2Q73,2Q73


Conserved Protein Domain Family
NTP-PPase_iMazG

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cd11536: NTP-PPase_iMazG 
Click on image for an interactive view with Cn3D
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in integron-associated MazG (iMazG) proteins
This family corresponds to the iMazG proteins representing a new subfamily of MazG NTP-PPases. iMazG is likely to act as a house-cleaning enzyme capable of removing aberrant dNTPs, preventing the incorporation of damaging non-canonical nucleotides into host-cell DNA. It can convert dNTP to dNMP and pyrophosphate by cleaving between the alpha- and beta-phosphates of its dNTP substrates, with a marked preference for dCTP and dATP. Unlike typical tandem-domain MazG proteins, iMazG contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. The divalent ions, such as Mg2+, are required for its pyrophosphatase activity.
Statistics
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PSSM-Id: 212143
Aligned: 8 rows
Threshold Bit Score: 110.612
Created: 1-Sep-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: metal binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:E E E DClick to see conserved feature residue pattern help
Evidence:
  • Structure:2Q73; Vibrio dat 722 iMazG protein binds Mg2+, contacts at 4.0A
  • Comment:Most of members the NTP-PPase superfamily contain the well-conserved divalent ion-binding motif, EEED.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                 #  #                         #  #      
2Q73_A         3 LSELQSHIKEFDyap--------------eqSEHYFFKLIEEVGELSESIRKgksgqp-tldelKGSVAEELYDVLYYVC 67  Vibrio sp. DAT722
YP_003164817  13 LKEVQYLIKQIEkgtlgkrkrektpqerkenGQRLVLKLIEEFGELAENIRKnvryd---gkniKGTIEEEVFDVFYYII 89  Leptotrichia bu...
ZP_02868947   10 LKEVQYLIKRIEkgtldesgdkenlqqkrenGQRLVLKLIEEFGELAENIRKnvrfd---geniKGTIEEEVFDVFYYVI 86  candidate divis...
ZP_01112828    4 LKELQAHVAQVDqlp--------------eaDTGYFLKLIEEVGELSEAIRHgksgqp-efdtlKGSIAEELVDVFYYTL 68  Reinekea sp. ME...
ZP_03801255    5 IEELQEYLFDHYkng--------------giDQSLFMKLVEEIGEVAEVLNKkagrksvgqedlQTQLGNELADVVHYTI 70  Coprococcus com...
YP_004478861  14 IKNYQDYLKSVYqfh--------------kgDQGLFIKLVEEVGEVAQVLNIqngrks-svinpTEALAEELSDIIHYSI 78  Streptococcus p...
YP_004478202   3 TLTFNNYTKYLSevyq-----------nhngQMGLFLKLIEEVGEVAEELYKtpn-------lnKENLGKELADVIHYTL 64  Streptococcus p...
2Q73_B         3 LSELQSHIKEFDyap--------------eqSEHYFFKLIEEVGELSESIRKgksgqp-tldelKGSVAEELYDVLYYVC 67  Vibrio sp. DAT722
Feature 1                                 
2Q73_A        68 ALANIHGVNLEKTHELKEVLNKVKY 92  Vibrio sp. DAT722
YP_003164817  90 AIANDYEIDLEKIFYIKDEVNEIKY 114 Leptotrichia buccalis DSM 1135
ZP_02868947   87 AIANDYGIDLEKIFYIKDELNKVKY 111 candidate division TM7 single-cell isolate TM7a
ZP_01112828   69 ALANQYGVNLERSFELKEAHNRIRY 93  Reinekea sp. MED297
ZP_03801255   71 AIAALNGIDMNDIILSKDKDASIKY 95  Coprococcus comes ATCC 27758
YP_004478861  79 AIAAINNIDLESAILEKDEKASLKY 103 Streptococcus parauberis KCTC 11537
YP_004478202  65 AIASMNNIDIERVIINKDKEASIKY 89  Streptococcus parauberis KCTC 11537
2Q73_B        68 ALANIHGVNLEKTHELKEVLNKVKY 92  Vibrio sp. DAT722

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