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Conserved domains on  [gi|390517020|ref|NP_001254552|]
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inosine triphosphate pyrophosphatase isoform c [Homo sapiens]

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:  17976651|22531138
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/ ...
 10-147 1.57e-61

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: 187.34  E-value: 1.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  10 IVFVTGNAKKLEEVQ------------------------------------------GPVLVEDTCLCFNALGGLPGPYI 47
Cdd:cd00515    1 IVFATGNKGKLKEFKeilapfgievvslkdiidieetgstfeenallkaraaaealgLPVLADDSGLCVDALNGFPGVYS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  48 KWFLE----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQT 122
Cdd:cd00515   81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                        170       180
                 ....*....|....*....|....*
gi 390517020 123 YAEMPKAEKNAVSHRFRALLELQEY 147
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/ ...
 10-147 1.57e-61

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: 187.34  E-value: 1.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  10 IVFVTGNAKKLEEVQ------------------------------------------GPVLVEDTCLCFNALGGLPGPYI 47
Cdd:cd00515    1 IVFATGNKGKLKEFKeilapfgievvslkdiidieetgstfeenallkaraaaealgLPVLADDSGLCVDALNGFPGVYS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  48 KWFLE----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQT 122
Cdd:cd00515   81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                        170       180
                 ....*....|....*....|....*
gi 390517020 123 YAEMPKAEKNAVSHRFRALLELQEY 147
Cdd:cd00515  159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 10-147 3.03e-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: 3.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   10 IVFVTGNAKKLEEVQ-------------------------------------------GPVLVEDTCLCFNALGGLPGPY 46
Cdd:pfam01725   1 IVFATGNAGKLRELKailadgievlslkdlgelpeieetggtfeenalikaraaaktgLPVLADDSGLEVDALNGFPGVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   47 IKWFLEKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGY 119
Cdd:pfam01725  81 SARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPPEG 158

                         170       180
                  ....*....|....*....|....*...
gi 390517020  120 EQTYAEMPKAEKNAVSHRFRALLELQEY 147
Cdd:pfam01725 159 GKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 9-148 1.22e-46

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 149.83  E-value: 1.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   9 KIVFVTGNAKKLEEVQ--------------------------------------------GPVLVEDTCLCFNALGGLPG 44
Cdd:COG0127    1 KLVFATGNAGKLREIRallaplgievvslsdlglpepeetgdtfeenalikaraaakatgLPALADDSGLEVDALGGAPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  45 PYIKWFL-----EKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPD 117
Cdd:COG0127   81 VYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAeEPRGEGGFGYDPIFIPD 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 390517020 118 GYEQTYAEMPKAEKNAVSHRFRALLELQEYF 148
Cdd:COG0127  159 GYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 9-147 4.25e-40

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: 132.87  E-value: 4.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020    9 KIVFVTGNAKKLEEVQ------------------------------------------GPVLVEDTCLCFNALGGLPGPY 46
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQsilsdlgdneieqldlgypeetgltfeenallkakhaakilnKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   47 IKWFLEKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTY 123
Cdd:TIGR00042  81 SARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKTF 158

                         170       180
                  ....*....|....*....|....
gi 390517020  124 AEMPKAEKNAVSHRFRALLELQEY 147
Cdd:TIGR00042 159 AELTTEEKNKISHRGKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-148 2.19e-32

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 113.51  E-value: 2.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   9 KIVFVTGNAKKLEEV-----------------------------------------QGPVLVEDTCLCFNALGGLPGPYI 47
Cdd:PRK14821   2 KIYFATGNKGKVEEAkiilkplgieveqikieypeiqadtleevaafgakwvynklNRPVIVEDSGLFIEALNGFPGPYS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  48 KWFLEKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQ 121
Cdd:PRK14821  82 AFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEK 153

                        170       180
                 ....*....|....*....|....*..
gi 390517020 122 TYAEMPKAEKNAVSHRFRALLELQEYF 148
Cdd:PRK14821 154 TFAEMTTEEKNKISHRKRAFDEFKEWL 180
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 10-147 1.57e-61

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: 187.34  E-value: 1.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  10 IVFVTGNAKKLEEVQ------------------------------------------GPVLVEDTCLCFNALGGLPGPYI 47
Cdd:cd00515    1 IVFATGNKGKLKEFKeilapfgievvslkdiidieetgstfeenallkaraaaealgLPVLADDSGLCVDALNGFPGVYS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  48 KWFLE----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQT 122
Cdd:cd00515   81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                        170       180
                 ....*....|....*....|....*
gi 390517020 123 YAEMPKAEKNAVSHRFRALLELQEY 147
Cdd:cd00515  159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 10-147 3.03e-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: 3.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   10 IVFVTGNAKKLEEVQ-------------------------------------------GPVLVEDTCLCFNALGGLPGPY 46
Cdd:pfam01725   1 IVFATGNAGKLRELKailadgievlslkdlgelpeieetggtfeenalikaraaaktgLPVLADDSGLEVDALNGFPGVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   47 IKWFLEKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGY 119
Cdd:pfam01725  81 SARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPPEG 158

                         170       180
                  ....*....|....*....|....*...
gi 390517020  120 EQTYAEMPKAEKNAVSHRFRALLELQEY 147
Cdd:pfam01725 159 GKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 9-148 1.22e-46

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 149.83  E-value: 1.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   9 KIVFVTGNAKKLEEVQ--------------------------------------------GPVLVEDTCLCFNALGGLPG 44
Cdd:COG0127    1 KLVFATGNAGKLREIRallaplgievvslsdlglpepeetgdtfeenalikaraaakatgLPALADDSGLEVDALGGAPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  45 PYIKWFL-----EKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPD 117
Cdd:COG0127   81 VYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAeEPRGEGGFGYDPIFIPD 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 390517020 118 GYEQTYAEMPKAEKNAVSHRFRALLELQEYF 148
Cdd:COG0127  159 GYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 9-147 4.25e-40

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: 132.87  E-value: 4.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020    9 KIVFVTGNAKKLEEVQ------------------------------------------GPVLVEDTCLCFNALGGLPGPY 46
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQsilsdlgdneieqldlgypeetgltfeenallkakhaakilnKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   47 IKWFLEKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTY 123
Cdd:TIGR00042  81 SARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKTF 158

                         170       180
                  ....*....|....*....|....
gi 390517020  124 AEMPKAEKNAVSHRFRALLELQEY 147
Cdd:TIGR00042 159 AELTTEEKNKISHRGKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-148 2.19e-32

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 113.51  E-value: 2.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   9 KIVFVTGNAKKLEEV-----------------------------------------QGPVLVEDTCLCFNALGGLPGPYI 47
Cdd:PRK14821   2 KIYFATGNKGKVEEAkiilkplgieveqikieypeiqadtleevaafgakwvynklNRPVIVEDSGLFIEALNGFPGPYS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  48 KWFLEKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQ 121
Cdd:PRK14821  82 AFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEK 153

                        170       180
                 ....*....|....*....|....*..
gi 390517020 122 TYAEMPKAEKNAVSHRFRALLELQEYF 148
Cdd:PRK14821 154 TFAEMTTEEKNKISHRKRAFDEFKEWL 180
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 8-153 7.54e-28

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 102.08  E-value: 7.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   8 KKIVFVTGNAKKLEEVQG--------------------------------------------PVLVEDTCLCFNALGGLP 43
Cdd:PRK00120   1 MKIVLASHNAGKLRELKAllapfgievvsqgelgvpepeetgttfvenalikarhaakatglPALADDSGLCVDALGGAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  44 GPY-IKWF---------LEKLkpegLHQLLA-GFEDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWD 111
Cdd:PRK00120  81 GVYsARYAgegasdaanNEKL----LEELKGvPDEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILwEPRGENGFGYD 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 390517020 112 PCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSLAA 153
Cdd:PRK00120 155 PIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALRELLA 196
PRK14822 PRK14822
XTP/dITP diphosphatase;
26-151 4.34e-24

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 92.26  E-value: 4.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  26 PVLVEDTCLCFNALGGLPGPYIKWF----------LEKLKPEglhqlLAG--FEDKSAYALCTFALSTgdPSQPVRLFRG 93
Cdd:PRK14822  65 PVIADDSGLEVDALNGAPGVYSARYageakddaanNEKLLKE-----LGGvpFEKRTARFHCVIAVAF--PGGETKTVEG 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 390517020  94 RTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSL 151
Cdd:PRK14822 138 TCEGEILeEPRGENGFGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEW 196
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 8-151 1.17e-18

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 78.18  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   8 KKIVFVTGNAKKLEEVQG--------------------------------------------PVLVEDTCLCFNALGGLP 43
Cdd:PRK14823   1 MKLVFATNNKHKLEEIRSilpekiellslsdigchedipetadtlegnallkaeyvykkygyDCFADDTGLEVEALNGAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  44 GPYIKWF----------LEKLkpegLHQLlAGFEDKSAYALCTFALSTgDPSQpvRLFRGRTSGRIVA-PRGCQDFGWDP 112
Cdd:PRK14823  81 GVYSARYaggehnaeanMRKL----LEEL-EGKDNRKAQFRTVIALIL-DGKE--HLFEGIIKGEIIKeKRGDSGFGYDP 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 390517020 113 CFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSL 151
Cdd:PRK14823 153 IFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSKA 191
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 26-151 2.74e-18

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 77.49  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  26 PVLVEDTCLCFNALGGLPGPY------IKW---FLEKLKP-----EGLHQLLAGFEDKSAYALCTFALSTGDpsqpVRLF 91
Cdd:PRK14824  61 PVLADDSGLEVPALEGYPGVYssrfyqIEFggkEEVVESKdeaniRKLLRLLEGKQNRKARFVAFVVLYFGD----WGIW 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 390517020  92 -RGRTSGRIVA-PRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRA---LLELQEYFGSL 151
Cdd:PRK14824 137 tEGECRGKIAEePRGSGGFGYDPVFIPEGYNKTMAELSPEEKNKISHRGKAvrkLVEILKYGGML 201
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
 10-99 6.43e-13

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: 61.75  E-value: 6.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  10 IVFVTGNAKKLEEVQ--------------------------------------------GPVLVEDTCLCFNalgGLPGP 45
Cdd:cd00985    1 LILASGSPRRLEELKqiggiefevlpsdidetglkgepedtveelallkaravaerlpdAPVIADDTGLVVD---GRPGG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 390517020  46 YIKWFLEKLKpeglhqLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRI 99
Cdd:cd00985   78 KPARFAEALE------MLRGLSGRTAEFVTAVALV--DPDGKIITFEGETEGKI 123
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 28-141 7.56e-13

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 63.15  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  28 LVEDTCLCFNALGGLPGPYIKWFL---EKLKP---EGLHQLL---AGFEDKSAYALCTFALSTGDPS-QPVRLFR----G 93
Cdd:PRK14826  81 LADDTGLEVDALGGAPGVYSARFApvpEGEKPtyeDNVRHLLsemEGKTERSARFRTVIALKGRLPGkNGAFEFEetaeG 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 390517020  94 RTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRAL 141
Cdd:PRK14826 161 VVEGSITtEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAV 209
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 27-148 1.77e-10

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 57.51  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020  27 VLVEDTCLCFNALGGLPGPYIKWFL------EKLKPEGLHQLLAGFE--DKSAYALCTFALSTgdPSQPVRLFRGRTSGR 98
Cdd:PRK02491 192 VLADDSGLKVDALGGLPGVWSARFSgpdatdAENNAKLLHELAMVFDlkDRSAQFHTTLVVAA--PNKDSLVVEADWPGY 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 390517020  99 I-VAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYF 148
Cdd:PRK02491 270 IaTEPKGENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVF 320
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 4-148 4.87e-07

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 47.24  E-value: 4.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390517020   4 SLVGKKIVFVTGNAKKleevqgPVLVEDTCLCFNALGGLPGPYIKWF-----LEKLKPEGLHQLLAGF----EDKSAYAL 74
Cdd:PRK14825  47 SLLKAKALFEILNNKQ------PVFSEDSGLCIEALNLEPGIYSKRYdqyklGKKLSTNEKNHLIIDLmkneKNRTAYFI 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 390517020  75 CTFALSTGDPSqpVRLFRGRTSGRIVAPRGCQD---FGWDPCFQPDGyEQTYAEMPKAEKNAVSHRFRALLELQEYF 148
Cdd:PRK14825 121 CNISYISKDGT--ILNFEGIIKGTIALSIDDYKkngFGYDPIFLTKN-NKRLSELTLEEKNKISHRGIAFDKFKKFL 194
 
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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