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Conserved domains on  [gi|38492430|pdb|1MQ0|A]
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Chain A, Cytidine Deaminase

Protein Classification

cytidine deaminase( domain architecture ID 11492267)

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
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 10-136 2.89e-69

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: 204.43  E-value: 2.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         10 QQLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 89
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
1MQ0_A         90 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
 
Name Accession Description Interval E-value
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 10-136 2.89e-69

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: 204.43  E-value: 2.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         10 QQLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 89
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
1MQ0_A         90 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 10-136 6.24e-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: 198.45  E-value: 6.24e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A       10 QQLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDF 89
Cdd:COG0295   4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1MQ0_A       90 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:COG0295  83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 11-136 7.93e-59

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 178.18  E-value: 7.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        11 QLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIAsDMQDDFI 90
Cdd:PRK05578   5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
1MQ0_A        91 SPCGACRQVMREFGT-NWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:PRK05578  84 SPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 17-124 1.82e-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: 1.82e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A       17 QEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDFISPCGAC 96
Cdd:cd01283   5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                        90       100
                ....*....|....*....|....*....
1MQ0_A       97 RQVMREFG-TNWPVYMTKPDGTYIVMTVQ 124
Cdd:cd01283  84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-104 9.56e-23

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 85.82  E-value: 9.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         10 QQLLVCSQEAKQSAYcPYSHFPVGAALLTQEGR-IFKGCNIENACYPLGICAERTAIQKAVSEGY-KDFRAIAIASDMqd 87
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
1MQ0_A         88 dfiSPCGACRQVMREFG 104
Cdd:pfam00383  80 ---EPCGMCAQAIIESG 93
 
Name Accession Description Interval E-value
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 10-136 2.89e-69

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: 204.43  E-value: 2.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         10 QQLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 89
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
1MQ0_A         90 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 10-136 6.24e-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: 198.45  E-value: 6.24e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A       10 QQLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDF 89
Cdd:COG0295   4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1MQ0_A       90 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:COG0295  83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 11-136 7.93e-59

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 178.18  E-value: 7.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        11 QLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIAsDMQDDFI 90
Cdd:PRK05578   5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
1MQ0_A        91 SPCGACRQVMREFGT-NWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:PRK05578  84 SPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 10-138 8.76e-47

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 147.80  E-value: 8.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        10 QQLLVCSQEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDF 89
Cdd:PRK12411   4 KQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVAD-TKRP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
1MQ0_A        90 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQK 138
Cdd:PRK12411  83 VPPCGACRQVMVELcKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 132
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 17-124 1.82e-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: 1.82e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A       17 QEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDFISPCGAC 96
Cdd:cd01283   5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                        90       100
                ....*....|....*....|....*....
1MQ0_A       97 RQVMREFG-TNWPVYMTKPDGTYIVMTVQ 124
Cdd:cd01283  84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
10-104 9.56e-23

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 85.82  E-value: 9.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         10 QQLLVCSQEAKQSAYcPYSHFPVGAALLTQEGR-IFKGCNIENACYPLGICAERTAIQKAVSEGY-KDFRAIAIASDMqd 87
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
1MQ0_A         88 dfiSPCGACRQVMREFG 104
Cdd:pfam00383  80 ---EPCGMCAQAIIESG 93
PRK06848 PRK06848
cytidine deaminase;
11-128 3.02e-21

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 82.87  E-value: 3.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        11 QLLVCSQEAKQSAYCPYSHfPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAI-AIASDMQDD- 88
Cdd:PRK06848   9 ELIKAAEKVIEKRYRNDWH-HVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDHEIDTIvAVRHPKPHEd 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
1MQ0_A        89 -----FISPCGACRQVMREFGTNWPVYMTKPDGTyIVMTVQELLP 128
Cdd:PRK06848  88 dreiwVVSPCGACRELISDYGKNTNVIVPYNDEL-VKVNIMELLP 131
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 18-111 4.12e-17

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: 71.04  E-value: 4.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A       18 EAKQSAYcPYSHFPVGAALLTQEG--RIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIAsdmqddfISPCGA 95
Cdd:cd00786   7 AADLGYA-KESNFQVGACLVNKKDggKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA-------LSPCGA 78

                        90
                ....*....|....*.
1MQ0_A       96 CRQVMREFGTNWPVYM 111
Cdd:cd00786  79 CAQLIIELGIKDVIVV 94
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 19-136 8.25e-15

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: 69.09  E-value: 8.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         19 AKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLG--ICAERTAIQKAVSEGYKDFRAIAIASDmqddfisPCGAC 96
Cdd:TIGR01355  32 AASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHhsIHAEQFLISHLALNGERGLNDLAVSFA-------PCGHC 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
1MQ0_A         97 RQVMREFgTNWP---VYMTKPDGTYiVMTVQELLPSSFGPEDL 136
Cdd:TIGR01355 105 RQFLNEI-RNASsikILLPDPHNKR-DMSLQSYLPDRFGPDDL 145
PRK09027 PRK09027
cytidine deaminase; Provisional
 23-137 8.56e-11

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 57.92  E-value: 8.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        23 AYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLG--ICAERTAIQKAVSEGYKDFRAIAIASdmqddfiSPCGACRQVM 100
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQqtVHAEQSAISHAWLRGEKAIADITVNY-------TPCGHCRQFM 136

                         90       100       110
                 ....*....|....*....|....*....|....*....
1MQ0_A       101 REF--GTNWPVYMTKPDgtyiVMTVQELLPSSFGPEDLQ 137
Cdd:PRK09027 137 NELnsASDLRIHLPGRQ----AHTLHDYLPDAFGPKDLN 171
PLN02402 PLN02402
cytidine deaminase
 9-136 1.33e-08

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 51.79  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A         9 VQQLLVCSQEAKQS-AYCPYSHFPVGAALLTQEGRIFKGCNIENACYPL--GICAERTAIQKAVSEGYKDFRAIAIASdm 85
Cdd:PLN02402  24 VLQLLPSLVKSAQSlARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLhhSVHAEQFLITNLTLNAEPHLKYVAVSA-- 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
1MQ0_A        86 qddfiSPCGACRQVMREF-------------GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 136
Cdd:PLN02402 102 -----APCGHCRQFFQEIrdapdikilitgdSNSNDSYKNSLADSQQFEPLSCLLPHRFGPDDL 160
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
19-54 4.27e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 45.60  E-value: 4.27e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
1MQ0_A         19 AKQSaYCPYSHFPVGAALLTQEGRIFKGCNIENACY 54
Cdd:pfam08211  44 ANRS-YAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
PRK08298 PRK08298
cytidine deaminase; Validated
 29-128 1.23e-05

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 42.09  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        29 HFPVG----AALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDD---FISPCGACRQVMR 101
Cdd:PRK08298  18 RYPNGwggaAAMRVEDGTILTSVAPEVINASTELCMETGAICEAHKLQKRVTHSICVARENEHSelkVLSPCGVCQERLF 97

                         90       100
                 ....*....|....*....|....*....
1MQ0_A       102 EFGTNWPVYMTKPDG--TYIVMTVQELLP 128
Cdd:PRK08298  98 YWGPDVMCAVTNADDptDIIFKPLKELQP 126
PLN02182 PLN02182
cytidine deaminase
 17-114 1.69e-05

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 43.12  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MQ0_A        17 QEAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPL--GICAERTAIQKAVSEGYKDF--RAIAIASDMQdDFISP 92
Cdd:PLN02182  53 RKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLhhSIHAEQFLVTNLALNSEKDLceLAVAISTDGK-EFGTP 131

                         90       100
                 ....*....|....*....|...
1MQ0_A        93 CGACRQVMREFGTNWPV-YMTKP 114
Cdd:PLN02182 132 CGHCLQFLMEMSNALDIkILSKP 154
PLN02402 PLN02402
cytidine deaminase
 18-54 1.81e-04

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 39.85  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
1MQ0_A        18 EAKQSAYCPYSHFPVGAALLTQEGRIFKGCNIENACY 54
Cdd:PLN02402 201 EAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAY 237
PRK09027 PRK09027
cytidine deaminase; Provisional
 9-52 4.45e-04

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 38.66  E-value: 4.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
1MQ0_A         9 VQQLLvcsQEAKQSaYCPYSHFPVGAALLTQEGRIFKGCNIENA 52
Cdd:PRK09027 193 IQAAL---DAANRS-HAPYSQSYSGVALETKDGRIYTGRYAENA 232
 
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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