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Conserved domains on  [gi|1883894125|ref|WP_181501149|]
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XTP/dITP diphosphatase [Methanococcus maripaludis]

Protein Classification

non-canonical purine NTP pyrophosphatase( domain architecture ID 10794072)

RdgB/HAM1 family pyrophosphatase that hydrolyzes non-canonical purine nucleotides to their respective monophosphates and prevents their incorporation into DNA

CATH:  3.90.950.10
EC:  3.6.1.-
Gene Ontology:  GO:0047429|GO:0009146|GO:0000166
PubMed:  17976651|22531138
SCOP:  4000518

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14821 PRK14821
XTP/dITP diphosphatase;
1-182 1.01e-108

XTP/dITP diphosphatase;


:

Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 308.03  E-value: 1.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEIILKEANCEIEQIEIPYAEVQ-GRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTY 79
Cdd:PRK14821    1 MKIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  80 SRFVQETIGNEGILKLLENETNRNAYFKTVIGYYDGDNIKLFTGIVKGTISTEIKDGGfGFAYDSIFIPDGKTKTFAEMT 159
Cdd:PRK14821   81 SAFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEKLFTGIVEGKIANEIRGKG-GFGYDPIFIPEGEEKTFAEMT 159

                         170       180
                  ....*....|....*....|...
gi 1883894125 160 TEEKSEISHRKRAFYELKNYLEN 182
Cdd:PRK14821  160 TEEKNKISHRKRAFDEFKEWLKE 182
 
Name Accession Description Interval E-value
PRK14821 PRK14821
XTP/dITP diphosphatase;
1-182 1.01e-108

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 308.03  E-value: 1.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEIILKEANCEIEQIEIPYAEVQ-GRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTY 79
Cdd:PRK14821    1 MKIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  80 SRFVQETIGNEGILKLLENETNRNAYFKTVIGYYDGDNIKLFTGIVKGTISTEIKDGGfGFAYDSIFIPDGKTKTFAEMT 159
Cdd:PRK14821   81 SAFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEKLFTGIVEGKIANEIRGKG-GFGYDPIFIPEGEEKTFAEMT 159

                         170       180
                  ....*....|....*....|...
gi 1883894125 160 TEEKSEISHRKRAFYELKNYLEN 182
Cdd:PRK14821  160 TEEKNKISHRKRAFDEFKEWLKE 182
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 2-182 2.49e-70

Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 211.07  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   2 KIYFATGNQNKVDEAEIILKEANCEIEQI-EIPYAEV--QGR-LEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPG 77
Cdd:COG0127     1 KLVFATGNAGKLREIRALLAPLGIEVVSLsDLGLPEPeeTGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  78 TYSRFVQ-----ETIGNEGILKLLEN-ETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIK-DGGFGfaYDSIFIPD 149
Cdd:COG0127    81 VYSARYAgegadDEANNEKLLKLLEGvDEDRRARFVCVLALADPDGePLVFEGEVEGEIAEEPRgEGGFG--YDPIFIPD 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1883894125 150 GKTKTFAEMTTEEKSEISHRKRAFYELKNYLEN 182
Cdd:COG0127   159 GYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 2-181 9.06e-67

non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272870 [Multi-domain]  Cd Length: 184  Bit Score: 202.21  E-value: 9.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   2 KIYFATGNQNKVDEAEIILKEANC-EIEQIEIPYAEVQGR-LEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTY 79
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDnEIEQLDLGYPEETGLtFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  80 SRFVQET-IGN-EGILKLLENETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIKdGGFGFAYDSIFIPDGKTKTFA 156
Cdd:TIGR00042  81 SARYQGTdIGNlEKILKLLEGVENRQAYFVCVIGYCDPNGePLVFEGIVKGKITREPR-GTYGFGYDPIFIPPEEGKTFA 159

                         170       180
                  ....*....|....*....|....*
gi 1883894125 157 EMTTEEKSEISHRKRAFYELKNYLE 181
Cdd:TIGR00042 160 ELTTEEKNKISHRGKAFKKFKKFLL 184
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 3-179 3.21e-66

NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.


Pssm-ID: 238285 [Multi-domain]  Cd Length: 183  Bit Score: 200.44  E-value: 3.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKEANCEIEQI--EIPYAEVQGRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTYS 80
Cdd:cd00515     1 IVFATGNKGKLKEFKEILAPFGIEVVSLkdIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVYS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  81 RFVQE----TIGNEGILKLLENETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIKdGGFGFAYDSIFIPDGKTKTF 155
Cdd:cd00515    81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDPDGePLVFEGEVEGKIVTEPR-GTGGFGYDPIFIPEGYGKTF 159

                         170       180
                  ....*....|....*....|....
gi 1883894125 156 AEMTTEEKSEISHRKRAFYELKNY 179
Cdd:cd00515   160 AEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 3-179 8.24e-58

Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae. The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions.


Pssm-ID: 460306 [Multi-domain]  Cd Length: 186  Bit Score: 179.18  E-value: 8.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKEaNCEIE-----QIEIPYAEVQGRLEEVSAFGVLEVFEKfNRPVIVEDSGFFVEKLNDFPG 77
Cdd:pfam01725   1 IVFATGNAGKLRELKAILAD-GIEVLslkdlGELPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  78 TYS-RFVQE----TIGNEGILKLLENE-TNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIK-DGGFGfaYDSIFIPD 149
Cdd:pfam01725  79 VYSaRFAGEggddEANNAKLLEELEVPdEDRSARFVCVIALADPGGpELVFEGEVEGEIVEEPRgEGGFG--YDPIFIPP 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1883894125 150 GKTKTFAEMTTEEKSEISHRKRAFYELKNY 179
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
 
Name Accession Description Interval E-value
PRK14821 PRK14821
XTP/dITP diphosphatase;
1-182 1.01e-108

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 308.03  E-value: 1.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEIILKEANCEIEQIEIPYAEVQ-GRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTY 79
Cdd:PRK14821    1 MKIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  80 SRFVQETIGNEGILKLLENETNRNAYFKTVIGYYDGDNIKLFTGIVKGTISTEIKDGGfGFAYDSIFIPDGKTKTFAEMT 159
Cdd:PRK14821   81 SAFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEKLFTGIVEGKIANEIRGKG-GFGYDPIFIPEGEEKTFAEMT 159

                         170       180
                  ....*....|....*....|...
gi 1883894125 160 TEEKSEISHRKRAFYELKNYLEN 182
Cdd:PRK14821  160 TEEKNKISHRKRAFDEFKEWLKE 182
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 2-182 2.49e-70

Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 211.07  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   2 KIYFATGNQNKVDEAEIILKEANCEIEQI-EIPYAEV--QGR-LEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPG 77
Cdd:COG0127     1 KLVFATGNAGKLREIRALLAPLGIEVVSLsDLGLPEPeeTGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  78 TYSRFVQ-----ETIGNEGILKLLEN-ETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIK-DGGFGfaYDSIFIPD 149
Cdd:COG0127    81 VYSARYAgegadDEANNEKLLKLLEGvDEDRRARFVCVLALADPDGePLVFEGEVEGEIAEEPRgEGGFG--YDPIFIPD 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1883894125 150 GKTKTFAEMTTEEKSEISHRKRAFYELKNYLEN 182
Cdd:COG0127   159 GYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 2-181 9.06e-67

non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272870 [Multi-domain]  Cd Length: 184  Bit Score: 202.21  E-value: 9.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   2 KIYFATGNQNKVDEAEIILKEANC-EIEQIEIPYAEVQGR-LEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTY 79
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDnEIEQLDLGYPEETGLtFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  80 SRFVQET-IGN-EGILKLLENETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIKdGGFGFAYDSIFIPDGKTKTFA 156
Cdd:TIGR00042  81 SARYQGTdIGNlEKILKLLEGVENRQAYFVCVIGYCDPNGePLVFEGIVKGKITREPR-GTYGFGYDPIFIPPEEGKTFA 159

                         170       180
                  ....*....|....*....|....*
gi 1883894125 157 EMTTEEKSEISHRKRAFYELKNYLE 181
Cdd:TIGR00042 160 ELTTEEKNKISHRGKAFKKFKKFLL 184
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 3-179 3.21e-66

NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.


Pssm-ID: 238285 [Multi-domain]  Cd Length: 183  Bit Score: 200.44  E-value: 3.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKEANCEIEQI--EIPYAEVQGRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGTYS 80
Cdd:cd00515     1 IVFATGNKGKLKEFKEILAPFGIEVVSLkdIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVYS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  81 RFVQE----TIGNEGILKLLENETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIKdGGFGFAYDSIFIPDGKTKTF 155
Cdd:cd00515    81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDPDGePLVFEGEVEGKIVTEPR-GTGGFGYDPIFIPEGYGKTF 159

                         170       180
                  ....*....|....*....|....
gi 1883894125 156 AEMTTEEKSEISHRKRAFYELKNY 179
Cdd:cd00515   160 AEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 3-179 8.24e-58

Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae. The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions.


Pssm-ID: 460306 [Multi-domain]  Cd Length: 186  Bit Score: 179.18  E-value: 8.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKEaNCEIE-----QIEIPYAEVQGRLEEVSAFGVLEVFEKfNRPVIVEDSGFFVEKLNDFPG 77
Cdd:pfam01725   1 IVFATGNAGKLRELKAILAD-GIEVLslkdlGELPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  78 TYS-RFVQE----TIGNEGILKLLENE-TNRNAYFKTVIGYYDGDN-IKLFTGIVKGTISTEIK-DGGFGfaYDSIFIPD 149
Cdd:pfam01725  79 VYSaRFAGEggddEANNAKLLEELEVPdEDRSARFVCVIALADPGGpELVFEGEVEGEIVEEPRgEGGFG--YDPIFIPP 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1883894125 150 GKTKTFAEMTTEEKSEISHRKRAFYELKNY 179
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 1-183 3.66e-40

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 134.42  E-value: 3.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEII---------LKEANCeieQIEIPyaEVQGRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEK 71
Cdd:PRK14823    1 MKLVFATNNKHKLEEIRSIlpekiellsLSDIGC---HEDIP--ETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  72 LNDFPGTYS-RFVQETIGNEG----ILKLLENETNRNAYFKTVIGYYDGDNIKLFTGIVKGTISTEiKDGGFGFAYDSIF 146
Cdd:PRK14823   76 LNGAPGVYSaRYAGGEHNAEAnmrkLLEELEGKDNRKAQFRTVIALILDGKEHLFEGIIKGEIIKE-KRGDSGFGYDPIF 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1883894125 147 IPDGKTKTFAEMTTEEKSEISHRKRAFYELKNYLENL 183
Cdd:PRK14823  155 VPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSKA 191
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 1-183 3.57e-36

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 124.43  E-value: 3.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEIILKEANCEIE-QIEIPYAEVqgrlEEVsafGV----------LEVFEKFNRPVIVEDSGFFV 69
Cdd:PRK00120    1 MKIVLASHNAGKLRELKALLAPFGIEVVsQGELGVPEP----EET---GTtfvenalikaRHAAKATGLPALADDSGLCV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  70 EKLNDFPGTYS-RFvqetiGNEG------ILKLLE-----NETNRNAYFKTVIGYYDGDNIKL-FTGIVKGTISTEIK-D 135
Cdd:PRK00120   74 DALGGAPGVYSaRY-----AGEGasdaanNEKLLEelkgvPDEDRRARFVCVLVLVRPDPTPLvAEGRWEGEILWEPRgE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1883894125 136 GGFGfaYDSIFIPDGKTKTFAEMTTEEKSEISHRKRAFYELKNYLENL 183
Cdd:PRK00120  149 NGFG--YDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
PRK14822 PRK14822
XTP/dITP diphosphatase;
1-181 3.74e-34

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 119.61  E-value: 3.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEIILKEANCEI----EQIEIPYAEVQGR-LEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDF 75
Cdd:PRK14822    2 KEIVIATKNKGKVREFKEIFEKFDIEVkslaDFPPIPEVEETGTtFEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  76 PGTYS-RFVQETIGNEG-ILKLLEN-----ETNRNAYFKTVIGY-YDGDNIKLFTGIVKGTISTEIK-DGGFGfaYDSIF 146
Cdd:PRK14822   82 PGVYSaRYAGEAKDDAAnNEKLLKElggvpFEKRTARFHCVIAVaFPGGETKTVEGTCEGEILEEPRgENGFG--YDPLF 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1883894125 147 IPDGKTKTFAEMTTEEKSEISHRKRAFYELKNYLE 181
Cdd:PRK14822  160 YVPEKGKTMAELSSEEKNAISHRGKALKKLEAELP 194
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 1-183 1.66e-32

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 115.24  E-value: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   1 MKIYFATGNQNKVDEAEIILKEANCEIEQIE--IPYAEVQGRLEEVSAFGVLEVFEKFNRPVIVEDSGFFVEKLNDFPGT 78
Cdd:PRK14824    1 MKILLATTNEGKVREIKRLLSDLGIEVLSPDkkIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  79 YS-RFVQETIG-------------NEGILKLLENETNRNAYFKTVIGYYDGDNIKLFTGIVKGTISTEiKDGGFGFAYDS 144
Cdd:PRK14824   81 YSsRFYQIEFGgkeevveskdeanIRKLLRLLEGKQNRKARFVAFVVLYFGDWGIWTEGECRGKIAEE-PRGSGGFGYDP 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1883894125 145 IFIPDGKTKTFAEMTTEEKSEISHRKRAFYELKNYLENL 183
Cdd:PRK14824  160 VFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVEILKYG 198
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 3-180 4.46e-27

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 101.17  E-value: 4.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKEANCeieQIEIP----YAEVQGRLEEVSAFGVLEVFEKFNR--PVIVEDSGFFVEKLNDFP 76
Cdd:PRK14825    4 LFFATTNINKINEVKQILDIPNI---KIEIPqnfdIKETGKTFKENSLLKAKALFEILNNkqPVFSEDSGLCIEALNLEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  77 GTYS-RFVQETIG--------NEGILKLLENETNRNAYFKTVIGYYDGD-NIKLFTGIVKGTISTEIKD-GGFGFAYDSI 145
Cdd:PRK14825   81 GIYSkRYDQYKLGkklstnekNHLIIDLMKNEKNRTAYFICNISYISKDgTILNFEGIIKGTIALSIDDyKKNGFGYDPI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1883894125 146 FIpDGKTKTFAEMTTEEKSEISHRKRAFYELKNYL 180
Cdd:PRK14825  161 FL-TKNNKRLSELTLEEKNKISHRGIAFDKFKKFL 194
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 3-181 1.65e-24

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 95.12  E-value: 1.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDE--------AEII----LKEAN--CEIEQIEiPYAEVQGRLEEVSAFGVLEvfEKFNRPV-IVEDSGF 67
Cdd:PRK14826   11 IVLATGNRDKVRElrpllehiSPLFsvrsLADLGveVDIEETE-ETLEGNALLKADAIFELLS--DRFPFLIaLADDTGL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  68 FVEKLNDFPGTYS-RFVQETIGNE--------GILKLLENETNRNAYFKTVIGYY----DGDNIKLF----TGIVKGTIS 130
Cdd:PRK14826   88 EVDALGGAPGVYSaRFAPVPEGEKptyednvrHLLSEMEGKTERSARFRTVIALKgrlpGKNGAFEFeetaEGVVEGSIT 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1883894125 131 TEiKDGGFGFAYDSIFIPDGKTKTFAEMTTEEKSEISHR----KRAFYELKNYLE 181
Cdd:PRK14826  168 TE-KKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRalavQKAVKFLRTILS 221
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
 3-130 1.20e-17

Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum formation in eukaryotes, bacteria and archaea. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides, such as hypoxanthine/xanthine NTP, but not standard nucleotides.


Pssm-ID: 238485  Cd Length: 131  Bit Score: 74.85  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKeanCEIEQIEIPYAEVQGR------LEEVSAFGVLEVFEKFN-RPVIVEDSGFFVeklNDF 75
Cdd:cd00985     1 LILASGSPRRLEELKQIGG---IEFEVLPSDIDETGLKgepedtVEELALLKARAVAERLPdAPVIADDTGLVV---DGR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1883894125  76 PGTYSRFVQETignegiLKLLENETNRNAYFKTVIGYYDGDN-IKLFTGIVKGTIS 130
Cdd:cd00985    75 PGGKPARFAEA------LEMLRGLSGRTAEFVTAVALVDPDGkIITFEGETEGKIA 124
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 3-176 3.34e-09

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 54.82  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125   3 IYFATGNQNKVDEAEIILKEANCEIEQI----EIPYAEVQGRLEEVSAFGVLEVFEKFN-RPVIVEDSGFFVEKLNDFPG 77
Cdd:PRK02491  130 ILIATRNEGKTKEFRKLFGKLGYKVENLndypDLPEVAETGMTFEENARLKAETISRLTgKMVLADDSGLKVDALGGLPG 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883894125  78 TYS-RFV-QETIGNEGILKLLE------NETNRNAYFKT--VIGYYDGDNIkLFTGIVKGTISTEIKdGGFGFAYDSIFI 147
Cdd:PRK02491  210 VWSaRFSgPDATDAENNAKLLHelamvfDLKDRSAQFHTtlVVAAPNKDSL-VVEADWPGYIATEPK-GENGFGYDPLFL 287

                         170       180
                  ....*....|....*....|....*....
gi 1883894125 148 PDGKTKTFAEMTTEEKSEISHRKRAFYEL 176
Cdd:PRK02491  288 VGETGRHAAELTAEEKNQLSHRGQAVKKL 316
 
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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