NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1887632593|ref|WP_182184620|]
View 

MULTISPECIES: MazG nucleotide pyrophosphohydrolase domain-containing protein [unclassified Colwellia]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase family protein( domain architecture ID 96940)

nucleoside triphosphate (NTP) pyrophosphohydrolase family protein may hydrolyze the alpha-beta phosphodiester bond of canonical NTPs into monophosphate derivatives and pyrophosphate, similar to Deinococcus radiodurans DR2231 with specific dUTPase activity

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NTP-PPase super family cl16941
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 3-88 8.12e-13

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This superfamily contains enzymes that hydrolyze the alpha-beta phosphodiester bond of all canonical NTPs into monophosphate derivatives and pyrophosphate (PPi). Divalent ions, such as Mg2+ ion(s), are essential to activate a proposed water nucleophile and stabilize the charged intermediates to facilitate catalysis. These enzymes share a conserved divalent ion-binding motif EXX[E/D] in their active sites. They also share a highly conserved four-helix bundle, where one face forms the active site, while the other participates in oligomer assembly. The four-helix bundle consists of two central antiparallel alpha-helices that can be contained within a single protomer or form upon dimerization. The superfamily members include dimeric dUTP pyrophosphatases (dUTPases; EC 3.6.1.23), the nonspecific NTP-PPase MazG proteins, HisE-encoded phosphoribosyl ATP pyrophosphohydolase (PRA-PH), fungal histidine biosynthesis trifunctional proteins, and several uncharacterized protein families.


The actual alignment was detected with superfamily member cd11542:

Pssm-ID: 473051  Cd Length: 99  Bit Score: 58.49  E-value: 8.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887632593  3 INKIAEQNYDWVERMGWHNKTTL------EALALVASEVGEAINECR-GEKPT-----DNFKEELADIVLRVLDIAHWQG 70
Cdd:cd11542    1 INELVDEAHENAVAHGWWDDPRTgnnnfgELLMLIHSEVSEALEGLRkGLMDDklphrPMIEVELADAVIRIFDTAGGLG 80

                         90
                 ....*....|....*...
gi 1887632593 71 INIEQELLAKMKKNEQRG 88
Cdd:cd11542   81 IDLEGAIAEKMAYNKNRP 98
 
Name Accession Description Interval E-value
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 3-88 8.12e-13

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212149  Cd Length: 99  Bit Score: 58.49  E-value: 8.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887632593  3 INKIAEQNYDWVERMGWHNKTTL------EALALVASEVGEAINECR-GEKPT-----DNFKEELADIVLRVLDIAHWQG 70
Cdd:cd11542    1 INELVDEAHENAVAHGWWDDPRTgnnnfgELLMLIHSEVSEALEGLRkGLMDDklphrPMIEVELADAVIRIFDTAGGLG 80

                         90
                 ....*....|....*...
gi 1887632593 71 INIEQELLAKMKKNEQRG 88
Cdd:cd11542   81 IDLEGAIAEKMAYNKNRP 98
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
12-87 6.31e-10

NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];


Pssm-ID: 441300  Cd Length: 95  Bit Score: 50.96  E-value: 6.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887632593 12 DWVERMGWHNKTTLEALALV----ASEVGEAINECRGEKPT------DNFKEELADIVLRVLDIAHWQGINIEQELLAKM 81
Cdd:COG1694    9 AFIKERGWGQYHSPKNLAAAlteeVGELAEAFQWLTGEQSKkdpekkEELAEELADVLIYLLCLANQLGIDLEEAFEEKM 88


                 ....*.
gi 1887632593 82 KKNEQR 87
Cdd:COG1694   89 EKNEKR 94
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 28-87 4.21e-04

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 35.65  E-value: 4.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887632593 28 LALVASEVGEAINECRGEKPtDNFKEELADIVLRVLDIAHW----QGINIEQELLAKMKKNEQR 87
Cdd:pfam03819  7 LPYLIEEVYEVAEAIEKEDL-DNLEEELGDVLLQVLFHANIaeeeGGFDLEDVFQRILEKLIRR 69
 
Name Accession Description Interval E-value
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 3-88 8.12e-13

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212149  Cd Length: 99  Bit Score: 58.49  E-value: 8.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887632593  3 INKIAEQNYDWVERMGWHNKTTL------EALALVASEVGEAINECR-GEKPT-----DNFKEELADIVLRVLDIAHWQG 70
Cdd:cd11542    1 INELVDEAHENAVAHGWWDDPRTgnnnfgELLMLIHSEVSEALEGLRkGLMDDklphrPMIEVELADAVIRIFDTAGGLG 80

                         90
                 ....*....|....*...
gi 1887632593 71 INIEQELLAKMKKNEQRG 88
Cdd:cd11542   81 IDLEGAIAEKMAYNKNRP 98
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
12-87 6.31e-10

NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];


Pssm-ID: 441300  Cd Length: 95  Bit Score: 50.96  E-value: 6.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887632593 12 DWVERMGWHNKTTLEALALV----ASEVGEAINECRGEKPT------DNFKEELADIVLRVLDIAHWQGINIEQELLAKM 81
Cdd:COG1694    9 AFIKERGWGQYHSPKNLAAAlteeVGELAEAFQWLTGEQSKkdpekkEELAEELADVLIYLLCLANQLGIDLEEAFEEKM 88


                 ....*.
gi 1887632593 82 KKNEQR 87
Cdd:COG1694   89 EKNEKR 94
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 25-87 1.52e-05

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs; This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, BsYpjD contains a single MazG-like domain.


Pssm-ID: 212138  Cd Length: 93  Bit Score: 39.60  E-value: 1.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887632593 25 LEALALVASEVGE---AINECRGEKPTD-----NFKEELADIVLRVLDIAHWQGINIEQELLAKMKKNEQR 87
Cdd:cd11531   22 LSNLARLTEEVGElarEINHRYGEKPKPgedegELEEELADILFVLTCLANQLGIDLEEAFKRTMEKKETR 92
NTP-PPase_RS21-C6_like cd11537
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ...
 12-84 3.34e-05

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse RS21-C6 protein and its homologs; RS21-C6 proteins, highly expressed in all vertebrate genomes and green plants, act as house-cleaning enzymes, removing 5-methyl dCTP (m5dCTP) in order to prevent gene silencing. They show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, RS21-C6 contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. Divalent ions, such as Mg2+, are required for its pyrophosphatase activity. This family also includes a pyrophosphatase from Archaeoglobus fulgidus (Af1178). Although its biological role remains unclear, Af1178 shows significant sequence similarity to the mouse RS21-C6 protein.


Pssm-ID: 212144  Cd Length: 90  Bit Score: 38.66  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887632593 12 DWVERMGWHNKTTLEALAL-VASEVGE-----------AINECRGEKPTDNFKEELADIVLRVLDIAHWQGINIEQELLA 79
Cdd:cd11537    6 EFRDERDWDQFHTPKNLAMaLSIEAGElleifqwkseeESELVWDPEKREHVGEELADVLIYLLRLADKLGIDLAEAVLE 85


                 ....*
gi 1887632593 80 KMKKN 84
Cdd:cd11537   86 KLEKN 90
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 28-87 4.21e-04

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 35.65  E-value: 4.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887632593 28 LALVASEVGEAINECRGEKPtDNFKEELADIVLRVLDIAHW----QGINIEQELLAKMKKNEQR 87
Cdd:pfam03819  7 LPYLIEEVYEVAEAIEKEDL-DNLEEELGDVLLQVLFHANIaeeeGGFDLEDVFQRILEKLIRR 69
NTP-PPase_SsMazG cd11535
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus ...
 34-82 4.48e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus solfataricus (Ss) and its homologs from archaea and bacteria; This family includes a MazG-like protein from Sulfolobus solfataricus (SsMazG) and its homologs from archaea and bacteria. Although its biological roles remain still unclear, SsMazG shows significant sequence similarity to the NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, SsMazG contains a single MazG-like domain. It is predicted that SsMazG might participate in house-cleaning by preventing incorporation of the oxidation product 2-oxo-(d)ATP (iso-dGTP), a mutagenic derivative of ATP, into DNA.


Pssm-ID: 212142  Cd Length: 76  Bit Score: 35.65  E-value: 4.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 1887632593 34 EVGEAINECRGEKPtDNFKEELADIVLRVLDIAHWQGINIEQELLAKMK 82
Cdd:cd11535   29 EVGELAKALRKNDG-ENIEEELADVFAWLLSLANLLGIDLEEAFKKKYP 76
NTP-PPase_iMazG cd11536
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 34-85 4.52e-04

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.


Pssm-ID: 212143  Cd Length: 90  Bit Score: 35.88  E-value: 4.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1887632593 34 EVGEAINECRGEKPT-DNFK----EELADIVLRVLDIAHWQGINIEQELLAKMKKNE 85
Cdd:cd11536   31 ELAEVIRKGKSGQPTgDNLKgslaEELADVFYYTIAIANINGIDLEKIIELKDELNS 87
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 12-68 3.44e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This superfamily contains enzymes that hydrolyze the alpha-beta phosphodiester bond of all canonical NTPs into monophosphate derivatives and pyrophosphate (PPi). Divalent ions, such as Mg2+ ion(s), are essential to activate a proposed water nucleophile and stabilize the charged intermediates to facilitate catalysis. These enzymes share a conserved divalent ion-binding motif EXX[E/D] in their active sites. They also share a highly conserved four-helix bundle, where one face forms the active site, while the other participates in oligomer assembly. The four-helix bundle consists of two central antiparallel alpha-helices that can be contained within a single protomer or form upon dimerization. The superfamily members include dimeric dUTP pyrophosphatases (dUTPases; EC 3.6.1.23), the nonspecific NTP-PPase MazG proteins, HisE-encoded phosphoribosyl ATP pyrophosphohydolase (PRA-PH), fungal histidine biosynthesis trifunctional proteins, and several uncharacterized protein families.


Pssm-ID: 212133  Cd Length: 72  Bit Score: 33.13  E-value: 3.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887632593 12 DWVERMGWHNKTTLEALAL-VASEVGEAINECRGEKPT--------DNFKEELADIVLRVLDIAHW 68
Cdd:cd11523    6 EFRRERGWDKEEGPETRALkLAEEVGELAEAIRKEEGYgrssaedkENLAEELADVLWNLLILANK 71
 
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