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Conserved domains on  [gi|1622834521|ref|XP_001096632|]
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cytidine deaminase isoform X1 [Macaca mulatta]

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 1.32e-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: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDMqDDF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622834521  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 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 1.32e-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: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDMqDDF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622834521  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 142
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 16-142 1.12e-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: 198.07  E-value: 1.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDmQDDF 95
Cdd:COG0295     4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622834521  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 142
Cdd:COG0295    83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 17-142 6.82e-59

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 178.57  E-value: 6.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  17 QLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIAsDMQDDFI 96
Cdd:PRK05578    5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834521  97 SPCGACRQVMREFGT-NWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 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 8.73e-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: 8.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  23 QEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDmQDDFISPCGAC 102
Cdd:cd01283     5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                          90       100
                  ....*....|....*....|....*....
gi 1622834521 103 RQVMREFG-TNWPVYMTKPDGTYVVMTVQ 130
Cdd:cd01283    84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-110 6.82e-23

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 86.20  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYcPYSHFPVGAALLTQEGR-IFKGCNIENACYPLGICAERTAIQKAVSEGY-KDFKAIAIASDMqd 93
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
gi 1622834521  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 1.32e-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: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDMqDDF 95
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSA-DDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622834521  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 142
Cdd:TIGR01354  80 VSPCGACRQVLAEFaGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 16-142 1.12e-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: 198.07  E-value: 1.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDmQDDF 95
Cdd:COG0295     4 EELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVAD-TGEP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622834521  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 142
Cdd:COG0295    83 VSPCGACRQVLAEFaGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 17-142 6.82e-59

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 178.57  E-value: 6.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  17 QLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIAsDMQDDFI 96
Cdd:PRK05578    5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACV-GETGEPL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834521  97 SPCGACRQVMREFGT-NWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 142
Cdd:PRK05578   84 SPCGRCRQVLAEFGGpDLLVTLVAKDGPTGEMTLGELLPYAFTPDDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 16-144 2.41e-46

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 147.03  E-value: 2.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDMqDDF 95
Cdd:PRK12411    4 KQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADT-KRP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622834521  96 ISPCGACRQVMREF-GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDLQK 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 8.73e-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: 8.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  23 QEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDmQDDFISPCGAC 102
Cdd:cd01283     5 LAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSD-EGGVWSPCGAC 83

                          90       100
                  ....*....|....*....|....*....
gi 1622834521 103 RQVMREFG-TNWPVYMTKPDGTYVVMTVQ 130
Cdd:cd01283    84 RQVLAEFLpSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-110 6.82e-23

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 86.20  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  16 QQLLVCSQEAKKSAYcPYSHFPVGAALLTQEGR-IFKGCNIENACYPLGICAERTAIQKAVSEGY-KDFKAIAIASDMqd 93
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEiIATGYNGENAGYDPTIHAERNAIRQAGKRGEgVRLEGATLYVTL-- 79

                          90
                  ....*....|....*..
gi 1622834521  94 dfiSPCGACRQVMREFG 110
Cdd:pfam00383  80 ---EPCGMCAQAIIESG 93
PRK06848 PRK06848
cytidine deaminase;
17-134 8.53e-22

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 84.79  E-value: 8.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  17 QLLVCSQEAKKSAYCPYSHfPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAI-AIASDMQDD- 94
Cdd:PRK06848    9 ELIKAAEKVIEKRYRNDWH-HVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDHEIDTIvAVRHPKPHEd 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622834521  95 -----FISPCGACRQVMREFGTNWPVYMTKPDGTyVVMTVQELLP 134
Cdd:PRK06848   88 dreiwVVSPCGACRELISDYGKNTNVIVPYNDEL-VKVNIMELLP 131
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 24-117 6.45e-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: 6.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  24 EAKKSAYCPYSHFPVGAALLTQEG--RIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIAsdmqddfISPCGA 101
Cdd:cd00786     6 KAADLGYAKESNFQVGACLVNKKDggKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVA-------LSPCGA 78

                          90
                  ....*....|....*.
gi 1622834521 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 6.57e-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: 69.47  E-value: 6.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521   6 PACTLQPECVQQLLVCSQ------------EAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLG--ICAERTAI 71
Cdd:TIGR01355   1 PKFVFTAEQAQSLGTLSGltdpkllpklipKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHhsIHAEQFLI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834521  72 QKAVSEGYKDFKAIAIASDmqddfisPCGACRQVMREFgTNWP---VYMTKPDGTyVVMTVQELLPSSFGPEDL 142
Cdd:TIGR01355  81 SHLALNGERGLNDLAVSFA-------PCGHCRQFLNEI-RNASsikILLPDPHNK-RDMSLQSYLPDRFGPDDL 145
PRK09027 PRK09027
cytidine deaminase; Provisional
 29-143 2.50e-10

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 56.77  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  29 AYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLG--ICAERTAIQKAVSEGYKDFKAIAIASdmqddfiSPCGACRQVM 106
Cdd:PRK09027   64 AVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQqtVHAEQSAISHAWLRGEKAIADITVNY-------TPCGHCRQFM 136

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622834521 107 REF--GTNWPVYMTKPDgtyvVMTVQELLPSSFGPEDLQ 143
Cdd:PRK09027  137 NELnsASDLRIHLPGRQ----AHTLHDYLPDAFGPKDLN 171
PLN02402 PLN02402
cytidine deaminase
 15-142 7.42e-09

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 52.56  E-value: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  15 VQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPL--GICAERTAIQKAVSEGYKDFKAIAIASdmq 92
Cdd:PLN02402   25 LQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLhhSVHAEQFLITNLTLNAEPHLKYVAVSA--- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834521  93 ddfiSPCGACRQVMREF-------------GTNWPVYMTKPDGTYVVMTVQELLPSSFGPEDL 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 1622834521  24 EAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACY 60
Cdd:pfam08211  42 AAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAF 78
PRK08298 PRK08298
cytidine deaminase; Validated
 35-134 2.82e-05

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 41.32  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  35 HFPVG----AALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFKAIAIASDMQDD---FISPCGACRQVMR 107
Cdd:PRK08298   18 RYPNGwggaAAMRVEDGTILTSVAPEVINASTELCMETGAICEAHKLQKRVTHSICVARENEHSelkVLSPCGVCQERLF 97

                          90       100
                  ....*....|....*....|....*....
gi 1622834521 108 EFGTNWPVYMTKPDG--TYVVMTVQELLP 134
Cdd:PRK08298   98 YWGPDVMCAVTNADDptDIIFKPLKELQP 126
PLN02182 PLN02182
cytidine deaminase
 23-120 3.19e-05

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 42.35  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834521  23 QEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPL--GICAERTAIQKAVSEGYKDF--KAIAIASDMQdDFISP 98
Cdd:PLN02182   53 RKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLhhSIHAEQFLVTNLALNSEKDLceLAVAISTDGK-EFGTP 131

                          90       100
                  ....*....|....*....|...
gi 1622834521  99 CGACRQVMREFGTNWPV-YMTKP 120
Cdd:PLN02182  132 CGHCLQFLMEMSNALDIkILSKP 154
PLN02402 PLN02402
cytidine deaminase
 24-60 1.29e-04

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 40.62  E-value: 1.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622834521  24 EAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACY 60
Cdd:PLN02402  201 EAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAY 237
PRK09027 PRK09027
cytidine deaminase; Provisional
 15-58 1.51e-03

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 37.51  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622834521  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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