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Conserved domains on  [gi|116666976]
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Chain A, cytidine deaminase

Protein Classification

cytidine deaminase( domain architecture ID 10793656)

cytidine deaminase catalyzes the deamination of cytidine to uridine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12411 PRK12411
cytidine deaminase; Provisional
 10-141 2.33e-103

cytidine deaminase; Provisional


:

Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 291.10  E-value: 2.33e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  10 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 89
Cdd:PRK12411   1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116666976  90 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 141
Cdd:PRK12411  81 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 132
 
Name Accession Description Interval E-value
PRK12411 PRK12411
cytidine deaminase; Provisional
 10-141 2.33e-103

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 291.10  E-value: 2.33e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  10 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 89
Cdd:PRK12411   1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116666976  90 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 141
Cdd:PRK12411  81 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 132
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 10-139 5.37e-78

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: 226.57  E-value: 5.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  10 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 89
Cdd:COG0295    1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116666976  90 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 139
Cdd:COG0295   81 EPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 14-139 7.74e-60

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: 180.54  E-value: 7.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976   14 QLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRPVP 93
Cdd:TIGR01354   2 KLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSADDPVS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 116666976   94 PCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 139
Cdd:TIGR01354  82 PCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 16-127 2.80e-47

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: 148.26  E-value: 2.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  16 IQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRPVPPC 95
Cdd:cd01283    1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPC 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 116666976  96 GACRQVMVELCKQDTKVYLSNLHGDVQETTVG 127
Cdd:cd01283   81 GACRQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
13-106 9.94e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 80.42  E-value: 9.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976   13 KQLIQEAIEARKQAYvPYSKFQVGAALLTQDGKV-YRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTkrp 91
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVT--- 78

                          90
                  ....*....|....*
gi 116666976   92 VPPCGACRQVMVELC 106
Cdd:pfam00383  79 LEPCGMCAQAIIESG 93
 
Name Accession Description Interval E-value
PRK12411 PRK12411
cytidine deaminase; Provisional
 10-141 2.33e-103

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 291.10  E-value: 2.33e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  10 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 89
Cdd:PRK12411   1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116666976  90 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 141
Cdd:PRK12411  81 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 132
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 10-139 5.37e-78

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: 226.57  E-value: 5.37e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  10 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 89
Cdd:COG0295    1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116666976  90 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 139
Cdd:COG0295   81 EPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 10-139 5.80e-68

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 201.29  E-value: 5.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  10 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 89
Cdd:PRK05578   1 MDWKELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACVGETG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116666976  90 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 139
Cdd:PRK05578  81 EPLSPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 14-139 7.74e-60

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: 180.54  E-value: 7.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976   14 QLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRPVP 93
Cdd:TIGR01354   2 KLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSADDPVS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 116666976   94 PCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 139
Cdd:TIGR01354  82 PCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 16-127 2.80e-47

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: 148.26  E-value: 2.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  16 IQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRPVPPC 95
Cdd:cd01283    1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPC 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 116666976  96 GACRQVMVELCKQDTKVYLSNLHGDVQETTVG 127
Cdd:cd01283   81 GACRQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 16-114 4.40e-25

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: 91.46  E-value: 4.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  16 IQEAIEARKQAYVPYSKFQVGAALLTQ--DGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVadtkrpVP 93
Cdd:cd00786    1 MTEALKAADLGYAKESNFQVGACLVNKkdGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA------LS 74

                         90       100
                 ....*....|....*....|.
gi 116666976  94 PCGACRQVMVELCKQDTKVYL 114
Cdd:cd00786   75 PCGACAQLIIELGIKDVIVVL 95
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
13-106 9.94e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 80.42  E-value: 9.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976   13 KQLIQEAIEARKQAYvPYSKFQVGAALLTQDGKV-YRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTkrp 91
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVT--- 78

                          90
                  ....*....|....*
gi 116666976   92 VPPCGACRQVMVELC 106
Cdd:pfam00383  79 LEPCGMCAQAIIESG 93
PRK06848 PRK06848
cytidine deaminase;
13-131 2.81e-20

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 80.56  E-value: 2.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  13 KQLIQEAIEARKQAYvPYSKFQVGAALLTQDGKVYRGCNVEnASYG-LCNCAERTALFKAVSEGDKEFVAIAIVADTK-- 89
Cdd:PRK06848   8 YELIKAAEKVIEKRY-RNDWHHVGAALRTKTGRIYAAVHLE-AYVGrITVCAEAIAIGKAISEGDHEIDTIVAVRHPKph 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116666976  90 ------RPVPPCGACRQVMVELCKqDTKVYLSNlHGDVQETTVGELLP 131
Cdd:PRK06848  86 eddreiWVVSPCGACRELISDYGK-NTNVIVPY-NDELVKVNIMELLP 131
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
15-57 9.42e-11

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 55.23  E-value: 9.42e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 116666976   15 LIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASY 57
Cdd:pfam08211  36 LKQAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 22-139 1.86e-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: 57.15  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976   22 ARKQAYVPYSKFQVGAALLTQDGKVYRGCNVE--NASYGLCNCAERTALFKAVSEGDKEFVAIAIVAdtkrpvPPCGACR 99
Cdd:TIGR01355  32 AASYARAPISKFNVGAVGRGSSGRFYLGVNVEfpGLPLHHSIHAEQFLISHLALNGERGLNDLAVSF------APCGHCR 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 116666976  100 QVMVELC-KQDTKVYLSNLHGDvQETTVGELLPGAFLAEDL 139
Cdd:TIGR01355 106 QFLNEIRnASSIKILLPDPHNK-RDMSLQSYLPDRFGPDDL 145
PRK09027 PRK09027
cytidine deaminase; Provisional
 15-57 5.81e-08

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 49.83  E-value: 5.81e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 116666976  15 LIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASY 57
Cdd:PRK09027 192 LIQAALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAF 234
PLN02402 PLN02402
cytidine deaminase
 15-57 6.45e-07

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 47.17  E-value: 6.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 116666976  15 LIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASY 57
Cdd:PLN02402 195 LKNEALEAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAY 237
PRK09027 PRK09027
cytidine deaminase; Provisional
 26-139 9.09e-07

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 46.37  E-value: 9.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  26 AYVPYSKFQVGAALLTQDGKVYRGCNVE--NASYGLCNCAERTALFKAVSEGDKEFVAIaIVADTkrpvpPCGACRQVMV 103
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEfaGAALQQTVHAEQSAISHAWLRGEKAIADI-TVNYT-----PCGHCRQFMN 137

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 116666976 104 ELCKQDT-KVYLSnlhgDVQETTVGELLPGAFLAEDL 139
Cdd:PRK09027 138 ELNSASDlRIHLP----GRQAHTLHDYLPDAFGPKDL 170
PLN02182 PLN02182
cytidine deaminase
 26-131 1.18e-05

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 43.51  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  26 AYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNC--AERTALFKAVSEGDKEF--VAIAIVADTKRPVPPCGACRQV 101
Cdd:PLN02182  59 ARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSihAEQFLVTNLALNSEKDLceLAVAISTDGKEFGTPCGHCLQF 138

                         90       100       110
                 ....*....|....*....|....*....|.
gi 116666976 102 MVELCKQ-DTKVYLSNLHGDVQETTVGELLP 131
Cdd:PLN02182 139 LMEMSNAlDIKILSKPKHEAGSFSSLRHLLP 169
PLN02402 PLN02402
cytidine deaminase
 22-139 1.17e-03

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 37.54  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116666976  22 ARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNC--AERTALFKAVSEGDKEFVAIAIVAdtkrpvPPCGACR 99
Cdd:PLN02402  35 AQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSvhAEQFLITNLTLNAEPHLKYVAVSA------APCGHCR 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116666976 100 QVMVELCKQ-DTKVYLS----------NLHGDVQE-TTVGELLPGAFLAEDL 139
Cdd:PLN02402 109 QFFQEIRDApDIKILITgdsnsndsykNSLADSQQfEPLSCLLPHRFGPDDL 160
 
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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