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Conserved domains on  [gi|897177973|emb|CPB18479|]
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Cytidine deaminase [Staphylococcus aureus]

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 ...
 5-133 7.10e-70

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: 205.58  E-value: 7.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973    5 PHYFQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADK 84
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 897177973   85 PSSPCGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:TIGR01354  79 PVSPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
 
Name Accession Description Interval E-value
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 5-133 7.10e-70

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: 205.58  E-value: 7.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973    5 PHYFQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADK 84
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 897177973   85 PSSPCGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:TIGR01354  79 PVSPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 8-133 3.30e-62

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: 186.51  E-value: 3.30e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   8 FQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADKPSS 87
Cdd:COG0295    7 IEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGER--EIKAIAVVADTGEPVS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 897177973  88 PCGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:COG0295   85 PCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 9-133 1.28e-48

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 152.42  E-value: 1.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   9 QEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADKPSSP 88
Cdd:PRK12411   8 QEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDK--EFVAIAIVADTKRPVPP 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 897177973  89 CGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:PRK12411  86 CGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-120 4.45e-43

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: 137.47  E-value: 4.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   8 FQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpGDFESITVTvDADKPSS 87
Cdd:cd01283    1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLR-RYLVTWAVS-DEGGVWS 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 897177973  88 PCGACRQVLKELCDDDMPVYMTNHKGDMVMMTV 120
Cdd:cd01283   79 PCGACRQVLAEFLPSRLYIIIDNPKGEEFAYTL 111
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
7-107 7.74e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 72.72  E-value: 7.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973    7 YFQEVRKAQQESYsPYSQFKVGAYLKTKDGRT-FYGTNVENASYPLSICAERASLVSAISQGYRpGDFESITVTVDAdkp 85
Cdd:pfam00383   5 FMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYDPTIHAERNAIRQAGKRGEG-VRLEGATLYVTL--- 79

                          90       100
                  ....*....|....*....|..
gi 897177973   86 sSPCGACRQVLKELCDDDMPVY 107
Cdd:pfam00383  80 -EPCGMCAQAIIESGIKRVVFG 100
 
Name Accession Description Interval E-value
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 5-133 7.10e-70

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: 205.58  E-value: 7.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973    5 PHYFQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADK 84
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYR--KFVAIAVADSADD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 897177973   85 PSSPCGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:TIGR01354  79 PVSPCGACRQVLAEFAGPDTPIYMTNNDGTYKVYTVGELLPFGFGPSDL 127
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 8-133 3.30e-62

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: 186.51  E-value: 3.30e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   8 FQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADKPSS 87
Cdd:COG0295    7 IEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGER--EIKAIAVVADTGEPVS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 897177973  88 PCGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:COG0295   85 PCGACRQVLAEFAGPDLEVILPNGDGEVKTVTLSELLPDAFGPEDL 130
PRK12411 PRK12411
cytidine deaminase; Provisional
 9-133 1.28e-48

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 152.42  E-value: 1.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   9 QEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESITVTVDADKPSSP 88
Cdd:PRK12411   8 QEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDK--EFVAIAIVADTKRPVPP 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 897177973  89 CGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:PRK12411  86 CGACRQVMVELCKQDTKVYLSNLHGDVQETTVGELLPGAFLAEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 7-134 1.43e-46

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 146.98  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   7 YFQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYrpGDFESITVTVDADKPS 86
Cdd:PRK05578   6 LIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGG--GRLVAIACVGETGEPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 897177973  87 SPCGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDLE 134
Cdd:PRK05578  84 SPCGRCRQVLAEFGGPDLLVTLVAKDGPTGEMTLGELLPYAFTPDDLG 131
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 8-120 4.45e-43

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: 137.47  E-value: 4.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   8 FQEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpGDFESITVTvDADKPSS 87
Cdd:cd01283    1 IEAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLR-RYLVTWAVS-DEGGVWS 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 897177973  88 PCGACRQVLKELCDDDMPVYMTNHKGDMVMMTV 120
Cdd:cd01283   79 PCGACRQVLAEFLPSRLYIIIDNPKGEEFAYTL 111
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
7-107 7.74e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 72.72  E-value: 7.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973    7 YFQEVRKAQQESYsPYSQFKVGAYLKTKDGRT-FYGTNVENASYPLSICAERASLVSAISQGYRpGDFESITVTVDAdkp 85
Cdd:pfam00383   5 FMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYDPTIHAERNAIRQAGKRGEG-VRLEGATLYVTL--- 79

                          90       100
                  ....*....|....*....|..
gi 897177973   86 sSPCGACRQVLKELCDDDMPVY 107
Cdd:pfam00383  80 -EPCGMCAQAIIESGIKRVVFG 100
PRK06848 PRK06848
cytidine deaminase;
10-129 9.04e-15

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 65.92  E-value: 9.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973  10 EVRKAQQESYSPYSQfKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYRpgDFESItVTVDADKPS--- 86
Cdd:PRK06848  13 AAEKVIEKRYRNDWH-HVGAALRTKTGRIYAAVHLEAYVGRITVCAEAIAIGKAISEGDH--EIDTI-VAVRHPKPHedd 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 897177973  87 ------SPCGACRQVLKELCDDDMPVYMTNhkGDMVMMTVAELLPFGFS 129
Cdd:PRK06848  89 reiwvvSPCGACRELISDYGKNTNVIVPYN--DELVKVNIMELLPNKYT 135
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 11-133 4.76e-13

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: 64.08  E-value: 4.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   11 VRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPL--SICAERASLVSAISQGYRpgDFESITVTvdadkpSSP 88
Cdd:TIGR01355  29 IPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLhhSIHAEQFLISHLALNGER--GLNDLAVS------FAP 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 897177973   89 CGACRQVLKELCDDDMPVYMTNHKGDMVMMTVAELLPFGFSGKDL 133
Cdd:TIGR01355 101 CGHCRQFLNEIRNASSIKILLPDPHNKRDMSLQSYLPDRFGPDDL 145
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 5-109 6.31e-11

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: 55.25  E-value: 6.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   5 PHYFQEVRKaqqESYSPYSQFKVGAYL-KTKDGRTFY-GTNVENASYPLSICAERASLVSAISQGyrPGDFESITVTVda 82
Cdd:cd00786    1 MTEALKAAD---LGYAKESNFQVGACLvNKKDGGKVGrGCNIENAAYSMCNHAERTALFNAGSEG--DTKGQMLYVAL-- 73

                         90       100
                 ....*....|....*....|....*..
gi 897177973  83 dkpsSPCGACRQVLKELCDDDMPVYMT 109
Cdd:cd00786   74 ----SPCGACAQLIIELGIKDVIVVLT 96
PLN02182 PLN02182
cytidine deaminase
 11-101 4.50e-09

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 53.14  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973  11 VRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPL--SICAERAsLVSAISQGYRPGDFE-SITVTVDADKPSS 87
Cdd:PLN02182  52 IRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLhhSIHAEQF-LVTNLALNSEKDLCElAVAISTDGKEFGT 130

                         90
                 ....*....|....
gi 897177973  88 PCGACRQVLKELCD 101
Cdd:PLN02182 131 PCGHCLQFLMEMSN 144
PRK09027 PRK09027
cytidine deaminase; Provisional
 18-99 4.57e-08

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 49.83  E-value: 4.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973  18 SYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPL--SICAERaslvSAISQGYRPGD--FESITVTvdadkpSSPCGACR 93
Cdd:PRK09027  64 AVTPISHFNVGAIARGVSGNFYFGANMEFAGAALqqTVHAEQ----SAISHAWLRGEkaIADITVN------YTPCGHCR 133


                 ....*.
gi 897177973  94 QVLKEL 99
Cdd:PRK09027 134 QFMNEL 139
PLN02402 PLN02402
cytidine deaminase
 11-133 1.52e-06

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 45.63  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973  11 VRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPL--SICAERAsLVSAISQGYRPgDFESITVTvdadkpSSP 88
Cdd:PLN02402  32 VKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLhhSVHAEQF-LITNLTLNAEP-HLKYVAVS------AAP 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 897177973  89 CGACRQVLKELCD-DDMPVYMT-------NHKGDMV----MMTVAELLPFGFSGKDL 133
Cdd:PLN02402 104 CGHCRQFFQEIRDaPDIKILITgdsnsndSYKNSLAdsqqFEPLSCLLPHRFGPDDL 160
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-80 4.48e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 42.90  E-value: 4.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 897177973    9 QEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGyrpGDFESITVTV 80
Cdd:pfam08211  38 QAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAFNPSLPPLQAALVDFVAGG---KDFEDIVRAV 106
PRK09027 PRK09027
cytidine deaminase; Provisional
 1-102 5.39e-05

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 41.36  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 897177973   1 MSYQPHYF---------QEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGYrpg 71
Cdd:PRK09027 177 MDPQDHGLaldtgdpliQAALDAANRSHAPYSQSYSGVALETKDGRIYTGRYAENAAFNPSLPPLQGALNLLNLSGE--- 253

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 897177973  72 DFESITVTVDADKPSSP---CGACRQVLKEL-CDD 102
Cdd:PRK09027 254 DFSDIQRAVLVEKADAKlsqWDATQATLKALgCHE 288
PLN02402 PLN02402
cytidine deaminase
 9-84 7.53e-05

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 41.00  E-value: 7.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 897177973   9 QEVRKAQQESYSPYSQFKVGAYLKTKDGRTFYGTNVENASYPLSICAERASLVSAISQGyRPGDFESITVTVDADK 84
Cdd:PLN02402 197 NEALEAANKSHAPYSNCPSGVALMDCEGKVYRGSYMESAAYNPSMGPVQAALVAYVAGG-RGGGYERIVAAVLVEK 271
 
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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