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Conserved domains on  [gi|11386157|ref|NP_001776|]
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cytidine deaminase [Homo sapiens]

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 ...
 16-142 1.44e-68

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: 202.88  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157    16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 11386157    96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
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 ...
 16-142 1.44e-68

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: 202.88  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157    16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 11386157    96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 16-142 1.92e-66

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: 197.68  E-value: 1.92e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDF 95
Cdd:COG0295   4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 11386157  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:COG0295  83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 17-142 2.02e-58

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 177.41  E-value: 2.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   17 QLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIAsDMQDDFI 96
Cdd:PRK05578   5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 11386157   97 SPCGACRQVMREFGT-NWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:PRK05578  84 SPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 23-130 8.54e-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: 139.78  E-value: 8.54e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157  23 QEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDFISPCGAC 102
Cdd:cd01283   5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                        90       100
                ....*....|....*....|....*....
gi 11386157 103 RQVMREFG-TNWPVYMTKPDGTYIVMTVQ 130
Cdd:cd01283  84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-110 2.59e-22

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 84.66  E-value: 2.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157    16 QQLLVCSQEAKKSAYcPYSHFPVGAALLTQEGR-IFKGCNIENACYPLGICAERTAIQKAVSEGY-KDFRAIAIASDMqd 93
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
gi 11386157    94 dfiSPCGACRQVMREFG 110
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 ...
 16-142 1.44e-68

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: 202.88  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157    16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 11386157    96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 16-142 1.92e-66

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: 197.68  E-value: 1.92e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDF 95
Cdd:COG0295   4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 11386157  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:COG0295  83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 17-142 2.02e-58

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 177.41  E-value: 2.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   17 QLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIAsDMQDDFI 96
Cdd:PRK05578   5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 11386157   97 SPCGACRQVMREFGT-NWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:PRK05578  84 SPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 16-144 1.66e-46

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 147.42  E-value: 1.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMqDDF 95
Cdd:PRK12411   4 KQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADT-KRP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 11386157   96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQK 144
Cdd:PRK12411  83 VPPCGACRQVMVELcKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDLHE 132
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 23-130 8.54e-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: 139.78  E-value: 8.54e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157  23 QEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDmQDDFISPCGAC 102
Cdd:cd01283   5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                        90       100
                ....*....|....*....|....*....
gi 11386157 103 RQVMREFG-TNWPVYMTKPDGTYIVMTVQ 130
Cdd:cd01283  84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-110 2.59e-22

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 84.66  E-value: 2.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157    16 QQLLVCSQEAKKSAYcPYSHFPVGAALLTQEGR-IFKGCNIENACYPLGICAERTAIQKAVSEGY-KDFRAIAIASDMqd 93
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
gi 11386157    94 dfiSPCGACRQVMREFG 110
Cdd:pfam00383  80 ---EPCGMCAQAIIESG 93
PRK06848 PRK06848
cytidine deaminase;
17-134 2.04e-21

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 83.64  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   17 QLLVCSQEAKKSAYCPYSHfPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAI-AIASDMQDD- 94
Cdd:PRK06848   9 ELIKAAEKVIEKRYRNDWH-HVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDHEIDTIvAVRHPKPHEd 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 11386157   95 -----FISPCGACRQVMREFGTNWPVYMTKPDGTyIVMTVQELLP 134
Cdd:PRK06848  88 dreiwVVSPCGACRELISDYGKNTNVIVPYNDEL-VKVNIMELLP 131
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 24-117 5.55e-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: 5.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157  24 EAKKSAYCPYSHFPVGAALLTQEG--RIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIAsdmqddfISPCGA 101
Cdd:cd00786   6 KAADLGYAKESNFQVGACLVNKKDggKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA-------LSPCGA 78

                        90
                ....*....|....*.
gi 11386157 102 CRQVMREFGTNWPVYM 117
Cdd:cd00786  79 CAQLIIELGIKDVIVV 94
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 6-142 8.22e-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: 8.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157     6 PACTLKPECVQQLLVCSQ------------EAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLG--ICAERTAI 71
Cdd:TIGR01355   1 PKFVFTAEQAQSLGTLSGltdpkllpklipKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHhsIHAEQFLI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11386157    72 QKAVSEGYKDFRAIAIASDmqddfisPCGACRQVMREFgTNWP---VYMTKPDGTYiVMTVQELLPSSFGPEDL 142
Cdd:TIGR01355  81 SHLALNGERGLNDLAVSFA-------PCGHCRQFLNEI-RNASsikILLPDPHNKR-DMSLQSYLPDRFGPDDL 145
PRK09027 PRK09027
cytidine deaminase; Provisional
 29-143 9.41e-11

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 57.92  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   29 AYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLG--ICAERTAIQKAVSEGYKDFRAIAIASdmqddfiSPCGACRQVM 106
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQqtVHAEQSAISHAWLRGEKAIADITVNY-------TPCGHCRQFM 136

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 11386157  107 REF--GTNWPVYMTKPDgtyiVMTVQELLPSSFGPEDLQ 143
Cdd:PRK09027 137 NELnsASDLRIHLPGRQ----AHTLHDYLPDAFGPKDLN 171
PLN02402 PLN02402
cytidine deaminase
 15-142 8.58e-09

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 52.56  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   15 VQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPL--GICAERTAIQKAVSEGYKDFRAIAIASdmq 92
Cdd:PLN02402  25 LQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLhhSVHAEQFLITNLTLNAEPHLKYVAVSA--- 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11386157   93 ddfiSPCGACRQVMREF-------------GTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDL 142
Cdd:PLN02402 102 ----APCGHCRQFFQEIrdapdikilitgdSNSNDSYKNSLADSQQFEPLSCLLPHRFGPDDL 160
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
24-60 3.67e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 45.99  E-value: 3.67e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 11386157    24 EAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACY 60
Cdd:pfam08211  42 AAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
PRK08298 PRK08298
cytidine deaminase; Validated
 35-134 1.98e-05

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 41.71  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   35 HFPVG----AALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDD---FISPCGACRQVMR 107
Cdd:PRK08298  18 RYPNGwggaAAMRVEDGTILTSVAPEVINASTELCMETGAICEAHKLQKRVTHSICVARENEHSelkVLSPCGVCQERLF 97

                         90       100
                 ....*....|....*....|....*....
gi 11386157  108 EFGTNWPVYMTKPDG--TYIVMTVQELLP 134
Cdd:PRK08298  98 YWGPDVMCAVTNADDptDIIFKPLKELQP 126
PLN02182 PLN02182
cytidine deaminase
 23-120 2.69e-05

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 42.35  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11386157   23 QEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPL--GICAERTAIQKAVSEGYKDF--RAIAIASDMQdDFISP 98
Cdd:PLN02182  53 RKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLhhSIHAEQFLVTNLALNSEKDLceLAVAISTDGK-EFGTP 131

                         90       100
                 ....*....|....*....|...
gi 11386157   99 CGACRQVMREFGTNWPV-YMTKP 120
Cdd:PLN02182 132 CGHCLQFLMEMSNALDIkILSKP 154
PLN02402 PLN02402
cytidine deaminase
 24-60 1.02e-04

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 40.62  E-value: 1.02e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 11386157   24 EAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACY 60
Cdd:PLN02402 201 EAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAY 237
PRK09027 PRK09027
cytidine deaminase; Provisional
 15-58 1.26e-03

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 37.51  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 11386157   15 VQQLLvcsqEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENA 58
Cdd:PRK09027 193 IQAAL----DAANRSHAPYSQSYSGVALETKDGRIYTGRYAENA 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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