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Conserved domains on  [gi|1256375933|gb|PEB08973|]
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nucleotide pyrophosphohydrolase [Bacillus cereus]

Protein Classification

nucleotide pyrophosphohydrolase( domain architecture ID 10183933)

nucleotide pyrophosphohydrolase similar to Bacillus-conserved MazG, a nucleoside triphosphate (NTP) pyrophosphohydrolase that prefers adenosine triphosphate as a substrate among canonical NTPs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 7-100 1.27e-46

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: 144.76  E-value: 1.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933   7 KDMQKEVDAYIGQFKEGYFSPLAMMARLTEEMGELAREVNHYYGEKPKKtTETERSIEEELGDVLFVMICMANSLNIDLE 86
Cdd:cd11531     1 KELQQEVDEWISQFEEGYFSPLSNLARLTEEVGELAREINHRYGEKPKP-GEDEGELEEELADILFVLTCLANQLGIDLE 79

                          90
                  ....*....|....
gi 1256375933  87 TAHNIVMNKFNTRD 100
Cdd:cd11531    80 EAFKRTMEKKETRD 93
 
Name Accession Description Interval E-value
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 7-100 1.27e-46

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: 144.76  E-value: 1.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933   7 KDMQKEVDAYIGQFKEGYFSPLAMMARLTEEMGELAREVNHYYGEKPKKtTETERSIEEELGDVLFVMICMANSLNIDLE 86
Cdd:cd11531     1 KELQQEVDEWISQFEEGYFSPLSNLARLTEEVGELAREINHRYGEKPKP-GEDEGELEEELADILFVLTCLANQLGIDLE 79

                          90
                  ....*....|....
gi 1256375933  87 TAHNIVMNKFNTRD 100
Cdd:cd11531    80 EAFKRTMEKKETRD 93
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
7-100 4.82e-36

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 117.99  E-value: 4.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933   7 KDMQKEVDAYIGQFKEG-YFSPLAMMARLTEEMGELAREVNHYYGEKPKKTTETERSIEEELGDVLFVMICMANSLNIDL 85
Cdd:COG1694     1 KELQKRVRAFIKERGWGqYHSPKNLAAALTEEVGELAEAFQWLTGEQSKKDPEKKEELAEELADVLIYLLCLANQLGIDL 80

                          90
                  ....*....|....*
gi 1256375933  86 ETAHNIVMNKFNTRD 100
Cdd:COG1694    81 EEAFEEKMEKNEKRY 95
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 25-104 1.36e-14

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: 63.00  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933  25 FSPLAMMARLTEEMGELAREVNHyygekpkkttETERSIEEELGDVLFVMICMANSLN----IDLETAHNIVMNKFNTRD 100
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEK----------EDLDNLEEELGDVLLQVLFHANIAEeeggFDLEDVFQRILEKLIRRH 70


                  ....
gi 1256375933 101 KDRW 104
Cdd:pfam03819  71 PHVF 74
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 26-88 3.18e-06

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 44.00  E-value: 3.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256375933  26 SPLAMMARLTEEMGELAREVNhyygekpkktTETERSIEEELGDVLFVMICMANSLNIDLETA 88
Cdd:PRK09562  163 SLEPVLDKVEEEIDELKEALA----------QGDQAKIEEEFGDLLFALVNLARHLGIDPEAA 215
 
Name Accession Description Interval E-value
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 7-100 1.27e-46

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: 144.76  E-value: 1.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933   7 KDMQKEVDAYIGQFKEGYFSPLAMMARLTEEMGELAREVNHYYGEKPKKtTETERSIEEELGDVLFVMICMANSLNIDLE 86
Cdd:cd11531     1 KELQQEVDEWISQFEEGYFSPLSNLARLTEEVGELAREINHRYGEKPKP-GEDEGELEEELADILFVLTCLANQLGIDLE 79

                          90
                  ....*....|....
gi 1256375933  87 TAHNIVMNKFNTRD 100
Cdd:cd11531    80 EAFKRTMEKKETRD 93
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
7-100 4.82e-36

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 117.99  E-value: 4.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933   7 KDMQKEVDAYIGQFKEG-YFSPLAMMARLTEEMGELAREVNHYYGEKPKKTTETERSIEEELGDVLFVMICMANSLNIDL 85
Cdd:COG1694     1 KELQKRVRAFIKERGWGqYHSPKNLAAALTEEVGELAEAFQWLTGEQSKKDPEKKEELAEELADVLIYLLCLANQLGIDL 80

                          90
                  ....*....|....*
gi 1256375933  86 ETAHNIVMNKFNTRD 100
Cdd:COG1694    81 EEAFEEKMEKNEKRY 95
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 25-104 1.36e-14

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: 63.00  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933  25 FSPLAMMARLTEEMGELAREVNHyygekpkkttETERSIEEELGDVLFVMICMANSLN----IDLETAHNIVMNKFNTRD 100
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEK----------EDLDNLEEELGDVLLQVLFHANIAEeeggFDLEDVFQRILEKLIRRH 70


                  ....
gi 1256375933 101 KDRW 104
Cdd:pfam03819  71 PHVF 74
NTP-PPase_iMazG cd11536
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 11-89 1.19e-10

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: 53.60  E-value: 1.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256375933  11 KEVDAYIGQFKEGYFSPLAMMARLTEEMGELAREVNHYYGEKPKKTTETErSIEEELGDVLFVMICMANSLNIDLETAH 89
Cdd:cd11536     2 KELQYYIKQVDKGPEGDQGLFLKLIEEVGELAEVIRKGKSGQPTGDNLKG-SLAEELADVFYYTIAIANINGIDLEKII 79
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 24-81 7.85e-10

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: 50.85  E-value: 7.85e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1256375933  24 YFSPLAMMARLTEEMGELAREVNHYYGEKPKKtTETERSIEEELGDVLFVMICMANSL 81
Cdd:cd11523    16 EEGPETRALKLAEEVGELAEAIRKEEGYGRSS-AEDKENLAEELADVLWNLLILANKL 72
NTP-PPase_SsMazG cd11535
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus ...
 9-88 4.37e-07

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: 43.74  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256375933   9 MQKEVDA-YI--GQFKEGyfsPLAMMARLTEEMGELAREVNHYYGEkpkktteterSIEEELGDVLFVMICMANSLNIDL 85
Cdd:cd11535     1 LQKLIREnYGerDFNKRG---VEKTFLWLVEEVGELAKALRKNDGE----------NIEEELADVFAWLLSLANLLGIDL 67


                  ...
gi 1256375933  86 ETA 88
Cdd:cd11535    68 EEA 70
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 26-88 3.18e-06

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 44.00  E-value: 3.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256375933  26 SPLAMMARLTEEMGELAREVNhyygekpkktTETERSIEEELGDVLFVMICMANSLNIDLETA 88
Cdd:PRK09562  163 SLEPVLDKVEEEIDELKEALA----------QGDQAKIEEEFGDLLFALVNLARHLGIDPEAA 215
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 31-88 2.58e-05

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress.


Pssm-ID: 212136  Cd Length: 116  Bit Score: 40.15  E-value: 2.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1256375933  31 MARLTEEMGELAREVNHYYGEKpkkttetersIEEELGDVLFVMICMANSLNIDLETA 88
Cdd:cd11529    27 LDKVEEELAELKEALASGDKEE----------IEEELGDLLFSLVNLARFLGVDPEEA 74
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 31-99 3.83e-05

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 40.86  E-value: 3.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256375933  31 MARLTEEMGELAREVNHyyGEKPKkttetersIEEELGDVLFVMICMANSLNIDLETAHNIVMNKFNTR 99
Cdd:COG3956   174 LDKVEEELAELKEALAS--GDQEA--------IEEELGDLLFALVNLARHLGIDPEEALRRANRKFERR 232
NTP-PPase_u3 cd11540
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 27-87 1.19e-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 and archaea, 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: 212147  Cd Length: 76  Bit Score: 37.61  E-value: 1.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256375933  27 PLAMMARLTEEMGELAREVNHYYGEKpkkttetersIEEELGDVLFVMICMANSLNIDLET 87
Cdd:cd11540    21 PRKQLLKLVEEVGELSEAIAKNKQEE----------IKDSIGDVLVVLIILCAQLGLSLEE 71
NTP-PPase_u4 cd11541
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 34-92 1.27e-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: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256375933  34 LTEEMGELAREV-NHYYGekpKKTTETERSIEEELGDVLFVMICMANSLNIDLET--AHNIV 92
Cdd:cd11541    27 LFGEVGEVADAIkKHIRD---GHAPLDKEALAEELGDVLWYLAALANVLGISLEEiaEANIA 85
NTP-PPase_Af0060_like cd11533
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 25-81 3.84e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in uncharacterized protein from Archaeoglobus fulgidus (Af0060) and its bacterial homologs; This family includes an uncharacterized protein from Archaeoglobus fulgidus (Af0060) and its homologs from bacteria. Although its biological role remains unclear, Af0060 shows 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: 212140  Cd Length: 75  Bit Score: 36.17  E-value: 3.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1256375933  25 FSPLAMMARLTEEMGELAREVNHYYGEKPKKTTETERSIEEELGDVLFVMICMANSL 81
Cdd:cd11533    19 ETLELRVLKLGEEVGELAEAILGARGQNPRGKSHTWDDVREELLDVAQVALLALEKL 75
NTP-PPase_u1 cd11538
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 31-88 2.38e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria; 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: 212145  Cd Length: 97  Bit Score: 34.60  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256375933  31 MARLTEEMGELAREVNHYYGE---KPKKTTETERSIEEELGDVLFVMICMANSLNIDLETA 88
Cdd:cd11538    29 LLKLQEEVGELTQAYLRLTGRgrrKGRSEDELRQDLEDELADVLGMLLLFARRFGIDLEAA 89
NTP-PPase_RS21-C6_like cd11537
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ...
 63-88 3.76e-03

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: 34.03  E-value: 3.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 1256375933  63 IEEELGDVLFVMICMANSLNIDLETA 88
Cdd:cd11537    57 VGEELADVLIYLLRLADKLGIDLAEA 82
 
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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