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Conserved domains on  [gi|446581969|ref|WP_000659315|]
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MULTISPECIES: XTP/dITP diphosphatase [Staphylococcus]

Protein Classification

non-canonical purine NTP pyrophosphatase( domain architecture ID 10794073)

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
PRK14822 PRK14822
XTP/dITP diphosphatase;
1-195 7.45e-118

XTP/dITP diphosphatase;


:

Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 332.24  E-value: 7.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822   1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFY 156
Cdd:PRK14822  81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446581969 157 VPKLDKTMAQLSKEEKGQISHRRNAINLLEAYLAGDQHV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
 
Name Accession Description Interval E-value
PRK14822 PRK14822
XTP/dITP diphosphatase;
1-195 7.45e-118

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 332.24  E-value: 7.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822   1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFY 156
Cdd:PRK14822  81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446581969 157 VPKLDKTMAQLSKEEKGQISHRRNAINLLEAYLAGDQHV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
3-191 1.72e-96

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 278.10  E-value: 1.72e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   3 EIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:COG0127    1 KLVFATGNAGKLREIRALLAPLGieVVSLSDL-GLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  81 GIYSARYAGENKSDEANIEKLLNKLGNT-TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPK 159
Cdd:COG0127   80 GVYSARYAGEGADDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPDG 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446581969 160 LDKTMAQLSKEEKGQISHRRNAINLLEAYLAG 191
Cdd:COG0127  160 YGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
4-188 5.99e-90

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: 261.23  E-value: 5.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969    4 IVIASNNQGKINDFKVIF-PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKaLNKTVIADDSGLEVFALNGEPGI 82
Cdd:pfam01725   1 IVFATGNAGKLRELKAILaDGIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   83 YSARYAGENKSDEANIEKLLNKL-GNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLD 161
Cdd:pfam01725  80 YSARFAGEGGDDEANNAKLLEELeVPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPPEGG 159
                         170       180
                  ....*....|....*....|....*..
gi 446581969  162 KTMAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLKEF 186
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
4-188 5.52e-87

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: 253.60  E-value: 5.52e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   4 IVIASNNQGKINDFKVIFPDYhVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGIY 83
Cdd:cd00515    1 IVFATGNKGKLKEFKEILAPF-GIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  84 SARYAGENkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDKT 163
Cdd:cd00515   80 SARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGYGKT 158
                        170       180
                 ....*....|....*....|....*
gi 446581969 164 MAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:cd00515  159 FAEMSPEEKNAISHRGKALRKLKEF 183
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
3-189 3.58e-68

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: 206.06  E-value: 3.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969    3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFdVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGY-PEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   83 YSARYAGenkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDK 162
Cdd:TIGR00042  80 YSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGTYGFGYDPIFIPPEEGK 156
                         170       180
                  ....*....|....*....|....*..
gi 446581969  163 TMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:TIGR00042 157 TFAELTTEEKNKISHRGKAFKKFKKFL 183
 
Name Accession Description Interval E-value
PRK14822 PRK14822
XTP/dITP diphosphatase;
1-195 7.45e-118

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 332.24  E-value: 7.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822   1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFY 156
Cdd:PRK14822  81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446581969 157 VPKLDKTMAQLSKEEKGQISHRRNAINLLEAYLAGDQHV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
3-191 1.72e-96

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 278.10  E-value: 1.72e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   3 EIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:COG0127    1 KLVFATGNAGKLREIRALLAPLGieVVSLSDL-GLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  81 GIYSARYAGENKSDEANIEKLLNKLGNT-TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPK 159
Cdd:COG0127   80 GVYSARYAGEGADDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPDG 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446581969 160 LDKTMAQLSKEEKGQISHRRNAINLLEAYLAG 191
Cdd:COG0127  160 YGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
4-188 5.99e-90

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: 261.23  E-value: 5.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969    4 IVIASNNQGKINDFKVIF-PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKaLNKTVIADDSGLEVFALNGEPGI 82
Cdd:pfam01725   1 IVFATGNAGKLRELKAILaDGIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   83 YSARYAGENKSDEANIEKLLNKL-GNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLD 161
Cdd:pfam01725  80 YSARFAGEGGDDEANNAKLLEELeVPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPPEGG 159
                         170       180
                  ....*....|....*....|....*..
gi 446581969  162 KTMAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLKEF 186
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
2-189 1.63e-88

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 258.09  E-value: 1.63e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   2 KEIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGE 79
Cdd:PRK00120   1 MKIVLASHNAGKLRELKALLAPFGieVVSQGEL-GVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  80 PGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYV 157
Cdd:PRK00120  80 PGVYSARYAGEGASDAANNEKLLEELKGVpdEDRRARFVCVLVLVRPDPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446581969 158 PKLDKTMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
4-188 5.52e-87

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: 253.60  E-value: 5.52e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   4 IVIASNNQGKINDFKVIFPDYhVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGIY 83
Cdd:cd00515    1 IVFATGNKGKLKEFKEILAPF-GIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  84 SARYAGENkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDKT 163
Cdd:cd00515   80 SARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGYGKT 158
                        170       180
                 ....*....|....*....|....*
gi 446581969 164 MAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:cd00515  159 FAEMSPEEKNAISHRGKALRKLKEF 183
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
3-189 3.58e-68

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: 206.06  E-value: 3.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969    3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFdVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGY-PEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   83 YSARYAGenkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDK 162
Cdd:TIGR00042  80 YSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGTYGFGYDPIFIPPEEGK 156
                         170       180
                  ....*....|....*....|....*..
gi 446581969  163 TMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:TIGR00042 157 TFAELTTEEKNKISHRGKAFKKFKKFL 183
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
2-189 8.74e-60

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 184.88  E-value: 8.74e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   2 KEIVIASNNQGKINDFKVIFPDY-HVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:PRK14823   1 MKLVFATNNKHKLEEIRSILPEKiELLSLSDIGCHEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  81 GIYSARYAGENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSgPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKL 160
Cdd:PRK14823  81 GVYSARYAGGEHNAEANMRKLLEELEGKDNRKAQFRTVIALI-LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIFVPEGY 159
                        170       180
                 ....*....|....*....|....*....
gi 446581969 161 DKTMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK14823 160 DKTFAELGLEIKNQISHRAKAVQKLIDFL 188
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
4-191 7.83e-54

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 171.00  E-value: 7.83e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   4 IVIASNNQGKINDFK----VIFPDYHVIGISELIPDFDVEETGSTFEENAILKSEA-----AAKALNKTVIADDSGLEVF 74
Cdd:PRK14826  11 IVLATGNRDKVRELRplleHISPLFSVRSLADLGVEVDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  75 ALNGEPGIYSARYA----GENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSG--PDMETKVF-----KGTVSGEIADGK 143
Cdd:PRK14826  91 ALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTERSARFRTVIALKGrlPGKNGAFEfeetaEGVVEGSITTEK 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446581969 144 YGDNGFGYDPIFYVPKLDKTMAQLSKEEKGQISHR----RNAINLLEAYLAG 191
Cdd:PRK14826 171 KGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRalavQKAVKFLRTILSQ 222
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
4-185 1.76e-51

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 164.16  E-value: 1.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   4 IVIASNNQGKINDFKVIFPDYhviGISELIPD--FDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPG 81
Cdd:PRK14824   3 ILLATTNEGKVREIKRLLSDL---GIEVLSPDkkIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  82 IYSAR-----YAGENK----SDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVfKGTVSGEIADGKYGDNGFGYD 152
Cdd:PRK14824  80 VYSSRfyqieFGGKEEvvesKDEANIRKLLRLLEGKQNRKARFVAFVVLYFGDWGIWT-EGECRGKIAEEPRGSGGFGYD 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446581969 153 PIFYVPKLDKTMAQLSKEEKGQISHRRNAINLL 185
Cdd:PRK14824 159 PVFIPEGYNKTMAELSPEEKNKISHRGKAVRKL 191
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
4-188 4.67e-49

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 161.90  E-value: 4.67e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   4 IVIASNNQGKINDFKVIFPD--YHVIGISELiPDF-DVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKlgYKVENLNDY-PDLpEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLP 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  81 GIYSARYAGENKSDEANIEKLLNKLG---NTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYV 157
Cdd:PRK02491 209 GVWSARFSGPDATDAENNAKLLHELAmvfDLKDRSAQFHTTLVVAAPNKDSLVVEADWPGYIATEPKGENGFGYDPLFLV 288
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446581969 158 PKLDKTMAQLSKEEKGQISHRRNAI-NLLEAY 188
Cdd:PRK02491 289 GETGRHAAELTAEEKNQLSHRGQAVkKLMEVF 320
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
1-189 2.09e-34

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 120.43  E-value: 2.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   1 MKEIVIASNNQGKINDFKVIFpdyHVIGISELIP-DFDVEETGSTFEENAILKSEAAAKALNKT--VIADDSGLEVFALN 77
Cdd:PRK14825   1 MKTLFFATTNINKINEVKQIL---DIPNIKIEIPqNFDIKETGKTFKENSLLKAKALFEILNNKqpVFSEDSGLCIEALN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  78 GEPGIYSARY----AGENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIA--DGKYGDNGFGY 151
Cdd:PRK14825  78 LEPGIYSKRYdqykLGKKLSTNEKNHLIIDLMKNEKNRTAYFICNISYISKDGTILNFEGIIKGTIAlsIDDYKKNGFGY 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446581969 152 DPIFyVPKLDKTMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK14825 158 DPIF-LTKNNKRLSELTLEEKNKISHRGIAFDKFKKFL 194
PRK14821 PRK14821
XTP/dITP diphosphatase;
3-189 3.18e-34

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 119.67  E-value: 3.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFDVEEtgSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQA--DTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969  83 YSArYAGENksdeANIEKLLNKLGNTTDRRAQFVCVISMSGPDMEtKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDK 162
Cdd:PRK14821  80 YSA-FVYKT----LGNEGILKLLEGEENRRAYFKSVIGYCDPGGE-KLFTGIVEGKIANEIRGKGGFGYDPIFIPEGEEK 153
                        170       180
                 ....*....|....*....|....*..
gi 446581969 163 TMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK14821 154 TFAEMTTEEKNKISHRKRAFDEFKEWL 180
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
4-140 1.55e-27

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: 100.65  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969   4 IVIASNNQGKINDFKVIFpdyhviGISELIPDFDVEETGS------TFEENAILKSEAAAKALNKT-VIADDSGLEVfal 76
Cdd:cd00985    1 LILASGSPRRLEELKQIG------GIEFEVLPSDIDETGLkgepedTVEELALLKARAVAERLPDApVIADDTGLVV--- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581969  77 NGEPGIYSARYAGEnksdeanieklLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIA 140
Cdd:cd00985   72 DGRPGGKPARFAEA-----------LEMLRGLSGRTAEFVTAVALVDPDGKIITFEGETEGKIA 124
 
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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