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Conserved domains on  [gi|755533180|ref|XP_011241502|]
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tRNA-specific adenosine deaminase 2 isoform X1 [Mus musculus]

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
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 23-116 7.49e-30

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: 105.20  E-value: 7.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  23 EKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCHQHGqspSTVFEHTVLYV 102
Cdd:COG0590    5 EEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAA---ARKLG---NWRLSGCTLYV 78

                         90
                 ....*....|....
gi 755533180 103 TVEPCIMCAAALRL 116
Cdd:COG0590   79 TLEPCPMCAGAIVW 92
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 23-116 7.49e-30

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: 105.20  E-value: 7.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  23 EKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCHQHGqspSTVFEHTVLYV 102
Cdd:COG0590    5 EEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAA---ARKLG---NWRLSGCTLYV 78

                         90
                 ....*....|....
gi 755533180 103 TVEPCIMCAAALRL 116
Cdd:COG0590   79 TLEPCPMCAGAIVW 92
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 26-116 1.09e-29

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: 103.85  E-value: 1.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  26 MEEAMRMAKEALENIEVPVGCLMVYNN-EVVGKGRNEVNQTKNATRHAEMVAIDQVLDWChqhgqsPSTVFEHTVLYVTV 104
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRL------GSYLLSGCTLYTTL 74

                         90
                 ....*....|..
gi 755533180 105 EPCIMCAAALRL 116
Cdd:cd01285   75 EPCPMCAGALLW 86
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
23-116 1.13e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 75.42  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180   23 EKWMEEAMRMAKEALENIEVPVGCLMV-YNNEVVGKGRNEVNQTKNATRHAEMVAIDQVLDwchqhgQSPSTVFEHTVLY 101
Cdd:pfam00383   3 EYFMRLALKAAKRAYPYSNFPVGAVIVkKDGEIIATGYNGENAGYDPTIHAERNAIRQAGK------RGEGVRLEGATLY 76

                          90
                  ....*....|....*
gi 755533180  102 VTVEPCIMCAAALRL 116
Cdd:pfam00383  77 VTLEPCGMCAQAIIE 91
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 23-114 1.00e-17

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 74.84  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  23 EKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIdqvldwcHQHGQSPSTV-FEHTVLY 101
Cdd:PRK10860  14 EYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMAL-------RQGGLVLQNYrLLDATLY 86

                         90
                 ....*....|...
gi 755533180 102 VTVEPCIMCAAAL 114
Cdd:PRK10860  87 VTLEPCVMCAGAM 99
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 43-107 6.21e-05

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: 41.35  E-value: 6.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755533180   43 PVGCLMVYNNEVVGKGRNEvnqtKNATRHAEMVAIdqvldwcHQHGQSPstvfEHTVLYVTVEPC 107
Cdd:TIGR00326  20 LVGCVIVKNGEIVGEGAHQ----KAGEPHAEVHAL-------RQAGENA----KGATAYVTLEPC 69
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 23-116 7.49e-30

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: 105.20  E-value: 7.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  23 EKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCHQHGqspSTVFEHTVLYV 102
Cdd:COG0590    5 EEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAA---ARKLG---NWRLSGCTLYV 78

                         90
                 ....*....|....
gi 755533180 103 TVEPCIMCAAALRL 116
Cdd:COG0590   79 TLEPCPMCAGAIVW 92
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 26-116 1.09e-29

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: 103.85  E-value: 1.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  26 MEEAMRMAKEALENIEVPVGCLMVYNN-EVVGKGRNEVNQTKNATRHAEMVAIDQVLDWChqhgqsPSTVFEHTVLYVTV 104
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRL------GSYLLSGCTLYTTL 74

                         90
                 ....*....|..
gi 755533180 105 EPCIMCAAALRL 116
Cdd:cd01285   75 EPCPMCAGALLW 86
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
23-116 1.13e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 75.42  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180   23 EKWMEEAMRMAKEALENIEVPVGCLMV-YNNEVVGKGRNEVNQTKNATRHAEMVAIDQVLDwchqhgQSPSTVFEHTVLY 101
Cdd:pfam00383   3 EYFMRLALKAAKRAYPYSNFPVGAVIVkKDGEIIATGYNGENAGYDPTIHAERNAIRQAGK------RGEGVRLEGATLY 76

                          90
                  ....*....|....*
gi 755533180  102 VTVEPCIMCAAALRL 116
Cdd:pfam00383  77 VTLEPCGMCAQAIIE 91
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 23-114 3.99e-18

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: 75.25  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180   23 EKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVldwCHQHGqspSTVFEHTVLYV 102
Cdd:pfam14437   4 EKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQA---AKKLG---SWRLDDATLYV 77

                          90
                  ....*....|..
gi 755533180  103 TVEPCIMCAAAL 114
Cdd:pfam14437  78 TLEPCPMCAGAI 89
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 23-114 1.00e-17

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 74.84  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  23 EKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIdqvldwcHQHGQSPSTV-FEHTVLY 101
Cdd:PRK10860  14 EYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMAL-------RQGGLVLQNYrLLDATLY 86

                         90
                 ....*....|...
gi 755533180 102 VTVEPCIMCAAAL 114
Cdd:PRK10860  87 VTLEPCVMCAGAM 99
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 23-114 8.49e-07

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: 46.59  E-value: 8.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  23 EKWMEEAMRMAKEAL----ENievP-VGCLMVYNNEVVGKGRnevnqTKNA-TRHAEMVAIDQVldwchqhGQSPStvfe 96
Cdd:COG0117    1 ERYMRRALELARRGLgttsPN---PlVGCVIVKDGRIVGEGY-----HQRAgGPHAEVNALAQA-------GEAAR---- 61

                         90       100
                 ....*....|....*....|....
gi 755533180  97 HTVLYVTVEPCIM------CAAAL 114
Cdd:COG0117   62 GATLYVTLEPCSHhgrtppCADAL 85
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
24-111 2.32e-06

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 44.45  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  24 KWMEEAMRMAKEALEN---IEVPVGCLMVYNNEVVGKGRN----------------EVNQTKNATR-------HAEMVAI 77
Cdd:COG2131    7 SWDEYFMEIAKLVALRstcLRRQVGAVIVKDKRILATGYNgapsglphcdevgclrEKLGIPSGERgeccrtvHAEQNAI 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 755533180  78 DQvldwCHQHGQSPstvfEHTVLYVTVEPCIMCA 111
Cdd:COG2131   87 LQ----AARHGVST----EGATLYVTHFPCLECA 112
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 26-114 2.89e-06

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


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 42.92  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  26 MEEAMRMAKEAL-ENIEVPVGCLMVYNNE--VVGKGRNEVNQTKNATRHAEMVAIDQvldwCHQHGQspstvFEHTVLYV 102
Cdd:cd00786    1 MTEALKAADLGYaKESNFQVGACLVNKKDggKVGRGCNIENAAYSMCNHAERTALFN----AGSEGD-----TKGQMLYV 71

                         90
                 ....*....|..
gi 755533180 103 TVEPCIMCAAAL 114
Cdd:cd00786   72 ALSPCGACAQLI 83
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 30-114 1.15e-05

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: 42.26  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  30 MRMAKEALENIEVP---VGCLMVYNNEVVGKGRN---------------------EVNQTKNATRHAEMVAIDQvldwCH 85
Cdd:cd01286    5 MAIARLAALRSTCPrrqVGAVIVKDKRIISTGYNgspsglphcaevgcerddlpsGEDQKCCRTVHAEQNAILQ----AA 80

                         90       100
                 ....*....|....*....|....*....
gi 755533180  86 QHGQSPstvfEHTVLYVTVEPCIMCAAAL 114
Cdd:cd01286   81 RHGVSL----EGATLYVTLFPCIECAKLI 105
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 43-107 6.21e-05

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: 41.35  E-value: 6.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755533180   43 PVGCLMVYNNEVVGKGRNEvnqtKNATRHAEMVAIdqvldwcHQHGQSPstvfEHTVLYVTVEPC 107
Cdd:TIGR00326  20 LVGCVIVKNGEIVGEGAHQ----KAGEPHAEVHAL-------RQAGENA----KGATAYVTLEPC 69
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 26-107 1.49e-04

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: 38.75  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180  26 MEEAMRMAKEALENIEV--PVGCLMVYNN-EVVGKGRNEvnqtKNATRHAEMVAIDQVLDwchqhgqspsTVFEHTVLYV 102
Cdd:cd01284    1 MRRALELAEKGRGLTSPnpPVGCVIVDDDgEIVGEGYHR----KAGGPHAEVNALASAGE----------KLARGATLYV 66


                 ....*
gi 755533180 103 TVEPC 107
Cdd:cd01284   67 TLEPC 71
Bd3614-deam pfam14439
Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 53-112 3.86e-03

Bd3614-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Bdellovibrio Bd3614. They are typified by a distinct N-terminal globular domain. The Bdellovibrio version occurs in a predicted operon with a 23S rRNA G2445-modifying methylase suggesting that it might be involved in RNA editing.


Pssm-ID: 405177 [Multi-domain]  Cd Length: 113  Bit Score: 34.81  E-value: 3.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755533180   53 EVVGKGRNevNQTKNATRHAEMVAIdQVLDWCHQHGQSPstvfEHTVLYVTVEPCIMCAA 112
Cdd:pfam14439  20 QLLDAAVN--TNAKNKTLHAEVNLL-QPLLRETARRPIP----PGARLLVTLQCCKMCAA 72
 
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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