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Conserved domains on  [gi|498435526|ref|WP_010741208|]
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MULTISPECIES: cytidine deaminase [Enterococcus]

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

 Zoom to residue level

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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 ...
 1-130 2.12e-72

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: 211.93  E-value: 2.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   1 MNKQEWIDIAVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTP 80
Cdd:COG0295    1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498435526  81 EPISPCGACRQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:COG0295   81 EPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 1-130 2.12e-72

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: 211.93  E-value: 2.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   1 MNKQEWIDIAVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTP 80
Cdd:COG0295    1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498435526  81 EPISPCGACRQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:COG0295   81 EPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 1-130 4.76e-66

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 195.90  E-value: 4.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   1 MNKQEWIDIAVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTP 80
Cdd:PRK05578   1 MDWKELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACVGETG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498435526  81 EPISPCGACRQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:PRK05578  81 EPLSPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 10-130 1.50e-56

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: 172.07  E-value: 1.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTPEPISPCGAC 89
Cdd:TIGR01354   7 AQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSADDPVSPCGAC 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 498435526   90 RQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:TIGR01354  87 RQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 10-118 1.22e-44

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: 141.32  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526  10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTPEPISPCGAC 89
Cdd:cd01283    4 ALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPCGAC 83

                         90       100
                 ....*....|....*....|....*....
gi 498435526  90 RQVMAEFCDPAMPVTLVGDNGVVKEMTVE 118
Cdd:cd01283   84 RQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
4-103 8.00e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 77.73  E-value: 8.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526    4 QEWIDIAVEALDKAYvPYSNFPVGACLVTKEGKT-YQGINIENASYGLTNCAERTAFFKAVSEGER-DFKHLVIAghtpE 81
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYDPTIHAERNAIRQAGKRGEGvRLEGATLY----V 77

                          90       100
                  ....*....|....*....|..
gi 498435526   82 PISPCGACRQVMAEFCDPAMPV 103
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRVVF 99
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 1-130 2.12e-72

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: 211.93  E-value: 2.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   1 MNKQEWIDIAVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTP 80
Cdd:COG0295    1 MDDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498435526  81 EPISPCGACRQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:COG0295   81 EPVSPCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 1-130 4.76e-66

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 195.90  E-value: 4.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   1 MNKQEWIDIAVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTP 80
Cdd:PRK05578   1 MDWKELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACVGETG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498435526  81 EPISPCGACRQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:PRK05578  81 EPLSPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 1-130 1.69e-57

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 174.38  E-value: 1.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   1 MNKQEWIDIAVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTP 80
Cdd:PRK12411   1 MNSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498435526  81 EPISPCGACRQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:PRK12411  81 RPVPPCGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 10-130 1.50e-56

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: 172.07  E-value: 1.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTPEPISPCGAC 89
Cdd:TIGR01354   7 AQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSADDPVSPCGAC 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 498435526   90 RQVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:TIGR01354  87 RQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 10-118 1.22e-44

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: 141.32  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526  10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAGHTPEPISPCGAC 89
Cdd:cd01283    4 ALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPCGAC 83

                         90       100
                 ....*....|....*....|....*....
gi 498435526  90 RQVMAEFCDPAMPVTLVGDNGVVKEMTVE 118
Cdd:cd01283   84 RQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 7-97 4.61e-21

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: 81.06  E-value: 4.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   7 IDIAVEALDKAYVPYSNFPVGACLVTKEG--KTYQGINIENASYGLTNCAERTAFFKAVSEGERDFKHLVIAghtpepIS 84
Cdd:cd00786    1 MTEALKAADLGYAKESNFQVGACLVNKKDggKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA------LS 74

                         90
                 ....*....|...
gi 498435526  85 PCGACRQVMAEFC 97
Cdd:cd00786   75 PCGACAQLIIELG 87
PRK06848 PRK06848
cytidine deaminase;
5-126 1.45e-20

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 80.94  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   5 EWIDIAVEALDKAYvPYSNFPVGACLVTKEGKTYQGINIEnASYG-LTNCAERTAFFKAVSEGERDFKHLVIAGHtPEP- 82
Cdd:PRK06848   9 ELIKAAEKVIEKRY-RNDWHHVGAALRTKTGRIYAAVHLE-AYVGrITVCAEAIAIGKAISEGDHEIDTIVAVRH-PKPh 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498435526  83 --------ISPCGACRQVMAEFCDPAMpVTLVGDNGVVKeMTVEGLLPYTFT 126
Cdd:PRK06848  86 eddreiwvVSPCGACRELISDYGKNTN-VIVPYNDELVK-VNIMELLPNKYT 135
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
4-103 8.00e-20

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 77.73  E-value: 8.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526    4 QEWIDIAVEALDKAYvPYSNFPVGACLVTKEGKT-YQGINIENASYGLTNCAERTAFFKAVSEGER-DFKHLVIAghtpE 81
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYDPTIHAERNAIRQAGKRGEGvRLEGATLY----V 77

                          90       100
                  ....*....|....*....|..
gi 498435526   82 PISPCGACRQVMAEFCDPAMPV 103
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRVVF 99
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 13-130 1.48e-12

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: 62.54  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526   13 ALDKAYVPYSNFPVGACLVTKEGKTYQGINIE--NASYGLTNCAERTAFFKAVSEGERDFKHLVIAGhtpepiSPCGACR 90
Cdd:TIGR01355  32 AASYARAPISKFNVGAVGRGSSGRFYLGVNVEfpGLPLHHSIHAEQFLISHLALNGERGLNDLAVSF------APCGHCR 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 498435526   91 QVMAEFCDPAMPVTLVGDNGVVKEMTVEGLLPYTFTDKDL 130
Cdd:TIGR01355 106 QFLNEIRNASSIKILLPDPHNKRDMSLQSYLPDRFGPDDL 145
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-48 8.49e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 44.83  E-value: 8.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 498435526   10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASY 48
Cdd:pfam08211  40 ALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
PLN02402 PLN02402
cytidine deaminase
 10-48 5.97e-06

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 43.70  E-value: 5.97e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 498435526  10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASY 48
Cdd:PLN02402 199 ALEAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAY 237
PRK09027 PRK09027
cytidine deaminase; Provisional
 17-130 1.33e-05

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 42.90  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526  17 AYVPYSNFPVGACLVTKEGKTYQGINIE--NASYGLTNCAERTAFFKAVSEGERDFKHLVIAghtpepISPCGACRQVMA 94
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEfaGAALQQTVHAEQSAISHAWLRGEKAIADITVN------YTPCGHCRQFMN 137

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 498435526  95 EFCD-PAMPVTLVGDngvvKEMTVEGLLPYTFTDKDL 130
Cdd:PRK09027 138 ELNSaSDLRIHLPGR----QAHTLHDYLPDAFGPKDL 170
PRK09027 PRK09027
cytidine deaminase; Provisional
 10-48 5.48e-04

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 38.28  E-value: 5.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 498435526  10 AVEALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASY 48
Cdd:PRK09027 196 ALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAF 234
PLN02402 PLN02402
cytidine deaminase
 17-109 1.69e-03

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 36.77  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526  17 AYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNC--AERTAFFKAVSEGERDFKHLVIAGhtpepiSPCGACRQVMA 94
Cdd:PLN02402  39 ARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSvhAEQFLITNLTLNAEPHLKYVAVSA------APCGHCRQFFQ 112

                         90
                 ....*....|....*.
gi 498435526  95 EFCD-PAMPVTLVGDN 109
Cdd:PLN02402 113 EIRDaPDIKILITGDS 128
PLN02182 PLN02182
cytidine deaminase
 12-98 2.18e-03

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 36.57  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498435526  12 EALDKAYVPYSNFPVGACLVTKEGKTYQGINIENASYGLTNC--AERTAFFKAVSEGERDFKHLVIAGHTP--EPISPCG 87
Cdd:PLN02182  54 KAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSihAEQFLVTNLALNSEKDLCELAVAISTDgkEFGTPCG 133

                         90
                 ....*....|.
gi 498435526  88 ACRQVMAEFCD 98
Cdd:PLN02182 134 HCLQFLMEMSN 144
 
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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