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Conserved domains on  [gi|568957398|ref|XP_006531348|]
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cancer-related nucleoside-triphosphatase homolog isoform X2 [Mus musculus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTPase_1 super family cl46504
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 20-130 3.95e-42

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


The actual alignment was detected with superfamily member pfam03266:

Pssm-ID: 460869  Cd Length: 168  Bit Score: 136.99  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398   20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCGpkhrVCIIDEIGKMELFSQPFIQAVRQMLStPGIIVVGTIPVPkgKP 99
Cdd:pfam03266  65 AVSGPRVGKYVVNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SD 137

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568957398  100 LALVEEIRKRRDVKVFNVTRDNRNSLLPDIV 130
Cdd:pfam03266 138 SPLLEEIRRREDVKIFVVTKENRDALPEEIL 168
 
Name Accession Description Interval E-value
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 20-130 3.95e-42

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 136.99  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398   20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCGpkhrVCIIDEIGKMELFSQPFIQAVRQMLStPGIIVVGTIPVPkgKP 99
Cdd:pfam03266  65 AVSGPRVGKYVVNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SD 137

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568957398  100 LALVEEIRKRRDVKVFNVTRDNRNSLLPDIV 130
Cdd:pfam03266 138 SPLLEEIRRREDVKIFVVTKENRDALPEEIL 168
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 20-129 2.11e-28

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 101.91  E-value: 2.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398  20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTpGIIVVGTIPVPKgkp 99
Cdd:cd19482   63 GAGSPKVGKYGVDVDELEEIAVPALRRALEEA----DVIIIDEIGPMELKSPKFREAVEEVLKS-DKPLLATVHRRS--- 134

                         90       100       110
                 ....*....|....*....|....*....|
gi 568957398 100 LALVEEIRKRrdVKVFNVTRDNRNSLLPDI 129
Cdd:cd19482  135 YPRLAEIRGL--GEVFWLTPENRDALPEEI 162
PRK13695 PRK13695
NTPase;
19-135 5.96e-27

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 98.45  E-value: 5.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398  19 PGKPecRVGQYVVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQML-STPGIIVVgtipVPKG 97
Cdd:PRK13695  67 PSRP--RVGKYVVNLEDLERIGIPALERALEEA----DVIIIDEIGKMELKSPKFVKAVEEVLdSEKPVIAT----LHRR 136

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568957398  98 KPLALVEEIRKRRDVKVFNVTRDNRNSLLPDIVAVVQS 135
Cdd:PRK13695 137 SVHPFVQEIKSRPGGRVYELTPENRDSLPFEILNRLKG 174
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
20-137 2.38e-24

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 91.89  E-value: 2.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398  20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTPgIIVVGTIPVpkgKP 99
Cdd:COG1618   66 IDSGPRVGKYGVDPEALEAIAVEALERALEEA----DLIVIDEIGKMELKSKGFREAIEEALDSD-KPVLATVHK---RS 137

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568957398 100 LALVEEIRKRRDVKVFNVTRDNRNSLLPDIVAVVQSSR 137
Cdd:COG1618  138 HPFLDEIRERGGVEVLEVTPENRDALPEEILELLREEL 175
 
Name Accession Description Interval E-value
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 20-130 3.95e-42

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 136.99  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398   20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCGpkhrVCIIDEIGKMELFSQPFIQAVRQMLStPGIIVVGTIPVPkgKP 99
Cdd:pfam03266  65 AVSGPRVGKYVVNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SD 137

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568957398  100 LALVEEIRKRRDVKVFNVTRDNRNSLLPDIV 130
Cdd:pfam03266 138 SPLLEEIRRREDVKIFVVTKENRDALPEEIL 168
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 20-129 2.11e-28

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 101.91  E-value: 2.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398  20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTpGIIVVGTIPVPKgkp 99
Cdd:cd19482   63 GAGSPKVGKYGVDVDELEEIAVPALRRALEEA----DVIIIDEIGPMELKSPKFREAVEEVLKS-DKPLLATVHRRS--- 134

                         90       100       110
                 ....*....|....*....|....*....|
gi 568957398 100 LALVEEIRKRrdVKVFNVTRDNRNSLLPDI 129
Cdd:cd19482  135 YPRLAEIRGL--GEVFWLTPENRDALPEEI 162
PRK13695 PRK13695
NTPase;
19-135 5.96e-27

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 98.45  E-value: 5.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398  19 PGKPecRVGQYVVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQML-STPGIIVVgtipVPKG 97
Cdd:PRK13695  67 PSRP--RVGKYVVNLEDLERIGIPALERALEEA----DVIIIDEIGKMELKSPKFVKAVEEVLdSEKPVIAT----LHRR 136

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568957398  98 KPLALVEEIRKRRDVKVFNVTRDNRNSLLPDIVAVVQS 135
Cdd:PRK13695 137 SVHPFVQEIKSRPGGRVYELTPENRDSLPFEILNRLKG 174
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
20-137 2.38e-24

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 91.89  E-value: 2.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957398  20 GKPECRVGQYVVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTPgIIVVGTIPVpkgKP 99
Cdd:COG1618   66 IDSGPRVGKYGVDPEALEAIAVEALERALEEA----DLIVIDEIGKMELKSKGFREAIEEALDSD-KPVLATVHK---RS 137

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568957398 100 LALVEEIRKRRDVKVFNVTRDNRNSLLPDIVAVVQSSR 137
Cdd:COG1618  138 HPFLDEIRERGGVEVLEVTPENRDALPEEILELLREEL 175
 
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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