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cd00227: CPT 
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Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary (C-3) hydroxyl of the antibiotic. Related structurally to shikimate kinase II.
Links
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Statistics
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PSSM-Id: 238139
View PSSM: cd00227
Aligned: 5 rows
Threshold Bit Score: 237.415
Threshold Setting Gi: 15075011
Created: 4-Sep-2001
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
Hierarchy
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Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:

cd00227 is part of a hierarchy of related CD models.
Use the graphical representation to navigate this hierarchy.
cd00227 is a member of the superfamily cl17391.
cd00227:CPT150750111QHY A1QHN A1347325213878865150750111QHY A1QHN A1347325213878865
cd00227 Sequence Cluster
cd00227 Sequence Cluster
Sub-family Hierarchy
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CD Hierarchy
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                 ## ###                                                                
1QHY_A        2 TTRMIILNGGSSAGKSGIVRCLQSVLPEPWLAFGVDSLIEA-MPLKMQsa----------egGIEFDAd--GGVSIG--P 66
1QHN_A        2 TTRXIILNGGSSAGKSGIVRCLQSVLPEPWLAFGVDSLIEA-XPLKXQsa----------egGIEFDAd--GGVSIG--P 66
gi 15075011   7 PGRIVILNGAPRSGKSSIAEAIQETFDGPWMNLGVDAYMERvMPRRCLp-------------GIGLRP---GGELPEieA 70
gi 13473252  58 KARIVLLNGVGSAGKSSIARALQTITAAPFLHVQMDSFLEM-LPDALQdhadg-----fsyeTVRQDGkpaVVIRAG--P 129
gi 13878865  22 EGKLILLNGGSSAGKTSLALAFQDLAAECWMHIGIDLFWFA-LPPEQLdlarvrpeyytwdsAVEADGlewFTVHPG--P 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                #                                         #   #  #     
1QHY_A       67 EFRALEGAWAEGVVAMARAGARIIIDDVFl-----gGAAAQERWRSFVGdLDVLWVGVRCDGAVAEGRETaRGDR----- 136
1QHN_A       67 EFRALEGAWAEGVVAXARAGARIIIDDVFl-----gGAAAQERWRSFVGdLDVLWVGVRCDGAVAEGRETaRGDR----- 136
gi 15075011  71 LVPLFYAALYESVAAHSRLGLNVVADVGHhdaygepRHILPDCARRLLG-LPVLFVGVRCPVETIMERRN-RGQPgregg 148
gi 13473252 130 VGERTLRGMRHAIAAMAGQGNDLIVDDVLc------NGELSDCVDLLSA-FDFHLVGVMAPLEVLEAREArRADR----- 197
gi 13878865  99 ILDLAMHSRYRAIRAYLDNGMNVIADDVIw-----tREWLVDALRVFEG-CRVWMVGVHVSDEEGARRELeRGDR----- 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
Feature 1                                          # #            
1QHY_A      137 ---------VAGMAAKQAYVVHEGVEYDVEVDTTHKESIECAWAIAAHVV 177
1QHN_A      137 ---------VAGXAAKQAYVVHEGVEYDVEVDTTHKESIECAWAIAAHVV 177
gi 15075011 149 yltgseaepVPRQVLAWQREVHRPGIYDLAVDTSMMTPDECAALIRKRLE 198
gi 13473252 198 ---------LPGLARWQYERVHAGISYDLEVDTSQSTPLECARRIQQRFQ 238
gi 13878865 168 ---------HPGWNRGSARAAHADAEYDFELDTTATPVHELARELHESYQ 208

Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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Click on image for an interactive view with Cn3D
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D