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Conserved domains on  [gi|13129100|ref|NP_077001|]
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dCTP pyrophosphatase 1 [Homo sapiens]

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 ...
 35-125 3.80e-44

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: 140.73  E-value: 3.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  35 RRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGpQGWSPRERAALQEELSDVLIYLVALAARCRVDL 114
Cdd:cd11537   1 RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESE-LVWDPEKREHVGEELADVLIYLLRLADKLGIDL 79

                        90
                ....*....|.
gi 13129100 115 PLAVLSKMDIN 125
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 ...
 35-125 3.80e-44

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: 140.73  E-value: 3.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  35 RRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGpQGWSPRERAALQEELSDVLIYLVALAARCRVDL 114
Cdd:cd11537   1 RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESE-LVWDPEKREHVGEELADVLIYLLRLADKLGIDL 79

                        90
                ....*....|.
gi 13129100 115 PLAVLSKMDIN 125
Cdd:cd11537  80 AEAVLEKLEKN 90
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
32-129 1.37e-33

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 114.14  E-value: 1.37e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  32 EDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPqgwSPRERAALQEELSDVLIYLVALAARCR 111
Cdd:COG1694   1 KELQKRVRAFIKERGWGQYHSPKNLAAALTEEVGELAEAFQWLTGEQSKK---DPEKKEELAEELADVLIYLLCLANQLG 77

                        90
                ....*....|....*...
gi 13129100 112 VDLPLAVLSKMDINRRRY 129
Cdd:COG1694  78 IDLEEAFEEKMEKNEKRY 95
MazG-like pfam12643
MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This ...
 63-144 9.44e-11

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: 55.27  E-value: 9.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100    63 EVGELAELFQWKTDGEpGPQGWSPRERAALQEELSDVLIYLVALAARCRVDlPLAVLSKMDINRRRYPAHLARSSSRKYT 142
Cdd:pfam12643   6 KAIELLKAELLKSVAE-LFKALLKGSQEAILDELADVIIYCYLLARRLGID-FDEIDEKLKKKLKKYPIEEGHGLEKWYG 83


                  ..
gi 13129100   143 EL 144
Cdd:pfam12643  84 DL 85
 
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 ...
 35-125 3.80e-44

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: 140.73  E-value: 3.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  35 RRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGpQGWSPRERAALQEELSDVLIYLVALAARCRVDL 114
Cdd:cd11537   1 RQALREFRDERDWDQFHTPKNLAMALSIEAGELLEIFQWKSEEESE-LVWDPEKREHVGEELADVLIYLLRLADKLGIDL 79

                        90
                ....*....|.
gi 13129100 115 PLAVLSKMDIN 125
Cdd:cd11537  80 AEAVLEKLEKN 90
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
32-129 1.37e-33

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 114.14  E-value: 1.37e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  32 EDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPqgwSPRERAALQEELSDVLIYLVALAARCR 111
Cdd:COG1694   1 KELQKRVRAFIKERGWGQYHSPKNLAAALTEEVGELAEAFQWLTGEQSKK---DPEKKEELAEELADVLIYLLCLANQLG 77

                        90
                ....*....|....*...
gi 13129100 112 VDLPLAVLSKMDINRRRY 129
Cdd:COG1694  78 IDLEEAFEEKMEKNEKRY 95
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 36-107 7.33e-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.


Pssm-ID: 212133  Cd Length: 72  Bit Score: 60.48  E-value: 7.33e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13129100  36 RLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPQGwsprERAALQEELSDVLIYLVALA 107
Cdd:cd11523   2 ERIKEFRRERGWDKEEGPETRALKLAEEVGELAEAIRKEEGYGRSSAE----DKENLAEELADVLWNLLILA 69
NTP-PPase_SsMazG cd11535
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus ...
 36-123 7.13e-12

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: 57.99  E-value: 7.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  36 RLHAEFAAERDWEQFHQPRNLLLaLVGEVGELAElfqwktdgepgpqGWSPRERAALQEELSDVLIYLVALAARCRVDLP 115
Cdd:cd11535   3 KLIRENYGERDFNKRGVEKTFLW-LVEEVGELAK-------------ALRKNDGENIEEELADVFAWLLSLANLLGIDLE 68


                ....*...
gi 13129100 116 LAVLSKMD 123
Cdd:cd11535  69 EAFKKKYP 76
MazG-like pfam12643
MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This ...
 63-144 9.44e-11

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: 55.27  E-value: 9.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100    63 EVGELAELFQWKTDGEpGPQGWSPRERAALQEELSDVLIYLVALAARCRVDlPLAVLSKMDINRRRYPAHLARSSSRKYT 142
Cdd:pfam12643   6 KAIELLKAELLKSVAE-LFKALLKGSQEAILDELADVIIYCYLLARRLGID-FDEIDEKLKKKLKKYPIEEGHGLEKWYG 83


                  ..
gi 13129100   143 EL 144
Cdd:pfam12643  84 DL 85
NTP-PPase_iMazG cd11536
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 45-129 7.76e-09

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: 50.52  E-value: 7.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  45 RDWEQFH-QPRNLLLALVGEVGELAELFQWKTDGEPGpqGWSPREraALQEELSDVLIYLVALAARCRVDLPLAVLSKMD 123
Cdd:cd11536   9 KQVDKGPeGDQGLFLKLIEEVGELAEVIRKGKSGQPT--GDNLKG--SLAEELADVFYYTIAIANINGIDLEKIIELKDE 84


                ....*.
gi 13129100 124 INRRRY 129
Cdd:cd11536  85 LNSIKY 90
NTP-PPase_u4 cd11541
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 55-114 1.05e-07

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: 47.22  E-value: 1.05e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  55 NLLLALVGEVGELAELFQWKTDgepgpQGWSPRERAALQEELSDVLIYLVALAARCRVDL 114
Cdd:cd11541  22 NALLGLFGEVGEVADAIKKHIR-----DGHAPLDKEALAEELGDVLWYLAALANVLGISL 76
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 47-128 1.06e-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: 39.61  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  47 WEQFHQPRN---LLLALVgeVGELAElfqwKTDGE-PGPQGWSPRERAALQEELSDVLIYLVALAARCRVDLPLAVLSKM 122
Cdd:cd11542  18 WDDPRTGNNnfgELLMLI--HSEVSE----ALEGLrKGLMDDKLPHRPMIEVELADAVIRIFDTAGGLGIDLEGAIAEKM 91


                ....*.
gi 13129100 123 DINRRR 128
Cdd:cd11542  92 AYNKNR 97
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 53-129 5.65e-04

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: 37.29  E-value: 5.65e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13129100  53 PRNLLLALVGEVGELAELFQwKTDGEPGPQGWSPREraaLQEELSDVLIYLVALAARCRVDLPLAVLSKMDINRRRY 129
Cdd:cd11531  21 PLSNLARLTEEVGELAREIN-HRYGEKPKPGEDEGE---LEEELADILFVLTCLANQLGIDLEEAFKRTMEKKETRD 93
NTP-PPase_u6 cd11543
Nucleoside Triphosphate Pyrophosphohydrolase EC 3.6.1.8) MazG-like domain found in a group of ...
 33-121 2.33e-03

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: 35.37  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  33 DIRRLHAEFAAERdWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPQGwspreRAALQEELSDVLIYLVALAARCRV 112
Cdd:cd11543   5 AIRALYHQLERKN-HGREWTVEEDALGFLGDVGDVGRLVMAQQGRWPIDGV-----DAELEHKLAECLWWVLVLADRLDV 78


                ....*....
gi 13129100 113 DLPLAVLSK 121
Cdd:cd11543  79 DILETFLTR 87
NTP-PPase_u1 cd11538
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 31-121 3.08e-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: 35.37  E-value: 3.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100  31 LEDIRRLHAE-FAAERD--WeqfhqprnLLLALVGEVGELAELFQwKTDGEPGPQGWSPRE-RAALQEELSDVLIYLVAL 106
Cdd:cd11538   8 VEAVSDIYAArFGIDRDddW--------YLLKLQEEVGELTQAYL-RLTGRGRRKGRSEDElRQDLEDELADVLGMLLLF 78

                        90
                ....*....|....*
gi 13129100 107 AARCRVDLPLAVLSK 121
Cdd:cd11538  79 ARRFGIDLEAAIERK 93
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 53-130 3.62e-03

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: 34.50  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129100    53 PRNLLLALVGEVGELAELFQWKtdgepgpqgwsprERAALQEELSDVLIYLVALAARCR----VDLPLAVLSKMDINRRR 128
Cdd:pfam03819   3 HETLLPYLIEEVYEVAEAIEKE-------------DLDNLEEELGDVLLQVLFHANIAEeeggFDLEDVFQRILEKLIRR 69


                  ..
gi 13129100   129 YP 130
Cdd:pfam03819  70 HP 71
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 54-128 7.13e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric 2-Deoxyuridine 5'-triphosphate nucleotidohydrolase and similar proteins; dUTPase (dUTP pyrophosphatase; EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate. It acts to ensure chromosomal integrity by reducing the effective ratio of dUTP/dTTP. Members in this family are dimeric dUTPases, such as those from Leishmania major, Trypanosoma cruzi, and Campylobacter jejuni, which differ from the monomeric and trimeric forms and adopt an all-alpha topology. A central four-helix bundle, consisting of two alpha-helices from the rigid domain and two helices from the mobile domain and connecting loops, form the active site in dimeric dUTPase-like proteins, requiring the presence of metal ion cofactors to hydrolyze both dUTP and dUDP.


Pssm-ID: 212134 [Multi-domain]  Cd Length: 94  Bit Score: 34.11  E-value: 7.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13129100  54 RNLLLALVGEVGELA---ELFQ-WKTDGEPgpqgwsprERAALQEELSDVLIYLVALAARcrvdlplAVLSKMDINRRR 128
Cdd:cd11527  26 KNKALALIVELAELAnetESFKyWKKNKPN--------DKEKILEELVDILHFLLSIALE-------LYIEKNKLNHKR 89
 
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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