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Conserved domains on  [gi|157822603|ref|NP_001102158|]
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cytidine deaminase [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 ...
 16-142 1.90e-64

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: 192.67  E-value: 1.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  16 QRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEF 95
Cdd:COG0295    4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157822603  96 ISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:COG0295   83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 16-142 1.90e-64

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: 192.67  E-value: 1.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  16 QRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEF 95
Cdd:COG0295    4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157822603  96 ISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:COG0295   83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 16-142 3.52e-62

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: 186.71  E-value: 3.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603   16 QRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADS-ADDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157822603   96 ISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
PRK05578 PRK05578
cytidine deaminase; Validated
 23-142 2.25e-57

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 174.71  E-value: 2.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  23 REAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIAsDLQEEFISPCGAC 102
Cdd:PRK05578  11 IEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPLSPCGRC 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157822603 103 RQVMREFGT-NWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:PRK05578  90 RQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 23-130 1.13e-41

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: 134.39  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  23 REAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGAC 102
Cdd:cd01283    5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                         90       100
                 ....*....|....*....|....*....
gi 157822603 103 RQVMREFG-TNWAVYMTKPDGTFVVRTVQ 130
Cdd:cd01283   84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-110 7.47e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 81.19  E-value: 7.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603   16 QRLLLSSREAKKSAYcPYSRFPVGAALLTGDGR-IFSGCNVENACYPLGVCAERTAIQKAISEGY-KDFRAIAIASDLqe 93
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
gi 157822603   94 efiSPCGACRQVMREFG 110
Cdd:pfam00383  80 ---EPCGMCAQAIIESG 93
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 16-142 1.90e-64

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: 192.67  E-value: 1.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  16 QRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEF 95
Cdd:COG0295    4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157822603  96 ISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:COG0295   83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 16-142 3.52e-62

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: 186.71  E-value: 3.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603   16 QRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADS-ADDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157822603   96 ISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
PRK05578 PRK05578
cytidine deaminase; Validated
 23-142 2.25e-57

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 174.71  E-value: 2.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  23 REAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIAsDLQEEFISPCGAC 102
Cdd:PRK05578  11 IEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPLSPCGRC 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157822603 103 RQVMREFGT-NWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:PRK05578  90 RQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 16-144 4.93e-45

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 143.56  E-value: 4.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  16 QRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDLQEEf 95
Cdd:PRK12411   4 KQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRP- 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157822603  96 ISPCGACRQVMREF-GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDLQK 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 1.13e-41

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: 134.39  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  23 REAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIASDlQEEFISPCGAC 102
Cdd:cd01283    5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                         90       100
                 ....*....|....*....|....*....
gi 157822603 103 RQVMREFG-TNWAVYMTKPDGTFVVRTVQ 130
Cdd:cd01283   84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
PRK06848 PRK06848
cytidine deaminase;
18-134 2.90e-22

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 85.95  E-value: 2.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  18 LLLSSREAKKSAYcPYSRFPVGAALLTGDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAI-AIASDLQEE-- 94
Cdd:PRK06848  10 LIKAAEKVIEKRY-RNDWHHVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDHEIDTIvAVRHPKPHEdd 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157822603  95 ----FISPCGACRQVMREFGTNWAVYMTKPDGTFVVrTVQELLP 134
Cdd:PRK06848  89 reiwVVSPCGACRELISDYGKNTNVIVPYNDELVKV-NIMELLP 131
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-110 7.47e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 81.19  E-value: 7.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603   16 QRLLLSSREAKKSAYcPYSRFPVGAALLTGDGR-IFSGCNVENACYPLGVCAERTAIQKAISEGY-KDFRAIAIASDLqe 93
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
gi 157822603   94 efiSPCGACRQVMREFG 110
Cdd:pfam00383  80 ---EPCGMCAQAIIESG 93
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 24-111 1.90e-16

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: 69.50  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  24 EAKKSAYCPYSRFPVGAALLT--GDGRIFSGCNVENACYPLGVCAERTAIQKAISEGYKDFRAIAIAsdlqeefISPCGA 101
Cdd:cd00786    6 KAADLGYAKESNFQVGACLVNkkDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA-------LSPCGA 78

                         90
                 ....*....|
gi 157822603 102 CRQVMREFGT 111
Cdd:cd00786   79 CAQLIIELGI 88
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 11-142 6.09e-14

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: 66.78  E-value: 6.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603   11 EPEHVQRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLG--VCAERTAIQKAISEGYKDFRAIAIA 88
Cdd:TIGR01355  18 GLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHhsIHAEQFLISHLALNGERGLNDLAVS 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822603   89 SDlqeefisPCGACRQVMREFGT--NWAVYMTKPDGTfVVRTVQELLPASFGPEDL 142
Cdd:TIGR01355  98 FA-------PCGHCRQFLNEIRNasSIKILLPDPHNK-RDMSLQSYLPDRFGPDDL 145
PLN02402 PLN02402
cytidine deaminase
 23-142 4.98e-09

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 53.33  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  23 REAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPL--GVCAERTAIQKAISEGYKDFRAIAIASdlqeefiSPCG 100
Cdd:PLN02402  33 KSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLhhSVHAEQFLITNLTLNAEPHLKYVAVSA-------APCG 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822603 101 ACRQVMREF-------------GTNWAVYMTKPDGTFVVRTVQELLPASFGPEDL 142
Cdd:PLN02402 106 HCRQFFQEIrdapdikilitgdSNSNDSYKNSLADSQQFEPLSCLLPHRFGPDDL 160
PRK09027 PRK09027
cytidine deaminase; Provisional
 29-143 1.92e-08

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 51.37  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  29 AYCPYSRFPVGAALLTGDGRIFSGCNVENACYPLG--VCAERTAIQKAISEGYKDFRAIAIASdlqeefiSPCGACRQVM 106
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQqtVHAEQSAISHAWLRGEKAIADITVNY-------TPCGHCRQFM 136

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157822603 107 REF--GTNWAVYMTKPDgtfvVRTVQELLPASFGPEDLQ 143
Cdd:PRK09027 137 NELnsASDLRIHLPGRQ----AHTLHDYLPDAFGPKDLN 171
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
24-60 3.04e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 46.37  E-value: 3.04e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 157822603   24 EAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACY 60
Cdd:pfam08211  42 AAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
PLN02182 PLN02182
cytidine deaminase
 23-134 7.07e-07

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 46.97  E-value: 7.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  23 REAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACYPL--GVCAERTAIQKAISEGYKDF--RAIAIASDlQEEFISP 98
Cdd:PLN02182  53 RKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLhhSIHAEQFLVTNLALNSEKDLceLAVAISTD-GKEFGTP 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157822603  99 CGACRQVMREFGTNWAV-YMTKPD---GTFvvRTVQELLP 134
Cdd:PLN02182 132 CGHCLQFLMEMSNALDIkILSKPKheaGSF--SSLRHLLP 169
PRK08298 PRK08298
cytidine deaminase; Validated
 35-134 2.56e-06

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 44.02  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822603  35 RFPVG----AALLTGDGRIFSGC--NVENACypLGVCAERTAIQKAISEGYKDFRAIAIASDLQEE---FISPCGACRQV 105
Cdd:PRK08298  18 RYPNGwggaAAMRVEDGTILTSVapEVINAS--TELCMETGAICEAHKLQKRVTHSICVARENEHSelkVLSPCGVCQER 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157822603 106 MREFGTNWAVYMTKPDG--TFVVRTVQELLP 134
Cdd:PRK08298  96 LFYWGPDVMCAVTNADDptDIIFKPLKELQP 126
PRK09027 PRK09027
cytidine deaminase; Provisional
 29-58 2.69e-04

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 39.43  E-value: 2.69e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 157822603  29 AYCPYSRFPVGAALLTGDGRIFSGCNVENA 58
Cdd:PRK09027 203 SHAPYSQSYSGVALETKDGRIYTGRYAENA 232
PLN02402 PLN02402
cytidine deaminase
 18-60 7.36e-04

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 38.31  E-value: 7.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 157822603  18 LLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNVENACY 60
Cdd:PLN02402 195 LKNEALEAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAY 237
 
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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