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Conserved domains on  [gi|444280195|gb|ELU85569|]
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cytidine deaminase [Streptococcus pneumoniae PNI0360]

Protein Classification

cytidine deaminase family protein( domain architecture ID 11416731)

cytidine deaminase family protein catalyzes the deamination of cytidine or deoxycytidine, converting them into uridine or deoxyuridine, and play essential roles in nucleotide metabolism, RNA editing, and immune responses

CATH:  3.40.140.10
EC:  3.5.4.5
Gene Ontology:  GO:0009972|GO:0008270|GO:0004126
PubMed:  16720547
SCOP:  3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 9-131 5.56e-61

Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage


:

Pssm-ID: 440064 [Multi-domain]  Cd Length: 130  Bit Score: 183.43  E-value: 5.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGETEDYL 88
Cdd:COG0295    6 LIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGERE--IKAIAVVADTGEPV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 444280195  89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFS 131
Cdd:COG0295   84 SPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFG 126
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 9-131 5.56e-61

Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440064 [Multi-domain]  Cd Length: 130  Bit Score: 183.43  E-value: 5.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGETEDYL 88
Cdd:COG0295    6 LIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGERE--IKAIAVVADTGEPV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 444280195  89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFS 131
Cdd:COG0295   84 SPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFG 126
PRK05578 PRK05578
cytidine deaminase; Validated
 9-130 4.84e-58

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 175.87  E-value: 4.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGETEDYL 88
Cdd:PRK05578   6 LIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGR--LVAIACVGETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 444280195  89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSF 130
Cdd:PRK05578  84 SPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAF 125
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 9-131 1.43e-46

cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in humans and most bacteria. A related, homodimeric form with a much larger subunit is found in E. coli and in Arabidopsis. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273572 [Multi-domain]  Cd Length: 127  Bit Score: 147.03  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195    9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRkgDILAIAVAGETEDYL 88
Cdd:TIGR01354   3 LFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADDPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 444280195   89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFS 131
Cdd:TIGR01354  81 SPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFG 123
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 10-123 8.91e-41

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: 131.69  E-value: 8.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195  10 MEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKGDIlAIAVAGEtEDYLP 89
Cdd:cd01283    1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLV-TWAVSDE-GGVWS 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 444280195  90 PCNICRQVMVEFCEPDTLVFLLNGKGNILELRLE 123
Cdd:cd01283   79 PCGACRQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-110 2.20e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 79.27  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195    9 LMEQAKKVLKNAYfPYSKFPVGAAILFKDGKVI-TGANIENVSFGVTNCAERSAIFYGTSQGYR---KGDILAIAVAget 84
Cdd:pfam00383   5 FMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIIaTGYNGENAGYDPTIHAERNAIRQAGKRGEGvrlEGATLYVTLE--- 80

                          90       100
                  ....*....|....*....|....*.
gi 444280195   85 edylpPCNICRQVMVEFCePDTLVFL 110
Cdd:pfam00383  81 -----PCGMCAQAIIESG-IKRVVFG 100
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 9-131 5.56e-61

Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440064 [Multi-domain]  Cd Length: 130  Bit Score: 183.43  E-value: 5.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGETEDYL 88
Cdd:COG0295    6 LIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGERE--IKAIAVVADTGEPV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 444280195  89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFS 131
Cdd:COG0295   84 SPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFG 126
PRK05578 PRK05578
cytidine deaminase; Validated
 9-130 4.84e-58

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 175.87  E-value: 4.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGETEDYL 88
Cdd:PRK05578   6 LIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGR--LVAIACVGETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 444280195  89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSF 130
Cdd:PRK05578  84 SPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAF 125
PRK12411 PRK12411
cytidine deaminase; Provisional
 4-135 3.58e-51

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 158.59  E-value: 3.58e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   4 INKFVLMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRkgDILAIAVAGE 83
Cdd:PRK12411   1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDK--EFVAIAIVAD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 444280195  84 TEDYLPPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFSSLEM 135
Cdd:PRK12411  79 TKRPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 9-131 1.43e-46

cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in humans and most bacteria. A related, homodimeric form with a much larger subunit is found in E. coli and in Arabidopsis. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273572 [Multi-domain]  Cd Length: 127  Bit Score: 147.03  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195    9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRkgDILAIAVAGETEDYL 88
Cdd:TIGR01354   3 LFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADDPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 444280195   89 PPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFS 131
Cdd:TIGR01354  81 SPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFG 123
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 10-123 8.91e-41

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: 131.69  E-value: 8.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195  10 MEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKGDIlAIAVAGEtEDYLP 89
Cdd:cd01283    1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLV-TWAVSDE-GGVWS 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 444280195  90 PCNICRQVMVEFCEPDTLVFLLNGKGNILELRLE 123
Cdd:cd01283   79 PCGACRQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-110 2.20e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 79.27  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195    9 LMEQAKKVLKNAYfPYSKFPVGAAILFKDGKVI-TGANIENVSFGVTNCAERSAIFYGTSQGYR---KGDILAIAVAget 84
Cdd:pfam00383   5 FMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIIaTGYNGENAGYDPTIHAERNAIRQAGKRGEGvrlEGATLYVTLE--- 80

                          90       100
                  ....*....|....*....|....*.
gi 444280195   85 edylpPCNICRQVMVEFCePDTLVFL 110
Cdd:pfam00383  81 -----PCGMCAQAIIESG-IKRVVFG 100
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 10-110 2.70e-16

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: 69.12  E-value: 2.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195  10 MEQAKKVLKNAYFPYSKFPVGAAILFK--DGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKGDILAIAvagetedy 87
Cdd:cd00786    1 MTEALKAADLGYAKESNFQVGACLVNKkdGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA-------- 72

                         90       100
                 ....*....|....*....|...
gi 444280195  88 LPPCNICRQVMVEFCEPDTLVFL 110
Cdd:cd00786   73 LSPCGACAQLIIELGIKDVIVVL 95
PRK06848 PRK06848
cytidine deaminase;
9-132 3.98e-13

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 61.68  E-value: 3.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKNAYfPYSKFPVGAAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKGD-ILAIAVAGETED- 86
Cdd:PRK06848  10 LIKAAEKVIEKRY-RNDWHHVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDHEIDtIVAVRHPKPHEDd 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 444280195  87 ----YLPPCNICRQVMVEFCePDTLVfLLNGKGNILELRLEELVPYSFSS 132
Cdd:PRK06848  89 reiwVVSPCGACRELISDYG-KNTNV-IVPYNDELVKVNIMELLPNKYTR 136
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 9-132 5.43e-10

cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis and some Proteobacteria. A related, homotetrameric form with a much smaller subunit is found most bacteria and in animals. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273573 [Multi-domain]  Cd Length: 283  Bit Score: 55.61  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195    9 LMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIE--NVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGeted 86
Cdd:TIGR01355  25 LPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEfpGLPLHHSIHAEQFLISHLALNGERG--LNDLAVSF---- 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 444280195   87 ylPPCNICRQVMVEFCEPDTLVFLLNGKGNILELRLEELVPYSFSS 132
Cdd:TIGR01355  99 --APCGHCRQFLNEIRNASSIKILLPDPHNKRDMSLQSYLPDRFGP 142
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
1-51 5.41e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 42.52  E-value: 5.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 444280195    1 MTVINKFVLMEQAKKVLKNAYFPYSKFPVGAAILFKDGKVITGANIENVSF 51
Cdd:pfam08211  28 LTLDDDDPLKQAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
PRK09027 PRK09027
cytidine deaminase; Provisional
 20-130 1.12e-04

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 40.20  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195  20 AYFPYSKFPVGAAILFKDGKVITGANIE--NVSFGVTNCAERSAIfygtSQGYRKGD--ILAIAVageteDYlPPCNICR 95
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEfaGAALQQTVHAEQSAI----SHAWLRGEkaIADITV-----NY-TPCGHCR 133

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 444280195  96 QVMVEFCEPDTLVFLLNGKGNileLRLEELVPYSF 130
Cdd:PRK09027 134 QFMNELNSASDLRIHLPGRQA---HTLHDYLPDAF 165
PRK08298 PRK08298
cytidine deaminase; Validated
 9-128 4.64e-04

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 37.86  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444280195   9 LMEQAKKVLKnayfpySKFPVG----AAILFKDGKVITGANIENVSFGVTNCAERSAIFYGTSQGYRKgdILAIAVAGET 84
Cdd:PRK08298   7 LYDVAKQLIE------QRYPNGwggaAAMRVEDGTILTSVAPEVINASTELCMETGAICEAHKLQKRV--THSICVAREN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 444280195  85 ED----YLPPCNICRQ--------VMVEFCEPDtlvfllnGKGNILELRLEELVPY 128
Cdd:PRK08298  79 EHselkVLSPCGVCQErlfywgpdVMCAVTNAD-------DPTDIIFKPLKELQPY 127
PRK09027 PRK09027
cytidine deaminase; Provisional
 20-51 1.03e-03

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 37.51  E-value: 1.03e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 444280195  20 AYFPYSKFPVGAAILFKDGKVITGANIENVSF 51
Cdd:PRK09027 203 SHAPYSQSYSGVALETKDGRIYTGRYAENAAF 234
 
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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