109 1.65e-31

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 108.54  E-value: 1.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A         10 WDQKGMDIAYEEAALGYKEGGVPIGGCLINNkDGSVLGRGHNMRFQKGSATLHGEISTLENCGRL-EGKVYKDTTLYTTL 88
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVGAVIVKK-DGEIIATGYNGENAGYDPTIHAERNAIRQAGKRgEGVRLEGATLYVTL 79

                          90       100
                  ....*....|....*....|.
1UAQ_A         89 SPCDMCTGAIIMYGIPRCVVG 109
Cdd:pfam00383  80 EPCGMCAQAIIESGIKRVVFG 100
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 11-111 1.00e-12

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 62.13  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A        11 DQKGMDIAYEEAALGYKEGGVPIGGCLINNkdGSVLGRGHNMRFQKGSATLHGEISTLENCG-RLEGKVYKDTTLYTTLS 89
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDEREVPVGAVLVHN--NRVIGEGWNRPIGRHDPTAHAEIMALRQGGlVLQNYRLLDATLYVTLE 90

                         90       100
                 ....*....|....*....|..
1UAQ_A        90 PCDMCTGAIIMYGIPRCVVGEN 111
Cdd:PRK10860  91 PCVMCAGAMVHSRIGRLVFGAR 112
 
Name Accession Description Interval E-value
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 15-109 1.69e-41

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: 133.83  E-value: 1.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       15 MDIAYEEAALGY-KEGGVPIGGCLINNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGkvYKDTTLYTTLSPCDM 93
Cdd:cd00786   1 MTEALKAADLGYaKESNFQVGACLVNKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGD--TKGQMLYVALSPCGA 78

                        90
                ....*....|....*...
1UAQ_A       94 CTGAIIMYGI--PRCVVG 109
Cdd:cd00786  79 CAQLIIELGIkdVIVVLT 96
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 11-148 4.79e-39

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: 129.47  E-value: 4.79e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       11 DQKGMDIAYEEAALGYKEGGVPIGGCLInnKDGSVLGRGHNMRFQKGSATLHGEISTLEN-CGRLEGKVYKDTTLYTTLS 89
Cdd:COG0590   4 DEEFMRRALELARKAVAEGEVPVGAVLV--KDGEIIARGHNRVETLNDPTAHAEILAIRAaARKLGNWRLSGCTLYVTLE 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1UAQ_A       90 PCDMCTGAIIMYGIPRCVVGENvNFKSKGEKYL------QTRGHEVVV---VDDERCKKIMKQFIDER 148
Cdd:COG0590  82 PCPMCAGAIVWARIGRVVYGAS-DPKAGAAGSIydlladPRLNHRVEVvggVLAEECAALLRDFFAAR 148
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 15-114 7.83e-38

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: 125.04  E-value: 7.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       15 MDIAYEEAALGYKEGGVPIGGCLINNkDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGK-VYKDTTLYTTLSPCDM 93
Cdd:cd01285   1 MRLAIELARKALAEGEVPFGAVIVDD-DGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSyLLSGCTLYTTLEPCPM 79

                        90       100
                ....*....|....*....|.
1UAQ_A       94 CTGAIIMYGIPRCVVGENVNF 114
Cdd:cd01285  80 CAGALLWARIKRVVYGASDPK 100
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-109 1.65e-31

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 108.54  E-value: 1.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A         10 WDQKGMDIAYEEAALGYKEGGVPIGGCLINNkDGSVLGRGHNMRFQKGSATLHGEISTLENCGRL-EGKVYKDTTLYTTL 88
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVGAVIVKK-DGEIIATGYNGENAGYDPTIHAERNAIRQAGKRgEGVRLEGATLYVTL 79

                          90       100
                  ....*....|....*....|.
1UAQ_A         89 SPCDMCTGAIIMYGIPRCVVG 109
Cdd:pfam00383  80 EPCGMCAQAIIESGIKRVVFG 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 11-148 1.00e-20

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: 82.57  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A         11 DQKGMDIAYEEAALGYKEGGVPIGGCLInnKDGSVLGRGHNMRFQKGSATLHGEISTLEN-CGRLEGKVYKDTTLYTTLS 89
Cdd:pfam14437   3 HEKWFRKALGLAEKAYDAGEVPIGAVIV--KDGKVIARGYNRKELNADTTAHAEILAIQQaAKKLGSWRLDDATLYVTLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1UAQ_A         90 PCDMCTGAIIMYGIPRCVVG-ENVNFKSKG----EKYLQTRGHEVVVVDDErCKKIMKQFIDER 148
Cdd:pfam14437  81 PCPMCAGAIVQAGLKSLVYGaGNPKGGAVGsvlnKLVIVLWNHRVELVEED-CSEILKGFFKKL 143
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 11-111 1.00e-12

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 62.13  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A        11 DQKGMDIAYEEAALGYKEGGVPIGGCLINNkdGSVLGRGHNMRFQKGSATLHGEISTLENCG-RLEGKVYKDTTLYTTLS 89
Cdd:PRK10860  13 HEYWMRHALTLAKRAWDEREVPVGAVLVHN--NRVIGEGWNRPIGRHDPTAHAEIMALRQGGlVLQNYRLLDATLYVTLE 90

                         90       100
                 ....*....|....*....|..
1UAQ_A        90 PCDMCTGAIIMYGIPRCVVGEN 111
Cdd:PRK10860  91 PCVMCAGAMVHSRIGRLVFGAR 112
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 35-126 3.40e-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: 56.86  E-value: 3.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       35 GCLINNKDGSVLGRGHNMRFqkGSAtlHGEISTLENCGrleGKVYKDTTLYTTLSPCDM------CTGAIIMYGIPRCVV 108
Cdd:cd01284  22 GCVIVDDDGEIVGEGYHRKA--GGP--HAEVNALASAG---EKLARGATLYVTLEPCSHhgktppCVDAIIEAGIKRVVV 94

                        90       100
                ....*....|....*....|.
1UAQ_A      109 G---ENVNFKSKGEKYLQTRG 126
Cdd:cd01284  95 GvrdPNPLVAGKGAERLRAAG 115
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 15-145 6.98e-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: 58.92  E-value: 6.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       15 MDIAYEEAALGykEGGV---PIGGCLINnKDGSVLGRGHNMRFqkGSAtlHGEISTLENCG-RLEGkvykdTTLYTTLSP 90
Cdd:COG0117   4 MRRALELARRG--LGTTspnPLVGCVIV-KDGRIVGEGYHQRA--GGP--HAEVNALAQAGeAARG-----ATLYVTLEP 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1UAQ_A       91 CDM------CTGAIIMYGIPRCVVG---ENVNFKSKGEKYLQTRGHEVVV-VDDERCKKIMKQFI 145
Cdd:COG0117  72 CSHhgrtppCADALIEAGIKRVVIAmldPNPLVAGKGIARLRAAGIEVEVgVLEEEARALNRGFL 136
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
9-135 1.47e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 53.31  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A        9 KWDQKGMDIAYEEA---------------------ALGYKegGVPIG-------GCLiNNKDGSVLGRGHNMrfqkgSAT 60
Cdd:COG2131   7 SWDEYFMEIAKLVAlrstclrrqvgavivkdkrilATGYN--GAPSGlphcdevGCL-REKLGIPSGERGEC-----CRT 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1UAQ_A       61 LHGEISTLENCGRLeGKVYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNfKSKGEKYLQTRGHEVVVVDDE 135
Cdd:COG2131  79 VHAEQNAILQAARH-GVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYP-DELAKELLKEAGVEVRQLELE 151
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 23-111 2.91e-09

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: 52.28  E-value: 2.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A       23 ALGYkeGGVPIG-------GCLINNKDGSVLgrghnmrfQKGSATLHGEISTLENCGRlEGKVYKDTTLYTTLSPCDMCT 95
Cdd:cd01286  34 STGY--NGSPSGlphcaevGCERDDLPSGED--------QKCCRTVHAEQNAILQAAR-HGVSLEGATLYVTLFPCIECA 102

                        90
                ....*....|....*.
1UAQ_A       96 GAIIMYGIPRCVVGEN 111
Cdd:cd01286 103 KLIIQAGIKKVVYAEP 118
cd PHA02588
deoxycytidylate deaminase; Provisional
 76-140 2.08e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 45.13  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1UAQ_A        76 GKVYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNfKSKGE--KYLQTRGHEVVVVDDERCKKI 140
Cdd:PHA02588  96 GISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYD-RNGPGwdDILRKSGIEVIQIPKEELNKL 161
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 11-129 2.32e-05

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


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 43.22  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UAQ_A        11 DQKGMDIAYEEAALG-YKEGGVPIGGCLINnKDGSVLGRGHNMRfqkgSATLHGEISTLencgRLEGKVYKDTTLYTTLS 89
Cdd:PRK10786   3 DEFYMARALKLAQRGrFTTHPNPNVGCVIV-KDGEIVGEGYHQR----AGEPHAEVHAL----RMAGEKAKGATAYVTLE 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
1UAQ_A        90 PCDM------CTGAIIMYGIPRCVVG---ENVNFKSKGEKYLQTRGHEV 129
Cdd:PRK10786  74 PCSHhgrtppCCDALIAAGVARVVAAmqdPNPQVAGRGLYRLQQAGIDV 122
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 35-108 5.08e-04

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: 37.71  E-value: 5.08e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UAQ_A       35 GCLINNKDGSVLgRGHNMRFQKGSATLHGEISTLENCgRLEGKVYKDTTLYTT-----LSPCDMCTGAIIMYGIPRCVV 108
Cdd:cd01283  21 GAALLTKDGRIF-TGVNVENASYGLTLCAERTAIGKA-VSEGLRRYLVTWAVSdeggvWSPCGACRQVLAEFLPSRLYI 97
 
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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