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Conserved domains on  [gi|15233630|ref|NP_194692|]
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Cytidine/deoxycytidylate deaminase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02182 super family cl30401
cytidine deaminase
 1-223 5.41e-120

cytidine deaminase


The actual alignment was detected with superfamily member PLN02182:

Pssm-ID: 177837  Cd Length: 339  Bit Score: 344.35  E-value: 5.41e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    1 MAQDQYKFVFTAKEAESEGVTEPMRLPNLIGKAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQFL 80
Cdd:PLN02182  23 MAQDRFKFVFTANEAAAEGVTDPIRLPNLIRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   81 VTNLALNSEKGLHLLAVTISTDGNDFGAPCGNCRQFLMEISKALNIKILLKSKYEAeGSFKSLRLLLPdrfspdDVLPKG 160
Cdd:PLN02182 103 VTNLALNSEKDLCELAVAISTDGKEFGTPCGHCLQFLMEMSNALDIKILSKPKHEA-GSFSSLRHLLP------NVLPKG 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233630  161 SPLLLEKRHNCLSLSGSAEEICSSDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:PLN02182 176 SPFLLEKRDNCLTLSGPAGEICSLDCSHLKCKALAAANNSFSPYTESPSGVALLDNDGKWYRG 238
 
Name Accession Description Interval E-value
PLN02182 PLN02182
cytidine deaminase
 1-223 5.41e-120

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 344.35  E-value: 5.41e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    1 MAQDQYKFVFTAKEAESEGVTEPMRLPNLIGKAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQFL 80
Cdd:PLN02182  23 MAQDRFKFVFTANEAAAEGVTDPIRLPNLIRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   81 VTNLALNSEKGLHLLAVTISTDGNDFGAPCGNCRQFLMEISKALNIKILLKSKYEAeGSFKSLRLLLPdrfspdDVLPKG 160
Cdd:PLN02182 103 VTNLALNSEKDLCELAVAISTDGKEFGTPCGHCLQFLMEMSNALDIKILSKPKHEA-GSFSSLRHLLP------NVLPKG 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233630  161 SPLLLEKRHNCLSLSGSAEEICSSDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:PLN02182 176 SPFLLEKRDNCLTLSGPAGEICSLDCSHLKCKALAAANNSFSPYTESPSGVALLDNDGKWYRG 238
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 6-223 1.87e-108

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: 312.92  E-value: 1.87e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630     6 YKFVFTAKEAESEG----VTEPMRLPNLIGKAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQFLV 81
Cdd:TIGR01355   1 PKFVFTAEQAQSLGtlsgLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    82 TNLALNSEKGLHLLAVTistdgndfGAPCGNCRQFLMEISKALNIKILLKSKYEAEGsfKSLRLLLPDRFSPDDVLPKGS 161
Cdd:TIGR01355  81 SHLALNGERGLNDLAVS--------FAPCGHCRQFLNEIRNASSIKILLPDPHNKRD--MSLQSYLPDRFGPDDLLIKSA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233630   162 PLLLEKRHNCLSLSGSAEEICSSDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:TIGR01355 151 PLLLEERHNCLALIDPDSIRNSDICSDLKQQALKAANRSYAPYSKSPSGVALKDREGKVYRG 212
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 32-155 1.47e-30

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: 109.47  E-value: 1.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630  32 KAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLhhSIHAEQFLVTNLALNSEKGlhLLAVTISTDGNDFGAPCG 111
Cdd:COG0295  12 EARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGL--TLCAERTAIFAAVAAGERE--IKAIAVVADTGEPVSPCG 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15233630 112 NCRQFLMEISKAlNIKILLkskYEAEGSFKSLRL--LLPDRFSPDD 155
Cdd:COG0295  88 ACRQVLAEFAGP-DLEVIL---PNGDGEVKTVTLseLLPDAFGPED 129
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
143-223 2.76e-28

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 103.38  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   143 LRLLLPDRFSPDDVLPKgsPLLLEKRHNCLSLSgsaeeicssDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYR 222
Cdd:pfam08211   1 LSSYLPDAFGPKDLLID--DLLLDPQDNGLTLD---------DDDPLKQAALAAANRSYAPYSKCPSGVALQDGDGRVYR 69


                  .
gi 15233630   223 G 223
Cdd:pfam08211  70 G 70
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 32-137 2.34e-22

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: 87.78  E-value: 2.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630  32 KAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHhsIHAEQFLVTNLALNSEKG-LHLLAVtisTDGNDFGAPC 110
Cdd:cd01283   6 AAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLT--LCAERTAIGKAVSEGLRRyLVTWAV---SDEGGVWSPC 80

                        90       100
                ....*....|....*....|....*..
gi 15233630 111 GNCRQFLMEISKAlNIKILLKSKYEAE 137
Cdd:cd01283  81 GACRQVLAEFLPS-RLYIIIDNPKGEE 106
 
Name Accession Description Interval E-value
PLN02182 PLN02182
cytidine deaminase
 1-223 5.41e-120

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 344.35  E-value: 5.41e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    1 MAQDQYKFVFTAKEAESEGVTEPMRLPNLIGKAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQFL 80
Cdd:PLN02182  23 MAQDRFKFVFTANEAAAEGVTDPIRLPNLIRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   81 VTNLALNSEKGLHLLAVTISTDGNDFGAPCGNCRQFLMEISKALNIKILLKSKYEAeGSFKSLRLLLPdrfspdDVLPKG 160
Cdd:PLN02182 103 VTNLALNSEKDLCELAVAISTDGKEFGTPCGHCLQFLMEMSNALDIKILSKPKHEA-GSFSSLRHLLP------NVLPKG 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233630  161 SPLLLEKRHNCLSLSGSAEEICSSDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:PLN02182 176 SPFLLEKRDNCLTLSGPAGEICSLDCSHLKCKALAAANNSFSPYTESPSGVALLDNDGKWYRG 238
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 6-223 1.87e-108

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: 312.92  E-value: 1.87e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630     6 YKFVFTAKEAESEG----VTEPMRLPNLIGKAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQFLV 81
Cdd:TIGR01355   1 PKFVFTAEQAQSLGtlsgLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    82 TNLALNSEKGLHLLAVTistdgndfGAPCGNCRQFLMEISKALNIKILLKSKYEAEGsfKSLRLLLPDRFSPDDVLPKGS 161
Cdd:TIGR01355  81 SHLALNGERGLNDLAVS--------FAPCGHCRQFLNEIRNASSIKILLPDPHNKRD--MSLQSYLPDRFGPDDLLIKSA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233630   162 PLLLEKRHNCLSLSGSAEEICSSDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:TIGR01355 151 PLLLEERHNCLALIDPDSIRNSDICSDLKQQALKAANRSYAPYSKSPSGVALKDREGKVYRG 212
PLN02402 PLN02402
cytidine deaminase
 4-223 7.87e-74

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 225.90  E-value: 7.87e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    4 DQYKFVFTAKEAES----EGVTEPMRLPNLIGKAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQF 79
Cdd:PLN02402   2 DGPIFVIEASEAESmakqSGLTVLQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSVHAEQF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   80 LVTNLALNSEKGLHLLAVTistdgndfGAPCGNCRQFLMEISKALNIKILLKSKYEAEGS----------FKSLRLLLPD 149
Cdd:PLN02402  82 LITNLTLNAEPHLKYVAVS--------AAPCGHCRQFFQEIRDAPDIKILITGDSNSNDSyknsladsqqFEPLSCLLPH 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233630  150 RFSPDDVLPKGSPLLLEKRHNCLSLSGsAEEICSSDCS---HLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:PLN02402 154 RFGPDDLLDKDVPLLLEPHHNHLSFVG-DDKLPNGISAssdDLKNEALEAANKSHAPYSNCPSGVALMDCEGKVYRG 229
PRK09027 PRK09027
cytidine deaminase; Provisional
 33-223 8.41e-42

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 143.44  E-value: 8.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   33 AMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSIHAEQFLVTNLALNSEKGlhLLAVTIstdgNDFgaPCGN 112
Cdd:PRK09027  60 AAACAVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQQTVHAEQSAISHAWLRGEKA--IADITV----NYT--PCGH 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630  113 CRQFLMEISKALNIKILLKSKYEAegsfkSLRLLLPDRFSPDDVLpkGSPLLLEKRHNCLSL-SGSAEEIcssdcshlkc 191
Cdd:PRK09027 132 CRQFMNELNSASDLRIHLPGRQAH-----TLHDYLPDAFGPKDLN--ITTLLMDPQDHGLALdTGDPLIQ---------- 194

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15233630  192 KALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:PRK09027 195 AALDAANRSHAPYSQSYSGVALETKDGRIYTG 226
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 32-155 1.47e-30

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: 109.47  E-value: 1.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630  32 KAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLhhSIHAEQFLVTNLALNSEKGlhLLAVTISTDGNDFGAPCG 111
Cdd:COG0295  12 EARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGL--TLCAERTAIFAAVAAGERE--IKAIAVVADTGEPVSPCG 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15233630 112 NCRQFLMEISKAlNIKILLkskYEAEGSFKSLRL--LLPDRFSPDD 155
Cdd:COG0295  88 ACRQVLAEFAGP-DLEVIL---PNGDGEVKTVTLseLLPDAFGPED 129
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
143-223 2.76e-28

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 103.38  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   143 LRLLLPDRFSPDDVLPKgsPLLLEKRHNCLSLSgsaeeicssDCSHLKCKALAAANNSFSPYTNSPSGVALQDDDGNWYR 222
Cdd:pfam08211   1 LSSYLPDAFGPKDLLID--DLLLDPQDNGLTLD---------DDDPLKQAALAAANRSYAPYSKCPSGVALQDGDGRVYR 69


                  .
gi 15233630   223 G 223
Cdd:pfam08211  70 G 70
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 32-137 2.34e-22

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: 87.78  E-value: 2.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630  32 KAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHhsIHAEQFLVTNLALNSEKG-LHLLAVtisTDGNDFGAPC 110
Cdd:cd01283   6 AAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLT--LCAERTAIGKAVSEGLRRyLVTWAV---SDEGGVWSPC 80

                        90       100
                ....*....|....*....|....*..
gi 15233630 111 GNCRQFLMEISKAlNIKILLKSKYEAE 137
Cdd:cd01283  81 GACRQVLAEFLPS-RLYIIIDNPKGEE 106
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 32-155 1.04e-21

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: 86.55  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    32 KAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLhhSIHAEQFLVTNLAlnSEKGLHLLAVTISTDGNDFGAPCG 111
Cdd:TIGR01354   9 EARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPL--TICAERSAIGKAI--SAGYRKFVAIAVADSADDPVSPCG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15233630   112 NCRQFLMEISKAlNIKILLkskYEAEGSFK--SLRLLLPDRFSPDD 155
Cdd:TIGR01354  85 ACRQVLAEFAGP-DTPIYM---TNNDGTYKvyTVGELLPFGFGPSD 126
PRK05578 PRK05578
cytidine deaminase; Validated
 32-155 8.09e-19

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 78.80  E-value: 8.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   32 KAMSLALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLhhSIHAEQFLVTNLAlnSEKGLHLLAVTISTDGNDFGAPCG 111
Cdd:PRK05578  12 EASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGL--TNCAERTAIFKAI--SEGGGRLVAIACVGETGEPLSPCG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15233630  112 NCRQFLMEISKAlNIKILLKSKyeaEGSFKSLRL--LLPDRFSPDD 155
Cdd:PRK05578  88 RCRQVLAEFGGP-DLLVTLVAK---DGPTGEMTLgeLLPYAFTPDD 129
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
32-120 8.12e-10

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 54.23  E-value: 8.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630    32 KAMSLALA------PISKYKVGAVG-RARSGRIYLGVNVELPGLPlhHSIHAEQFLVTNLALNSEkGLHL----LAVTIS 100
Cdd:pfam00383   4 YFMRLALKaakrayPYSNFPVGAVIvKKDGEIIATGYNGENAGYD--PTIHAERNAIRQAGKRGE-GVRLegatLYVTLE 80

                          90       100
                  ....*....|....*....|
gi 15233630   101 tdgndfgaPCGNCRQFLMEI 120
Cdd:pfam00383  81 --------PCGMCAQAIIES 92
PRK12411 PRK12411
cytidine deaminase; Provisional
 37-156 5.95e-07

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 47.26  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233630   37 ALAPISKYKVGAVGRARSGRIYLGVNVELPGLPLHHSihAEQFLVtnLALNSEKGLHLLAVTISTDGNDFGAPCGNCRQF 116
Cdd:PRK12411  17 AYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNC--AERTAL--FKAVSEGDKEFVAIAIVADTKRPVPPCGACRQV 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15233630  117 LMEISKAlNIKILLkSKYEAEGSFKSLRLLLPDRFSPDDV 156
Cdd:PRK12411  93 MVELCKQ-DTKVYL-SNLHGDVQETTVGELLPGAFLAEDL 130
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 192-223 8.97e-03

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: 35.13  E-value: 8.97e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 15233630 192 KALAAANNSFSPYTNSPSGVALQDDDGNWYRG 223
Cdd:COG0295   9 AAREARENAYAPYSKFPVGAALLTEDGRIYTG 40
 
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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