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Conserved domains on  [gi|1144518473|gb|ONV68993|]
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cytidine deaminase [Burkholderia cenocepacia]

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 ...
 1-127 3.30e-67

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: 198.84  E-value: 3.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   1 MERDELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGD 80
Cdd:COG0295     1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGER--EIKAIAVVAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1144518473  81 TDGPIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAF 127
Cdd:COG0295    79 TGEPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAF 125
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 1-127 3.30e-67

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: 198.84  E-value: 3.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   1 MERDELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGD 80
Cdd:COG0295     1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGER--EIKAIAVVAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1144518473  81 TDGPIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAF 127
Cdd:COG0295    79 TGEPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAF 125
PRK12411 PRK12411
cytidine deaminase; Provisional
 1-128 6.87e-61

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 183.24  E-value: 6.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   1 MERDELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGD 80
Cdd:PRK12411    1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDK--EFVAIAIVAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1144518473  81 TDGPIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAFM 128
Cdd:PRK12411   79 TKRPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFL 126
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 4-127 3.87e-52

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: 160.51  E-value: 3.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   4 DELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGDTDG 83
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1144518473  84 PIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAF 127
Cdd:TIGR01354  79 PVSPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGF 122
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 7-118 4.30e-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: 132.08  E-value: 4.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   7 IEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGDTDGPIA 86
Cdd:cd01283     1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLR--RYLVTWAVSDEGGVWS 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1144518473  87 PCGACRQVIIEIGKPDIEVILTNLKGAVEITT 118
Cdd:cd01283    79 PCGACRQVLAEFLPSRLYIIIDNPKGEEFAYT 110
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
5-103 1.40e-16

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 69.64  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   5 ELIEQAKAARERAYaPYSRFKVGAAL-QARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRPGDFARLAVVgdtdg 83
Cdd:pfam00383   4 YFMRLALKAAKRAY-PYSNFPVGAVIvKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYV----- 77

                          90       100
                  ....*....|....*....|
gi 1144518473  84 PIAPCGACRQVIIEIGKPDI 103
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRV 97
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 1-127 3.30e-67

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: 198.84  E-value: 3.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   1 MERDELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGD 80
Cdd:COG0295     1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGER--EIKAIAVVAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1144518473  81 TDGPIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAF 127
Cdd:COG0295    79 TGEPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAF 125
PRK12411 PRK12411
cytidine deaminase; Provisional
 1-128 6.87e-61

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 183.24  E-value: 6.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   1 MERDELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGD 80
Cdd:PRK12411    1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDK--EFVAIAIVAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1144518473  81 TDGPIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAFM 128
Cdd:PRK12411   79 TKRPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFL 126
PRK05578 PRK05578
cytidine deaminase; Validated
 1-127 3.12e-55

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 168.55  E-value: 3.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   1 MERDELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYrpGDFARLAVVGD 80
Cdd:PRK05578    1 MDWKELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGG--GRLVAIACVGE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1144518473  81 TDGPIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAF 127
Cdd:PRK05578   79 TGEPLSPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAF 125
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 4-127 3.87e-52

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: 160.51  E-value: 3.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   4 DELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGDTDG 83
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1144518473  84 PIAPCGACRQVIIEIGKPDIEVILTNLKGAVEITTARALLPGAF 127
Cdd:TIGR01354  79 PVSPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGF 122
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 7-118 4.30e-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: 132.08  E-value: 4.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   7 IEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGDTDGPIA 86
Cdd:cd01283     1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLR--RYLVTWAVSDEGGVWS 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1144518473  87 PCGACRQVIIEIGKPDIEVILTNLKGAVEITT 118
Cdd:cd01283    79 PCGACRQVLAEFLPSRLYIIIDNPKGEEFAYT 110
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
5-103 1.40e-16

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 69.64  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   5 ELIEQAKAARERAYaPYSRFKVGAAL-QARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRPGDFARLAVVgdtdg 83
Cdd:pfam00383   4 YFMRLALKAAKRAY-PYSNFPVGAVIvKKDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYV----- 77

                          90       100
                  ....*....|....*....|
gi 1144518473  84 PIAPCGACRQVIIEIGKPDI 103
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRV 97
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 7-108 3.35e-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: 68.35  E-value: 3.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   7 IEQAKAARERAYAPYSRFKVGAAL--QARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGyrPGDFARLAVVgdtdgp 84
Cdd:cd00786     1 MTEALKAADLGYAKESNFQVGACLvnKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEG--DTKGQMLYVA------ 72

                          90       100
                  ....*....|....*....|....
gi 1144518473  85 IAPCGACRQVIIEIGKPDIEVILT 108
Cdd:cd00786    73 LSPCGACAQLIIELGIKDVIVVLT 96
PRK06848 PRK06848
cytidine deaminase;
5-124 9.62e-12

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 58.22  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   5 ELIEQAKAARERAYAPySRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRpgDFARLAVV-----G 79
Cdd:PRK06848    9 ELIKAAEKVIEKRYRN-DWHHVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDH--EIDTIVAVrhpkpH 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1144518473  80 DTDGPIA---PCGACRQVIIEIGkPDIEVILTNlKGAVEITTARALLP 124
Cdd:PRK06848   86 EDDREIWvvsPCGACRELISDYG-KNTNVIVPY-NDELVKVNIMELLP 131
PRK09027 PRK09027
cytidine deaminase; Provisional
 4-90 7.87e-09

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 52.14  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   4 DELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRPGDFARLAVVGDTDG 83
Cdd:PRK09027  190 DPLIQAALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAFNPSLPPLQGALNLLNLSGEDFSDIQRAVLVEKADA 269


                  ....*..
gi 1144518473  84 PIAPCGA 90
Cdd:PRK09027  270 KLSQWDA 276
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 13-127 3.09e-08

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: 50.21  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473  13 ARERAYAPYSRFKVGAALQARDGTVFHGCNVE--NASYGLCNCAERTALFAAIAAGYRpgDFARLAVVGdtdgpiAPCGA 90
Cdd:TIGR01355  32 AASYARAPISKFNVGAVGRGSSGRFYLGVNVEfpGLPLHHSIHAEQFLISHLALNGER--GLNDLAVSF------APCGH 103

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1144518473  91 CRQVIIEI-GKPDIEVILTNlKGAVEITTARALLPGAF 127
Cdd:TIGR01355 104 CRQFLNEIrNASSIKILLPD-PHNKRDMSLQSYLPDRF 140
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
4-85 4.08e-08

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 48.30  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473   4 DELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRPGDFARLAVVGDTDG 83
Cdd:pfam08211  34 DPLKQAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAFNPSLPPLQAALVDFVAGGKDFEDIVRAVLVEKEDA 113


                  ..
gi 1144518473  84 PI 85
Cdd:pfam08211 114 KV 115
PLN02182 PLN02182
cytidine deaminase
 11-124 4.72e-07

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 46.97  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144518473  11 KAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGYRPGDFARLAVVGDTDGPI--APC 88
Cdd:PLN02182   53 RKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFLVTNLALNSEKDLCELAVAISTDGKEfgTPC 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1144518473  89 GACRQVIIEIGKP-DIEVILTNLKGAVEITTARALLP 124
Cdd:PLN02182  133 GHCLQFLMEMSNAlDIKILSKPKHEAGSFSSLRHLLP 169
PLN02402 PLN02402
cytidine deaminase
 4-75 1.80e-04

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 39.46  E-value: 1.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1144518473   4 DELIEQAKAARERAYAPYSRFKVGAALQARDGTVFHGCNVENASYGLCNCAERTALFAAIAAGyRPGDFARL 75
Cdd:PLN02402  193 DDLKNEALEAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAYNPSMGPVQAALVAYVAGG-RGGGYERI 263
 
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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