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Conserved domains on  [gi|1958777593|ref|XP_038966350|]
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cytidine deaminase isoform X1 [Rattus norvegicus]

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 ...
 11-101 2.92e-44

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: 139.90  E-value: 2.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQ 89
Cdd:COG0295    40 GCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEPVSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLS 118

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:COG0295   119 ELLPDAFGPEDL 130
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 11-101 2.92e-44

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: 139.90  E-value: 2.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQ 89
Cdd:COG0295    40 GCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEPVSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLS 118

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:COG0295   119 ELLPDAFGPEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 11-101 8.25e-43

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: 135.86  E-value: 8.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQ 89
Cdd:TIGR01354  37 GVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADS-ADDPVSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVG 115

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:TIGR01354 116 ELLPFGFGPSDL 127
PRK05578 PRK05578
cytidine deaminase; Validated
 11-101 7.66e-38

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 123.48  E-value: 7.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIAsDLQEEFISPCGACRQVMREFGT-NWAVYMTKPDGTFVVRTVQ 89
Cdd:PRK05578   40 GCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPLSPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLG 118

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:PRK05578  119 ELLPYAFTPDDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 11-89 6.61e-26

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: 92.79  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREFG-TNWAVYMTKPDGTFVVRTVQ 89
Cdd:cd01283    34 GVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGACRQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
11-69 1.67e-11

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 55.77  E-value: 1.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGY-KDFRAIAIASDLqeefiSPCGACRQVMREFG 69
Cdd:pfam00383  39 GYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-----EPCGMCAQAIIESG 93
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 11-101 2.92e-44

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: 139.90  E-value: 2.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQ 89
Cdd:COG0295    40 GCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEPVSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLS 118

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:COG0295   119 ELLPDAFGPEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 11-101 8.25e-43

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: 135.86  E-value: 8.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQ 89
Cdd:TIGR01354  37 GVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADS-ADDPVSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVG 115

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:TIGR01354 116 ELLPFGFGPSDL 127
PRK05578 PRK05578
cytidine deaminase; Validated
 11-101 7.66e-38

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 123.48  E-value: 7.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIAsDLQEEFISPCGACRQVMREFGT-NWAVYMTKPDGTFVVRTVQ 89
Cdd:PRK05578   40 GCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPLSPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLG 118

                          90
                  ....*....|..
gi 1958777593  90 ELLPASFGPEDL 101
Cdd:PRK05578  119 ELLPYAFTPDDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 10-103 2.13e-28

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 99.65  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  10 KGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDLQEEfISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTV 88
Cdd:PRK12411   39 RGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRP-VPPCGACRQVMVELcKQDTKVYLSNLHGDVQETTV 117

                          90
                  ....*....|....*
gi 1958777593  89 QELLPASFGPEDLQK 103
Cdd:PRK12411  118 GELLPGAFLAEDLHE 132
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 11-89 6.61e-26

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: 92.79  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGACRQVMREFG-TNWAVYMTKPDGTFVVRTVQ 89
Cdd:cd01283    34 GVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGACRQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
PRK06848 PRK06848
cytidine deaminase;
21-93 3.80e-14

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 63.61  E-value: 3.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  21 LGVCAERTAIQKAISEGYKDFRAI-AIASDLQEE------FISPCGACRQVMREFGTNWAVYMTKPDGTFVVrTVQELLP 93
Cdd:PRK06848   53 ITVCAEAIAIGKAISEGDHEIDTIvAVRHPKPHEddreiwVVSPCGACRELISDYGKNTNVIVPYNDELVKV-NIMELLP 131
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
11-69 1.67e-11

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 55.77  E-value: 1.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLGVCAERTAIQKAISEGY-KDFRAIAIASDLqeefiSPCGACRQVMREFG 69
Cdd:pfam00383  39 GYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-----EPCGMCAQAIIESG 93
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 10-70 1.44e-09

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: 50.63  E-value: 1.44e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777593  10 KGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIAsdlqeefISPCGACRQVMREFGT 70
Cdd:cd00786    35 RGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA-------LSPCGACAQLIIELGI 88
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 11-101 1.51e-06

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: 44.82  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLG--VCAERTAIQKAISEGYKDFRAIAIASDlqeefisPCGACRQVMREFGT--NWAVYMTKPDGTfVVR 86
Cdd:TIGR01355  59 GVNVEFPGLPLHhsIHAEQFLISHLALNGERGLNDLAVSFA-------PCGHCRQFLNEIRNasSIKILLPDPHNK-RDM 130

                          90
                  ....*....|....*
gi 1958777593  87 TVQELLPASFGPEDL 101
Cdd:TIGR01355 131 SLQSYLPDRFGPDDL 145
PRK09027 PRK09027
cytidine deaminase; Provisional
 11-102 1.28e-05

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 42.13  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777593  11 GCNVENACYPLG--VCAERTAIQKAISEGYKDFRAIAIASdlqeefiSPCGACRQVMREF--GTNWAVYMTKPDgtfvVR 86
Cdd:PRK09027   87 GANMEFAGAALQqtVHAEQSAISHAWLRGEKAIADITVNY-------TPCGHCRQFMNELnsASDLRIHLPGRQ----AH 155

                          90
                  ....*....|....*.
gi 1958777593  87 TVQELLPASFGPEDLQ 102
Cdd:PRK09027  156 TLHDYLPDAFGPKDLN 171
 
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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