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Conserved domains on  [gi|1037100316|ref|XP_017130033|]
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inosine triphosphate pyrophosphatase [Drosophila elegans]

Protein Classification

non-canonical purine NTP pyrophosphatase( domain architecture ID 10087719)

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:  22531138|17976651
SCOP:  4000518

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 5-182 1.87e-82

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: 242.04  E-value: 1.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVSKK--IDLPELQGDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPY 82
Cdd:cd00515     1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  83 IKWFLE----KLQPEGLHRLLHGWEDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKT 157
Cdd:cd00515    80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDP-DGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                         170       180
                  ....*....|....*....|....*
gi 1037100316 158 YAELPKSEKNTISHRYRALALLQQH 182
Cdd:cd00515   159 FAEMSPEEKNAISHRGKALRKLKEF 183
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 5-182 1.87e-82

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: 242.04  E-value: 1.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVSKK--IDLPELQGDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPY 82
Cdd:cd00515     1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  83 IKWFLE----KLQPEGLHRLLHGWEDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKT 157
Cdd:cd00515    80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDP-DGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                         170       180
                  ....*....|....*....|....*
gi 1037100316 158 YAELPKSEKNTISHRYRALALLQQH 182
Cdd:cd00515   159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 5-182 2.04e-75

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: 224.25  E-value: 2.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFPrtIVSKK-----IDLPELQGDIDEIAIKKCKEAARQvNGPVLVEDTSLCFNALEGLP 79
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIE--VLSLKdlgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  80 GPYIKWFLE--KLQPEGLHRLLHGW----EDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPK 152
Cdd:pfam01725  78 GVYSARFAGegGDDEANNAKLLEELevpdEDRSARFVCVIALADP-GGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPP 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1037100316 153 GYDKTYAELPKSEKNTISHRYRALALLQQH 182
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 5-185 7.57e-66

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 200.29  E-value: 7.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVS-KKIDLPE--LQGD-IDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPG 80
Cdd:COG0127     2 LVFATGNAGKLREIRALLAP-LGIEVVSlSDLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  81 PYIKWFL-----EKLQPEGLHRLLHG-WEDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKG 153
Cdd:COG0127    81 VYSARYAgegadDEANNEKLLKLLEGvDEDRRARFVCVLALADP-DGEPLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDG 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1037100316 154 YDKTYAELPKSEKNTISHRYRALALLQQHFEK 185
Cdd:COG0127   160 YGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 5-179 5.63e-58

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: 180.25  E-value: 5.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFPRTIVSKKIDLPELQG-DIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPYI 83
Cdd:TIGR00042   2 IVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGlTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIYS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  84 KWFLEKLQ--PEGLHRLLHGWEDKSAQAVCTFGYCDgADAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKTYAE 160
Cdd:TIGR00042  82 ARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYCD-PNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKTFAE 160

                         170
                  ....*....|....*....
gi 1037100316 161 LPKSEKNTISHRYRALALL 179
Cdd:TIGR00042 161 LTTEEKNKISHRGKAFKKF 179
PRK14821 PRK14821
XTP/dITP diphosphatase;
5-176 2.35e-46

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 150.49  E-value: 2.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVSKKIDLPELQ-GDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPYI 83
Cdd:PRK14821    3 IYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  84 KWFLEKLQPEGLHRLLHGWEDKSAQAVCTFGYCDGADAEplIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKTYAELP 162
Cdd:PRK14821   82 AFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEK--LFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMT 159

                         170
                  ....*....|....
gi 1037100316 163 KSEKNTISHRYRAL 176
Cdd:PRK14821  160 TEEKNKISHRKRAF 173
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 5-182 1.87e-82

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: 242.04  E-value: 1.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVSKK--IDLPELQGDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPY 82
Cdd:cd00515     1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  83 IKWFLE----KLQPEGLHRLLHGWEDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKT 157
Cdd:cd00515    80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDP-DGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                         170       180
                  ....*....|....*....|....*
gi 1037100316 158 YAELPKSEKNTISHRYRALALLQQH 182
Cdd:cd00515   159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 5-182 2.04e-75

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: 224.25  E-value: 2.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFPrtIVSKK-----IDLPELQGDIDEIAIKKCKEAARQvNGPVLVEDTSLCFNALEGLP 79
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIE--VLSLKdlgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  80 GPYIKWFLE--KLQPEGLHRLLHGW----EDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPK 152
Cdd:pfam01725  78 GVYSARFAGegGDDEANNAKLLEELevpdEDRSARFVCVIALADP-GGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPP 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1037100316 153 GYDKTYAELPKSEKNTISHRYRALALLQQH 182
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 5-185 7.57e-66

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 200.29  E-value: 7.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVS-KKIDLPE--LQGD-IDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPG 80
Cdd:COG0127     2 LVFATGNAGKLREIRALLAP-LGIEVVSlSDLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  81 PYIKWFL-----EKLQPEGLHRLLHG-WEDKSAQAVCTFGYCDGaDAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKG 153
Cdd:COG0127    81 VYSARYAgegadDEANNEKLLKLLEGvDEDRRARFVCVLALADP-DGEPLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDG 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1037100316 154 YDKTYAELPKSEKNTISHRYRALALLQQHFEK 185
Cdd:COG0127   160 YGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 5-179 5.63e-58

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: 180.25  E-value: 5.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFPRTIVSKKIDLPELQG-DIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPYI 83
Cdd:TIGR00042   2 IVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGlTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIYS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  84 KWFLEKLQ--PEGLHRLLHGWEDKSAQAVCTFGYCDgADAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKTYAE 160
Cdd:TIGR00042  82 ARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYCD-PNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKTFAE 160

                         170
                  ....*....|....*....
gi 1037100316 161 LPKSEKNTISHRYRALALL 179
Cdd:TIGR00042 161 LTTEEKNKISHRGKAFKKF 179
PRK14821 PRK14821
XTP/dITP diphosphatase;
5-176 2.35e-46

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 150.49  E-value: 2.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPsFPRTIVSKKIDLPELQ-GDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPYI 83
Cdd:PRK14821    3 IYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  84 KWFLEKLQPEGLHRLLHGWEDKSAQAVCTFGYCDGADAEplIFKGITEGVIV-EPRGPRDFGWDPVFQPKGYDKTYAELP 162
Cdd:PRK14821   82 AFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEK--LFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMT 159

                         170
                  ....*....|....
gi 1037100316 163 KSEKNTISHRYRAL 176
Cdd:PRK14821  160 TEEKNKISHRKRAF 173
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 9-186 1.46e-38

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 130.97  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   9 TGNAKKLEELVAILGPsFPRTIVSKKiDLPElqGDIDEI-------AIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGP 81
Cdd:PRK00120    7 SHNAGKLRELKALLAP-FGIEVVSQG-ELGV--PEPEETgttfvenALIKARHAAKATGLPALADDSGLCVDALGGAPGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  82 Y--------------IKWFLEKLQPEGLhrllhgwEDKSAQAVCTFGYCDgADAEPLIFKGITEGVIV-EPRGPRDFGWD 146
Cdd:PRK00120   83 YsaryagegasdaanNEKLLEELKGVPD-------EDRRARFVCVLVLVR-PDPTPLVAEGRWEGEILwEPRGENGFGYD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1037100316 147 PVFQPKGYDKTYAELPKSEKNTISHRYRALALLQQHFEKL 186
Cdd:PRK00120  155 PIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
PRK14822 PRK14822
XTP/dITP diphosphatase;
3-188 7.20e-35

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 121.53  E-value: 7.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   3 KPITFVTGNAKKLEELVAILGPsFPRTIVSKK--IDLPELQGD---IDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEG 77
Cdd:PRK14822    2 KEIVIATKNKGKVREFKEIFEK-FDIEVKSLAdfPPIPEVEETgttFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  78 LPGPY--------------IKWFLEKLqpEGLHrllhgWEDKSAQAVCTFGYCdGADAEPLIFKGITEGVIVE-PRGPRD 142
Cdd:PRK14822   81 APGVYsaryageakddaanNEKLLKEL--GGVP-----FEKRTARFHCVIAVA-FPGGETKTVEGTCEGEILEePRGENG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1037100316 143 FGWDPVFQPKGYDKTYAELPKSEKNTISHRYRALALLQQHFEKLDK 188
Cdd:PRK14822  153 FGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLK 198
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 5-186 4.26e-28

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 103.99  E-value: 4.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFprTIVS-KKI----DLPELQGDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLP 79
Cdd:PRK14823    3 LVFATNNKHKLEEIRSILPEKI--ELLSlSDIgcheDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  80 GPYIKWFL--EKLQPEGLHRLLHGWEDKSAQAVCtFG--YCDGADAEPLIFKGITEGVIV-EPRGPRDFGWDPVFQPKGY 154
Cdd:PRK14823   81 GVYSARYAggEHNAEANMRKLLEELEGKDNRKAQ-FRtvIALILDGKEHLFEGIIKGEIIkEKRGDSGFGYDPIFVPEGY 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1037100316 155 DKTYAELPKSEKNTISHRYRALALLQQHFEKL 186
Cdd:PRK14823  160 DKTFAELGLEIKNQISHRAKAVQKLIDFLSKA 191
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 5-189 7.58e-27

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 100.99  E-value: 7.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFPRTI-VSKKIDLPELQGDIDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPYI 83
Cdd:PRK14824    3 ILLATTNEGKVREIKRLLSDLGIEVLsPDKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGVYS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  84 KWF---------LEKLQP-----EGLHRLLHGWEDKSAQAVCTFGYCDGadaEPLIF-KGITEGVIV-EPRGPRDFGWDP 147
Cdd:PRK14824   83 SRFyqiefggkeEVVESKdeaniRKLLRLLEGKQNRKARFVAFVVLYFG---DWGIWtEGECRGKIAeEPRGSGGFGYDP 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1037100316 148 VFQPKGYDKTYAELPKSEKNTISHRYRALALLQQHFEKLDKL 189
Cdd:PRK14824  160 VFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVEILKYGGML 201
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
 5-134 9.05e-25

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: 93.33  E-value: 9.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   5 ITFVTGNAKKLEELVAILGPSFprtiVSKKIDLPELQG------DIDEIAIKKCKEAARQVNG-PVLVEDTSLCFNaleG 77
Cdd:cd00985     1 LILASGSPRRLEELKQIGGIEF----EVLPSDIDETGLkgepedTVEELALLKARAVAERLPDaPVIADDTGLVVD---G 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037100316  78 LPGPYIKWFLEKLqpeglhRLLHGWEDKSAQAVCTFGYCDGADaEPLIFKGITEGVI 134
Cdd:cd00985    74 RPGGKPARFAEAL------EMLRGLSGRTAEFVTAVALVDPDG-KIITFEGETEGKI 123
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 1-191 2.87e-19

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 81.64  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   1 MSKPITFV--TGNAKKLEELVAILGPSFPRTIVSKKIDLPeLQGDIDEI-------AIKKCKE-----AARQVNGPVLVE 66
Cdd:PRK14826    5 ATETITIVlaTGNRDKVRELRPLLEHISPLFSVRSLADLG-VEVDIEETeetlegnALLKADAifellSDRFPFLIALAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  67 DTSLCFNALEGLPGPYIKWFLEklQPEG--------LHRLLH---GWEDKSAQ---AVCTFGYCDGADAePLIFKGITEG 132
Cdd:PRK14826   84 DTGLEVDALGGAPGVYSARFAP--VPEGekptyednVRHLLSemeGKTERSARfrtVIALKGRLPGKNG-AFEFEETAEG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037100316 133 VI-----VEPRGPRDFGWDPVFQPKGYDKTYAELPKSEKNTISHRYRAlalLQQHFEKLDKLIN 191
Cdd:PRK14826  161 VVegsitTEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALA---VQKAVKFLRTILS 221
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 3-172 3.60e-13

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 64.96  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316   3 KPITFVTGNAKKLEELVAILGPSFPRTIVSKKIDLPELQGDIDEIAIKKCKEAARQVNG--PVLVEDTSLCFNALEGLPG 80
Cdd:PRK14825    2 KTLFFATTNINKINEVKQILDIPNIKIEIPQNFDIKETGKTFKENSLLKAKALFEILNNkqPVFSEDSGLCIEALNLEPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  81 PYIKWF-----LEKLQP-EGLH---RLLHGWEDKSAQAVCTFGYCDgADAEPLIFKGITEGVI---VEPRGPRDFGWDPV 148
Cdd:PRK14825   82 IYSKRYdqyklGKKLSTnEKNHliiDLMKNEKNRTAYFICNISYIS-KDGTILNFEGIIKGTIalsIDDYKKNGFGYDPI 160

                         170       180
                  ....*....|....*....|....
gi 1037100316 149 FQPKGyDKTYAELPKSEKNTISHR 172
Cdd:PRK14825  161 FLTKN-NKRLSELTLEEKNKISHR 183
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 36-183 1.48e-11

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 61.75  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316  36 DLPELQGD---IDEIAIKKCKEAARQVNGPVLVEDTSLCFNALEGLPGPYIKWF--LEKLQPEGLHRLLHGW------ED 104
Cdd:PRK02491  162 DLPEVAETgmtFEENARLKAETISRLTGKMVLADDSGLKVDALGGLPGVWSARFsgPDATDAENNAKLLHELamvfdlKD 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037100316 105 KSAQAVCTFgYCDGADAEPLIFKGITEGVI-VEPRGPRDFGWDPVFQPKGYDKTYAELPKSEKNTISHRYRALALLQQHF 183
Cdd:PRK02491  242 RSAQFHTTL-VVAAPNKDSLVVEADWPGYIaTEPKGENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVF 320
 
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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