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Conserved domains on  [gi|446475710|ref|WP_000553564|]
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MULTISPECIES: cytidine deaminase [Enterobacteriaceae]

Protein Classification

cytidine deaminase( domain architecture ID 11483494)

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
PRK09027 PRK09027
cytidine deaminase; Provisional
 1-294 0e+00

cytidine deaminase; Provisional


:

Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 502.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710   1 MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGV 80
Cdd:PRK09027   1 MQPRFQTALAQLPDALQSALAPILADQDFPAMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISHFNVGAIARGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  81 SGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDY 160
Cdd:PRK09027  81 SGNFYFGANMEFAGAALQQTVHAEQSAISHAWLRGEKAIADITVNYTPCGHCRQFMNELNSASDLRIHLPGRQAHTLHDY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710 161 LPDAFGPKDLEIKTLLMDEQDHGYAL-TGDALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPP 239
Cdd:PRK09027 161 LPDAFGPKDLNITTLLMDPQDHGLALdTGDPLIQAALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAFNPSLPP 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446475710 240 LQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA 294
Cdd:PRK09027 241 LQGALNLLNLSGEDFSDIQRAVLVEKADAKLSQWDATQATLKALGCHELERVLLA 295
 
Name Accession Description Interval E-value
PRK09027 PRK09027
cytidine deaminase; Provisional
 1-294 0e+00

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 502.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710   1 MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGV 80
Cdd:PRK09027   1 MQPRFQTALAQLPDALQSALAPILADQDFPAMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISHFNVGAIARGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  81 SGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDY 160
Cdd:PRK09027  81 SGNFYFGANMEFAGAALQQTVHAEQSAISHAWLRGEKAIADITVNYTPCGHCRQFMNELNSASDLRIHLPGRQAHTLHDY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710 161 LPDAFGPKDLEIKTLLMDEQDHGYAL-TGDALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPP 239
Cdd:PRK09027 161 LPDAFGPKDLNITTLLMDPQDHGLALdTGDPLIQAALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAFNPSLPP 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446475710 240 LQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA 294
Cdd:PRK09027 241 LQGALNLLNLSGEDFSDIQRAVLVEKADAKLSQWDATQATLKALGCHELERVLLA 295
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 29-283 1.32e-85

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: 257.84  E-value: 1.32e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710   29 FPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAI 108
Cdd:TIGR01355   1 PKFVFTAEQAQSLGTLSGLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  109 SHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLP---GREAHALRDYLPDAFGPKDLEIKT--LLMDEQDHG 183
Cdd:TIGR01355  81 SHLALNGERGLNDLAVSFAPCGHCRQFLNEIRNASSIKILLPdphNKRDMSLQSYLPDRFGPDDLLIKSapLLLEERHNC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  184 YALTG----------DALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPPLQGALI--LLNLKG 251
Cdd:TIGR01355 161 LALIDpdsirnsdicSDLKQQALKAANRSYAPYSKSPSGVALKDREGKVYRGWYIESAAFNPSLGPLQAALVdfMANGGG 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 446475710  252 YDYPDIQRAVLAEKADAPLIQWDATSATLKAL 283
Cdd:TIGR01355 241 KGFEDIVRAVLVEKADAKVSHEATARALLETI 272
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
157-276 5.26e-62

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 191.98  E-value: 5.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  157 LRDYLPDAFGPKDLEIKTLLMDEQDHGYAL-TGDALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNP 235
Cdd:pfam08211   1 LSSYLPDAFGPKDLLIDDLLLDPQDNGLTLdDDDPLKQAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAFNP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446475710  236 TLPPLQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDAT 276
Cdd:pfam08211  81 SLPPLQAALVDFVAGGKDFEDIVRAVLVEKEDAKVSQEATA 121
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 66-170 3.62e-41

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: 138.74  E-value: 3.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  66 TPLSNFNVGAIARGVSGTWYFGANMEfiGATMQQTVHAEQSAISHAWLSGEKALAAITVN------YTPCGHCRQFMNEL 139
Cdd:COG0295   19 APYSKFPVGAALLTEDGRIYTGCNVE--NASYGLTLCAERTAIFAAVAAGEREIKAIAVVadtgepVSPCGACRQVLAEF 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446475710 140 NSGlDLRIHLPGRE----AHALRDYLPDAFGPKDL 170
Cdd:COG0295   97 AGP-DLEVILPNGDgevkTVTLSELLPDAFGPEDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 65-152 9.02e-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: 9.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  65 RTPLSNFNVGAIARGVSGTWYFGANMEFIGATMqqTVHAEQSAISHAWLSGEK------ALAAITVNYTPCGHCRQFMNE 138
Cdd:cd01283   12 YAPYSNFTVGAALLTKDGRIFTGVNVENASYGL--TLCAERTAIGKAVSEGLRrylvtwAVSDEGGVWSPCGACRQVLAE 89

                         90
                 ....*....|....
gi 446475710 139 LNSGlDLRIHLPGR 152
Cdd:cd01283   90 FLPS-RLYIIIDNP 102
 
Name Accession Description Interval E-value
PRK09027 PRK09027
cytidine deaminase; Provisional
 1-294 0e+00

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 502.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710   1 MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGV 80
Cdd:PRK09027   1 MQPRFQTALAQLPDALQSALAPILADQDFPAMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISHFNVGAIARGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  81 SGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDY 160
Cdd:PRK09027  81 SGNFYFGANMEFAGAALQQTVHAEQSAISHAWLRGEKAIADITVNYTPCGHCRQFMNELNSASDLRIHLPGRQAHTLHDY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710 161 LPDAFGPKDLEIKTLLMDEQDHGYAL-TGDALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPP 239
Cdd:PRK09027 161 LPDAFGPKDLNITTLLMDPQDHGLALdTGDPLIQAALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAFNPSLPP 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446475710 240 LQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA 294
Cdd:PRK09027 241 LQGALNLLNLSGEDFSDIQRAVLVEKADAKLSQWDATQATLKALGCHELERVLLA 295
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 29-283 1.32e-85

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: 257.84  E-value: 1.32e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710   29 FPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAI 108
Cdd:TIGR01355   1 PKFVFTAEQAQSLGTLSGLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  109 SHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLP---GREAHALRDYLPDAFGPKDLEIKT--LLMDEQDHG 183
Cdd:TIGR01355  81 SHLALNGERGLNDLAVSFAPCGHCRQFLNEIRNASSIKILLPdphNKRDMSLQSYLPDRFGPDDLLIKSapLLLEERHNC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  184 YALTG----------DALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPPLQGALI--LLNLKG 251
Cdd:TIGR01355 161 LALIDpdsirnsdicSDLKQQALKAANRSYAPYSKSPSGVALKDREGKVYRGWYIESAAFNPSLGPLQAALVdfMANGGG 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 446475710  252 YDYPDIQRAVLAEKADAPLIQWDATSATLKAL 283
Cdd:TIGR01355 241 KGFEDIVRAVLVEKADAKVSHEATARALLETI 272
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
157-276 5.26e-62

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 191.98  E-value: 5.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  157 LRDYLPDAFGPKDLEIKTLLMDEQDHGYAL-TGDALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNP 235
Cdd:pfam08211   1 LSSYLPDAFGPKDLLIDDLLLDPQDNGLTLdDDDPLKQAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAFNP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446475710  236 TLPPLQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDAT 276
Cdd:pfam08211  81 SLPPLQAALVDFVAGGKDFEDIVRAVLVEKEDAKVSQEATA 121
PLN02402 PLN02402
cytidine deaminase
 65-272 7.49e-48

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 161.96  E-value: 7.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  65 RTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLD 144
Cdd:PLN02402  40 RPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSVHAEQFLITNLTLNAEPHLKYVAVSAAPCGHCRQFFQEIRDAPD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710 145 LRIHLPG---------------REAHALRDYLPDAFGPKDLEIKT--LLMDEQDHGYALTGDA------------LSQAA 195
Cdd:PLN02402 120 IKILITGdsnsndsyknsladsQQFEPLSCLLPHRFGPDDLLDKDvpLLLEPHHNHLSFVGDDklpngisassddLKNEA 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446475710 196 IAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPPLQGALI--LLNLKGYDYPDIQRAVLAEKADAPLIQ 272
Cdd:PLN02402 200 LEAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAYNPSMGPVQAALVayVAGGRGGGYERIVAAVLVEKEGAVVRQ 278
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 66-170 3.62e-41

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: 138.74  E-value: 3.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  66 TPLSNFNVGAIARGVSGTWYFGANMEfiGATMQQTVHAEQSAISHAWLSGEKALAAITVN------YTPCGHCRQFMNEL 139
Cdd:COG0295   19 APYSKFPVGAALLTEDGRIYTGCNVE--NASYGLTLCAERTAIFAAVAAGEREIKAIAVVadtgepVSPCGACRQVLAEF 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446475710 140 NSGlDLRIHLPGRE----AHALRDYLPDAFGPKDL 170
Cdd:COG0295   97 AGP-DLEVILPNGDgevkTVTLSELLPDAFGPEDL 130
PLN02182 PLN02182
cytidine deaminase
 65-289 1.93e-32

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 122.47  E-value: 1.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  65 RTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNY--------TPCGHCRQFM 136
Cdd:PLN02182  60 RAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFLVTNLALNSEKDLCELAVAIstdgkefgTPCGHCLQFL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710 137 NELNSGLDLRI-HLPGREA---HALRDYLPDAFgPKDleiKTLLMDEQDHGYALTGDA----------LSQAAIAAANRS 202
Cdd:PLN02182 140 MEMSNALDIKIlSKPKHEAgsfSSLRHLLPNVL-PKG---SPFLLEKRDNCLTLSGPAgeicsldcshLKCKALAAANNS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710 203 HMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPPLQGALI--LLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATL 280
Cdd:PLN02182 216 FSPYTESPSGVALLDNDGKWYRGWYIESVASNPSFGPVQAALVdfVARSRGKMFNKIVQAVLVEKNNAIVSQERTAKIIL 295


                 ....*....
gi 446475710 281 KALGCHSID 289
Cdd:PLN02182 296 DTIAAPNCD 304
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 65-152 9.02e-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: 9.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  65 RTPLSNFNVGAIARGVSGTWYFGANMEFIGATMqqTVHAEQSAISHAWLSGEK------ALAAITVNYTPCGHCRQFMNE 138
Cdd:cd01283   12 YAPYSNFTVGAALLTKDGRIFTGVNVENASYGL--TLCAERTAIGKAVSEGLRrylvtwAVSDEGGVWSPCGACRQVLAE 89

                         90
                 ....*....|....
gi 446475710 139 LNSGlDLRIHLPGR 152
Cdd:cd01283   90 FLPS-RLYIIIDNP 102
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 66-170 4.32e-20

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: 83.86  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710   66 TPLSNFNVGAIARGVSGTWYFGANMEfiGATMQQTVHAEQSAISHAWLSGEKALAAITVN------YTPCGHCRQFMNEL 139
Cdd:TIGR01354  16 APYSNFKVGAALLTKDGRIFTGVNVE--NASYPLTICAERSAIGKAISAGYRKFVAIAVAdsaddpVSPCGACRQVLAEF 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446475710  140 nSGLDLRIHLPGR----EAHALRDYLPDAFGPKDL 170
Cdd:TIGR01354  94 -AGPDTPIYMTNNdgtyKVYTVGELLPFGFGPSDL 127
PRK05578 PRK05578
cytidine deaminase; Validated
 67-171 1.15e-15

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 71.87  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  67 PLSNFNVGAIARGVSGTWYFGANMEfiGATMQQTVHAEQSAISHAWLSGEKALAAITV-----NYT-PCGHCRQFMNELn 140
Cdd:PRK05578  20 PYSKFPVGAALLTDDGRIYTGCNIE--NASYGLTNCAERTAIFKAISEGGGRLVAIACvgetgEPLsPCGRCRQVLAEF- 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446475710 141 SGLDLRIHLPGREAHA----LRDYLPDAFGPKDLE 171
Cdd:PRK05578  97 GGPDLLVTLVAKDGPTgemtLGELLPYAFTPDDLG 131
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
67-139 1.95e-12

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 62.32  E-value: 1.95e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446475710   67 PLSNFNVGAIARGVSGTWYF-GANMEFIGATMqqTVHAEQSAISHAWLSGEK---ALAAITVNYTPCGHCRQFMNEL 139
Cdd:pfam00383  18 PYSNFPVGAVIVKKDGEIIAtGYNGENAGYDP--TIHAERNAIRQAGKRGEGvrlEGATLYVTLEPCGMCAQAIIES 92
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 200-252 7.12e-10

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: 55.43  E-value: 7.12e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446475710 200 NRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTLPPLQGALILLNLKGY 252
Cdd:cd01283    9 EFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGL 61
PRK12411 PRK12411
cytidine deaminase; Provisional
 67-170 2.47e-08

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 51.89  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475710  67 PLSNFNVGAIARGVSGTWYFGANMEfiGATMQQTVHAEQSAISHAWLSGEKALAAITV------NYTPCGHCRQFMNELN 140
Cdd:PRK12411  20 PYSKFQVGAALLTQDGKVYRGCNVE--NASYGLCNCAERTALFKAVSEGDKEFVAIAIvadtkrPVPPCGACRQVMVELC 97

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446475710 141 SGlDLRIHLPGREAH----ALRDYLPDAFGPKDL 170
Cdd:PRK12411  98 KQ-DTKVYLSNLHGDvqetTVGELLPGAFLAEDL 130
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 189-237 1.06e-05

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: 44.18  E-value: 1.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446475710  189 DALSQAAIAAANRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTL 237
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTI 49
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 67-139 3.91e-05

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: 41.77  E-value: 3.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446475710  67 PLSNFNVGA--IARGVSGTWYFGANMEFIGATMqqTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNEL 139
Cdd:cd00786   14 KESNFQVGAclVNKKDGGKVGRGCNIENAAYSM--CNHAERTALFNAGSEGDTKGQMLYVALSPCGACAQLIIEL 86
PRK05578 PRK05578
cytidine deaminase; Validated
 201-237 5.06e-04

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 39.12  E-value: 5.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446475710 201 RSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTL 237
Cdd:PRK05578  16 KAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTN 52
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 200-237 5.79e-04

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: 38.98  E-value: 5.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446475710 200 NRSHMPYSKSPSGVTLECKDGRIFSGSYAENAAFNPTL 237
Cdd:COG0295   15 ENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTL 52
 
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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