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Conserved domains on  [gi|961939950|ref|XP_014866243|]
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PREDICTED: dCTP pyrophosphatase 1 [Poecilia mexicana]

Protein Classification

nucleotide pyrophosphohydrolase( domain architecture ID 10183967)

nucleotide pyrophosphohydrolase similar to mammalian dCTP diphosphatase, which hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTP-PPase_RS21-C6_like cd11537
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ...
 65-155 6.90e-43

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: 138.04  E-value: 6.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  65 RRMQADFTDERDWNKFHQPRNLLLAMVGEVGEVAELFQWRGEVAEGLPdWTESEREQLAHELSDVLIYLVELAEKCRVDL 144
Cdd:cd11537    1 RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESELV-WDPEKREHVGEELADVLIYLLRLADKLGIDL 79

                         90
                 ....*....|.
gi 961939950 145 PQAVLRKMALN 155
Cdd:cd11537   80 AEAVLEKLEKN 90
 
Name Accession Description Interval E-value
NTP-PPase_RS21-C6_like cd11537
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ...
 65-155 6.90e-43

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: 138.04  E-value: 6.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  65 RRMQADFTDERDWNKFHQPRNLLLAMVGEVGEVAELFQWRGEVAEGLPdWTESEREQLAHELSDVLIYLVELAEKCRVDL 144
Cdd:cd11537    1 RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESELV-WDPEKREHVGEELADVLIYLLRLADKLGIDL 79

                         90
                 ....*....|.
gi 961939950 145 PQAVLRKMALN 155
Cdd:cd11537   80 AEAVLEKLEKN 90
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
62-159 1.84e-28

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 101.42  E-value: 1.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  62 EDIRRMQADFTDERDWNKFHQPRNLLLAMVGEVGEVAELFQWRgevaEGLPDWTESE-REQLAHELSDVLIYLVELAEKC 140
Cdd:COG1694    1 KELQKRVRAFIKERGWGQYHSPKNLAAALTEEVGELAEAFQWL----TGEQSKKDPEkKEELAEELADVLIYLLCLANQL 76

                         90
                 ....*....|....*....
gi 961939950 141 RVDLPQAVLRKMALNRLKY 159
Cdd:COG1694   77 GIDLEEAFEEKMEKNEKRY 95
MazG-like pfam12643
MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This ...
 93-173 1.48e-09

MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This suggests that these proteins are enzymes that catalyze a related reaction.


Pssm-ID: 463653  Cd Length: 85  Bit Score: 52.19  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950   93 EVGEVAELFQWrGEVAEGLPDWTESEREQLAHELSDVLIYLVELAEKCRVDlPQAVLRKMALNRLKYPASKVHGSAKKYT 172
Cdd:pfam12643   6 KAIELLKAELL-KSVAELFKALLKGSQEAILDELADVIIYCYLLARRLGID-FDEIDEKLKKKLKKYPIEEGHGLEKWYG 83


                  .
gi 961939950  173 E 173
Cdd:pfam12643  84 D 84
 
Name Accession Description Interval E-value
NTP-PPase_RS21-C6_like cd11537
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ...
 65-155 6.90e-43

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: 138.04  E-value: 6.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  65 RRMQADFTDERDWNKFHQPRNLLLAMVGEVGEVAELFQWRGEVAEGLPdWTESEREQLAHELSDVLIYLVELAEKCRVDL 144
Cdd:cd11537    1 RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESELV-WDPEKREHVGEELADVLIYLLRLADKLGIDL 79

                         90
                 ....*....|.
gi 961939950 145 PQAVLRKMALN 155
Cdd:cd11537   80 AEAVLEKLEKN 90
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
62-159 1.84e-28

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 101.42  E-value: 1.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  62 EDIRRMQADFTDERDWNKFHQPRNLLLAMVGEVGEVAELFQWRgevaEGLPDWTESE-REQLAHELSDVLIYLVELAEKC 140
Cdd:COG1694    1 KELQKRVRAFIKERGWGQYHSPKNLAAALTEEVGELAEAFQWL----TGEQSKKDPEkKEELAEELADVLIYLLCLANQL 76

                         90
                 ....*....|....*....
gi 961939950 141 RVDLPQAVLRKMALNRLKY 159
Cdd:COG1694   77 GIDLEEAFEEKMEKNEKRY 95
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 68-139 1.76e-11

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: 57.01  E-value: 1.76e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961939950  68 QADFTDERDWNKFHQPRNLLLAMVGEVGEVAELFQWRgevaEGLPDWTESEREQLAHELSDVLIYLVELAEK 139
Cdd:cd11523    4 IKEFRRERGWDKEEGPETRALKLAEEVGELAEAIRKE----EGYGRSSAEDKENLAEELADVLWNLLILANK 71
NTP-PPase_SsMazG cd11535
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus ...
 74-153 1.36e-10

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: 54.52  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  74 ERDWNKfhqpRNLLLAMVGEVGEVAELFQ-WRGEvaeglpdwtesEREQLAHELSDVLIYLVELAEKCRVDLPQAVLRKM 152
Cdd:cd11535   11 ERDFNK----RGVEKTFLWLVEEVGELAKaLRKN-----------DGENIEEELADVFAWLLSLANLLGIDLEEAFKKKY 75


                 .
gi 961939950 153 A 153
Cdd:cd11535   76 P 76
MazG-like pfam12643
MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This ...
 93-173 1.48e-09

MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This suggests that these proteins are enzymes that catalyze a related reaction.


Pssm-ID: 463653  Cd Length: 85  Bit Score: 52.19  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950   93 EVGEVAELFQWrGEVAEGLPDWTESEREQLAHELSDVLIYLVELAEKCRVDlPQAVLRKMALNRLKYPASKVHGSAKKYT 172
Cdd:pfam12643   6 KAIELLKAELL-KSVAELFKALLKGSQEAILDELADVIIYCYLLARRLGID-FDEIDEKLKKKLKKYPIEEGHGLEKWYG 83


                  .
gi 961939950  173 E 173
Cdd:pfam12643  84 D 84
NTP-PPase_iMazG cd11536
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 86-159 2.50e-07

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: 46.28  E-value: 2.50e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961939950  86 LLLAMVGEVGEVAE-LFQWRGEVAEGlpdwtESEREQLAHELSDVLIYLVELAEKCRVDLPQAVLRKMALNRLKY 159
Cdd:cd11536   21 LFLKLIEEVGELAEvIRKGKSGQPTG-----DNLKGSLAEELADVFYYTIAIANINGIDLEKIIELKDELNSIKY 90
NTP-PPase_u6 cd11543
Nucleoside Triphosphate Pyrophosphohydrolase EC 3.6.1.8) MazG-like domain found in a group of ...
 86-151 1.42e-05

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.


Pssm-ID: 212150  Cd Length: 87  Bit Score: 41.53  E-value: 1.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961939950  86 LLLAMVGEVGEVAELFQwrgeVAEGLPDwTESEREQLAHELSDVLIYLVELAEKCRVDLPQAVLRK 151
Cdd:cd11543   27 DALGFLGDVGDVGRLVM----AQQGRWP-IDGVDAELEHKLAECLWWVLVLADRLDVDILETFLTR 87
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 73-156 1.43e-04

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: 39.23  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961939950  73 DERDWNKFHQprnLLLAMVGEVGEVAElfqwrgEVAEGLPDWTESEREQLAHELSDVLIYLVELAEKCRVDLPQAVLRKM 152
Cdd:cd11542   21 PRTGNNNFGE---LLMLIHSEVSEALE------GLRKGLMDDKLPHRPMIEVELADAVIRIFDTAGGLGIDLEGAIAEKM 91


                 ....
gi 961939950 153 ALNR 156
Cdd:cd11542   92 AYNK 95
NTP-PPase_u4 cd11541
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 85-144 3.05e-04

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: 212148  Cd Length: 91  Bit Score: 37.98  E-value: 3.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961939950  85 NLLLAMVGEVGEVAELFQ--WRGEVAEGlpdwtesEREQLAHELSDVLIYLVELAEKCRVDL 144
Cdd:cd11541   22 NALLGLFGEVGEVADAIKkhIRDGHAPL-------DKEALAEELGDVLWYLAALANVLGISL 76
 
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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