NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1575441804|ref|WP_129889671|]
View 

cytidine deaminase [Ktedonosporobacter rubrisoli]

Protein Classification

cytidine deaminase family protein( domain architecture ID 11416731)

cytidine deaminase family protein catalyzes the deamination of cytidine or deoxycytidine, converting them into uridine or deoxyuridine, and play essential roles in nucleotide metabolism, RNA editing, and immune responses

CATH:  3.40.140.10
EC:  3.5.4.5
Gene Ontology:  GO:0009972|GO:0008270|GO:0004126
PubMed:  16720547
SCOP:  3001838

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
29-136 2.99e-28

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: 100.61  E-value: 2.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVWKDEKgkiyVLSPCGRCREFVSQVHKENL 107
Cdd:COG0295    26 VGAALLTEDGRIYTGCNVENASyGLTLCAERTAIFAAVAAGEREIKAIAVVADTGE----PVSPCGACRQVLAEFAGPDL 101
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1575441804 108 EtdVVL----GRDNVVKMRELIPHPdqFVPVEL 136
Cdd:COG0295   102 E--VILpngdGEVKTVTLSELLPDA--FGPEDL 130
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
29-136 2.99e-28

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: 100.61  E-value: 2.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVWKDEKgkiyVLSPCGRCREFVSQVHKENL 107
Cdd:COG0295    26 VGAALLTEDGRIYTGCNVENASyGLTLCAERTAIFAAVAAGEREIKAIAVVADTGE----PVSPCGACRQVLAEFAGPDL 101
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1575441804 108 EtdVVL----GRDNVVKMRELIPHPdqFVPVEL 136
Cdd:COG0295   102 E--VILpngdGEVKTVTLSELLPDA--FGPEDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
29-107 6.24e-17

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: 71.22  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVwkdeKGKIYVLSPCGRCREFVSQVHKENL 107
Cdd:cd01283    20 VGAALLTKDGRIFTGVNVENASyGLTLCAERTAIGKAVSEGLRRYLVTWAV----SDEGGVWSPCGACRQVLAEFLPSRL 95
PRK05578 PRK05578
cytidine deaminase; Validated
29-137 1.51e-16

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 70.71  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVwkDEKGKIyvLSPCGRCR----EFVSQvh 103
Cdd:PRK05578   26 VGAALLTDDGRIYTGCNIENASyGLTNCAERTAIFKAISEGGGRLVAIACV--GETGEP--LSPCGRCRqvlaEFGGP-- 99
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1575441804 104 kenlETDVVL----GRDNVVKMRELIphPDQFVPVELE 137
Cdd:PRK05578  100 ----DLLVTLvakdGPTGEMTLGELL--PYAFTPDDLG 131
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
29-101 1.21e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 41.52  E-value: 1.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1575441804  29 VGCALVTDQGNV-YVGVCLDTASGTGF-CAEASAIAAMVTAGEfrisqivaVWKDEKGKIYV-LSPCGRCREFVSQ 101
Cdd:pfam00383  24 VGAVIVKKDGEIiATGYNGENAGYDPTiHAERNAIRQAGKRGE--------GVRLEGATLYVtLEPCGMCAQAIIE 91
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
29-136 2.99e-28

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: 100.61  E-value: 2.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVWKDEKgkiyVLSPCGRCREFVSQVHKENL 107
Cdd:COG0295    26 VGAALLTEDGRIYTGCNVENASyGLTLCAERTAIFAAVAAGEREIKAIAVVADTGE----PVSPCGACRQVLAEFAGPDL 101
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1575441804 108 EtdVVL----GRDNVVKMRELIPHPdqFVPVEL 136
Cdd:COG0295   102 E--VILpngdGEVKTVTLSELLPDA--FGPEDL 130
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
29-107 6.24e-17

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: 71.22  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVwkdeKGKIYVLSPCGRCREFVSQVHKENL 107
Cdd:cd01283    20 VGAALLTKDGRIFTGVNVENASyGLTLCAERTAIGKAVSEGLRRYLVTWAV----SDEGGVWSPCGACRQVLAEFLPSRL 95
PRK05578 PRK05578
cytidine deaminase; Validated
29-137 1.51e-16

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 70.71  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIVAVwkDEKGKIyvLSPCGRCR----EFVSQvh 103
Cdd:PRK05578   26 VGAALLTDDGRIYTGCNIENASyGLTNCAERTAIFKAISEGGGRLVAIACV--GETGEP--LSPCGRCRqvlaEFGGP-- 99
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1575441804 104 kenlETDVVL----GRDNVVKMRELIphPDQFVPVELE 137
Cdd:PRK05578  100 ----DLLVTLvakdGPTGEMTLGELL--PYAFTPDDLG 131
PRK06848 PRK06848
cytidine deaminase;
8-128 2.21e-16

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 70.54  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804   8 LIKRAAAVVNPQRIGDRlvGDVGCALVTDQGNVYVGVCLDTASG-TGFCAEASAIAAMVTAGEFRISQIVAVW----KDE 82
Cdd:PRK06848   10 LIKAAEKVIEKRYRNDW--HHVGAALRTKTGRIYAAVHLEAYVGrITVCAEAIAIGKAISEGDHEIDTIVAVRhpkpHED 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1575441804  83 KGKIYVLSPCGRCREFVSQVHKenlETDVVL-GRDNVVKMR--ELIPHP 128
Cdd:PRK06848   88 DREIWVVSPCGACRELISDYGK---NTNVIVpYNDELVKVNimELLPNK 133
PRK08298 PRK08298
cytidine deaminase; Validated
32-97 9.52e-08

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 47.87  E-value: 9.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1575441804  32 ALVTDQGNVYVGVCLDTA-SGTGFCAEASAIAAMVTAGEFRISQIVAVWKDEKGKIYVLSPCGRCRE 97
Cdd:PRK08298   28 AMRVEDGTILTSVAPEVInASTELCMETGAICEAHKLQKRVTHSICVARENEHSELKVLSPCGVCQE 94
PRK12411 PRK12411
cytidine deaminase; Provisional
29-126 5.60e-07

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 45.72  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575441804  29 VGCALVTDQGNVYVGVCLDTAS-GTGFCAEASAIAAMVTAGEFRISQIvAVWKDEKGKIyvlSPCGRCREFV-------S 100
Cdd:PRK12411   26 VGAALLTQDGKVYRGCNVENASyGLCNCAERTALFKAVSEGDKEFVAI-AIVADTKRPV---PPCGACRQVMvelckqdT 101
                          90       100
                  ....*....|....*....|....*.
gi 1575441804 101 QVHKENLETDVvlgrdNVVKMRELIP 126
Cdd:PRK12411  102 KVYLSNLHGDV-----QETTVGELLP 122
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
29-101 1.21e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 41.52  E-value: 1.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1575441804  29 VGCALVTDQGNV-YVGVCLDTASGTGF-CAEASAIAAMVTAGEfrisqivaVWKDEKGKIYV-LSPCGRCREFVSQ 101
Cdd:pfam00383  24 VGAVIVKKDGEIiATGYNGENAGYDPTiHAERNAIRQAGKRGE--------GVRLEGATLYVtLEPCGMCAQAIIE 91
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH