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Conserved domains on  [gi|13385098|ref|NP_079912|]
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cancer-related nucleoside-triphosphatase homolog isoform 1 [Mus musculus]

Protein Classification

nucleoside-triphosphatase( domain architecture ID 10505514)

nucleoside-triphosphatase catalyzes the hydrolysis of nucleoside triphosphates to yield the corresponding nucleoside diphosphates and phosphate, similar to Staphylothermus marinus nucleoside-triphosphatase THEP1 and human cancer-related nucleoside-triphosphatase

Graphical summary

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List of domain hits

 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 ...
 4-182 9.16e-79

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: 232.13  E-value: 9.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098     4 HVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGSqplpgKPECRVGQYV 82
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRRIGFKIVDLaSGEEGWLARVGA-----VSGPRVGKYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098    83 VNLDSFEQLALPVLRNAGSSCGpkhrVCIIDEIGKMELFSQPFIQAVRQMLStPGIIVVGTIPVPkgKPLALVEEIRKRR 162
Cdd:pfam03266  76 VNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SDSPLLEEIRRRE 148

                         170       180
                  ....*....|....*....|
gi 13385098   163 DVKVFNVTRDNRNSLLPDIV 182
Cdd:pfam03266 149 DVKIFVVTKENRDALPEEIL 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 ...
 4-182 9.16e-79

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: 232.13  E-value: 9.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098     4 HVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGSqplpgKPECRVGQYV 82
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRRIGFKIVDLaSGEEGWLARVGA-----VSGPRVGKYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098    83 VNLDSFEQLALPVLRNAGSSCGpkhrVCIIDEIGKMELFSQPFIQAVRQMLStPGIIVVGTIPVPkgKPLALVEEIRKRR 162
Cdd:pfam03266  76 VNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SDSPLLEEIRRRE 148

                         170       180
                  ....*....|....*....|
gi 13385098   163 DVKVFNVTRDNRNSLLPDIV 182
Cdd:pfam03266 149 DVKIFVVTKENRDALPEEIL 168
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 5-181 1.84e-61

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: 188.19  E-value: 1.84e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098   5 VFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGsqplPGKPecRVGQYVV 83
Cdd:cd19482   1 IFITGPPGVGKTTLVLKVAELLKESGLKVGGFYTPEVREGGKRIGFKIVDLaSGERGWLARVG----AGSP--KVGKYGV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098  84 NLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTpGIIVVGTIPVPKgkpLALVEEIRKRrd 163
Cdd:cd19482  75 DVDELEEIAVPALRRALEEA----DVIIIDEIGPMELKSPKFREAVEEVLKS-DKPLLATVHRRS---YPRLAEIRGL-- 144

                       170
                ....*....|....*...
gi 13385098 164 VKVFNVTRDNRNSLLPDI 181
Cdd:cd19482 145 GEVFWLTPENRDALPEEI 162
PRK13695 PRK13695
NTPase;
5-187 6.28e-58

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 179.34  E-value: 6.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098    5 VFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGsqpLPGKPecRVGQYVV 83
Cdd:PRK13695   3 IGITGPPGVGKTTLVLKIAELLKEEGYKVGGFYTEEVREGGKRIGFKIIDLdTGEEGILARVG---FPSRP--RVGKYVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098   84 NLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQML-STPGIIVVgtipVPKGKPLALVEEIRKRR 162
Cdd:PRK13695  78 NLEDLERIGIPALERALEEA----DVIIIDEIGKMELKSPKFVKAVEEVLdSEKPVIAT----LHRRSVHPFVQEIKSRP 149

                        170       180
                 ....*....|....*....|....*
gi 13385098  163 DVKVFNVTRDNRNSLLPDIVAVVQS 187
Cdd:PRK13695 150 GGRVYELTPENRDSLPFEILNRLKG 174
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
3-189 3.80e-53

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 167.39  E-value: 3.80e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098   3 RHVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGsqplpGKPECRVGQY 81
Cdd:COG1618   1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRVGGFITPEVREGGRRVGFKLVDLaTGEEAILASVD-----IDSGPRVGKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098  82 VVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTPgIIVVGTIPVpkgKPLALVEEIRKR 161
Cdd:COG1618  76 GVDPEALEAIAVEALERALEEA----DLIVIDEIGKMELKSKGFREAIEEALDSD-KPVLATVHK---RSHPFLDEIRER 147

                       170       180
                ....*....|....*....|....*...
gi 13385098 162 RDVKVFNVTRDNRNSLLPDIVAVVQSSR 189
Cdd:COG1618 148 GGVEVLEVTPENRDALPEEILELLREEL 175
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-59 2.14e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13385098      3 RHVFLTGPPGVGKTTLIQKAIEVLQSSGLPV------DGFYTQEVRQEGKRIGFDVVTLSGAQ 59
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGViyidgeDILEEVLDQLLLIIVGGKKASGSGEL 65
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 4-18 7.82e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 36.12  E-value: 7.82e-03
                          10
                  ....*....|....*
gi 13385098     4 HVFLTGPPGVGKTTL 18
Cdd:TIGR00635  32 HLLLYGPPGLGKTTL 46
 
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 ...
 4-182 9.16e-79

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: 232.13  E-value: 9.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098     4 HVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGSqplpgKPECRVGQYV 82
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRRIGFKIVDLaSGEEGWLARVGA-----VSGPRVGKYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098    83 VNLDSFEQLALPVLRNAGSSCGpkhrVCIIDEIGKMELFSQPFIQAVRQMLStPGIIVVGTIPVPkgKPLALVEEIRKRR 162
Cdd:pfam03266  76 VNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SDSPLLEEIRRRE 148

                         170       180
                  ....*....|....*....|
gi 13385098   163 DVKVFNVTRDNRNSLLPDIV 182
Cdd:pfam03266 149 DVKIFVVTKENRDALPEEIL 168
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 5-181 1.84e-61

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: 188.19  E-value: 1.84e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098   5 VFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGsqplPGKPecRVGQYVV 83
Cdd:cd19482   1 IFITGPPGVGKTTLVLKVAELLKESGLKVGGFYTPEVREGGKRIGFKIVDLaSGERGWLARVG----AGSP--KVGKYGV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098  84 NLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTpGIIVVGTIPVPKgkpLALVEEIRKRrd 163
Cdd:cd19482  75 DVDELEEIAVPALRRALEEA----DVIIIDEIGPMELKSPKFREAVEEVLKS-DKPLLATVHRRS---YPRLAEIRGL-- 144

                       170
                ....*....|....*...
gi 13385098 164 VKVFNVTRDNRNSLLPDI 181
Cdd:cd19482 145 GEVFWLTPENRDALPEEI 162
PRK13695 PRK13695
NTPase;
5-187 6.28e-58

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 179.34  E-value: 6.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098    5 VFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGsqpLPGKPecRVGQYVV 83
Cdd:PRK13695   3 IGITGPPGVGKTTLVLKIAELLKEEGYKVGGFYTEEVREGGKRIGFKIIDLdTGEEGILARVG---FPSRP--RVGKYVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098   84 NLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQML-STPGIIVVgtipVPKGKPLALVEEIRKRR 162
Cdd:PRK13695  78 NLEDLERIGIPALERALEEA----DVIIIDEIGKMELKSPKFVKAVEEVLdSEKPVIAT----LHRRSVHPFVQEIKSRP 149

                        170       180
                 ....*....|....*....|....*
gi 13385098  163 DVKVFNVTRDNRNSLLPDIVAVVQS 187
Cdd:PRK13695 150 GGRVYELTPENRDSLPFEILNRLKG 174
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
3-189 3.80e-53

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 167.39  E-value: 3.80e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098   3 RHVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTL-SGAQGPLSRVGsqplpGKPECRVGQY 81
Cdd:COG1618   1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRVGGFITPEVREGGRRVGFKLVDLaTGEEAILASVD-----IDSGPRVGKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098  82 VVNLDSFEQLALPVLRNAGSSCgpkhRVCIIDEIGKMELFSQPFIQAVRQMLSTPgIIVVGTIPVpkgKPLALVEEIRKR 161
Cdd:COG1618  76 GVDPEALEAIAVEALERALEEA----DLIVIDEIGKMELKSKGFREAIEEALDSD-KPVLATVHK---RSHPFLDEIRER 147

                       170       180
                ....*....|....*....|....*...
gi 13385098 162 RDVKVFNVTRDNRNSLLPDIVAVVQSSR 189
Cdd:COG1618 148 GGVEVLEVTPENRDALPEEILELLREEL 175
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 2-33 7.18e-07

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 48.43  E-value: 7.18e-07
                        10        20        30
                ....*....|....*....|....*....|..
gi 13385098   2 SRHVFLTGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:COG0507 140 RRVSVLTGGAGTGKTTTLRALLAALEALGLRV 171
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 2-33 1.89e-05

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 42.93  E-value: 1.89e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 13385098   2 SRHVFLTGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:cd17933  12 NRVSVLTGGAGTGKTTTLKALLAALEAEGKRV 43
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 5-44 4.60e-05

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 40.67  E-value: 4.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 13385098     5 VFLTGPPGVGKTTLIQK-AIEVLQSSGLPVDGFYTQEVRQE 44
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYlARALLKKLGLPKDSVYSRNPDDD 41
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 3-55 1.15e-04

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 41.01  E-value: 1.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13385098     3 RHVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGF--YTQEVRQEGKRIGFDVVTL 55
Cdd:pfam13604  19 RVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLapTGRAAKVLGEELGIPADTI 73
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 3-33 1.80e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.21  E-value: 1.80e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 13385098   3 RHVFLTGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:cd00009  20 KNLLLYGPPGTGKTTLARAIANELFRPGAPF 50
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-59 2.14e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13385098      3 RHVFLTGPPGVGKTTLIQKAIEVLQSSGLPV------DGFYTQEVRQEGKRIGFDVVTLSGAQ 59
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGViyidgeDILEEVLDQLLLIIVGGKKASGSGEL 65
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
4-18 1.28e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.57  E-value: 1.28e-03
                         10
                 ....*....|....*
gi 13385098    4 HVFLTGPPGVGKTTL 18
Cdd:PRK00080  53 HVLLYGPPGLGKTTL 67
COG3899 COG3899
Predicted ATPase [General function prediction only];
2-33 1.57e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 38.69  E-value: 1.57e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 13385098    2 SRHVFLTGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:COG3899  311 GELVLVSGEAGIGKSRLVRELARRARARGGRV 342
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 5-41 2.27e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 37.61  E-value: 2.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 13385098    5 VFLTGPPGVGKTTLIQKAIEVLQSSG------LPVDGF-YTQEV 41
Cdd:PRK09270  36 VGIAGPPGAGKSTLAEFLEALLQQDGelpaiqVPMDGFhLDNAV 79
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 4-18 2.41e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 37.75  E-value: 2.41e-03
                        10
                ....*....|....*
gi 13385098   4 HVFLTGPPGVGKTTL 18
Cdd:COG2255  56 HVLLYGPPGLGKTTL 70
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 3-23 2.81e-03

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 37.45  E-value: 2.81e-03
                        10        20
                ....*....|....*....|.
gi 13385098   3 RHVFLTGPPGVGKTTLIqKAI 23
Cdd:COG0714  32 GHLLLEGVPGVGKTTLA-KAL 51
COG3911 COG3911
Predicted ATPase [General function prediction only];
1-33 3.54e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 36.72  E-value: 3.54e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 13385098   1 MSRHVFLTGPPGVGKTTLiqkaIEVLQSSGLPV 33
Cdd:COG3911   2 MTRRIVITGGPGSGKTTL----LNALARRGYAC 30
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 5-33 3.57e-03

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 36.84  E-value: 3.57e-03
                        10        20
                ....*....|....*....|....*....
gi 13385098   5 VFLTGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:cd18037  15 VFFTGSAGTGKSYLLRRIIRALPSRPKRV 43
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 3-141 3.83e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 36.33  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385098     3 RHVFLTGPPGVGKTTLIQKAIEVLQSSG-----------LPVDGFYT-----QEVRQEGKRIGFDVVTLSGAQGPLSRVG 66
Cdd:pfam13191  25 PSVLLTGEAGTGKTTLLRELLRALERDGgyflrgkcdenLPYSPLLEaltreGLLRQLLDELESSLLEAWRAALLEALAP 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13385098    67 SQPLPGKPECRVgqyvvnLDSFEQLAlpvlrnAGSSCGPKHRVCIIDEIGKMELFSQPFIQAVRQMLSTPGIIVV 141
Cdd:pfam13191 105 VPELPGDLAERL------LDLLLRLL------DLLARGERPLVLVLDDLQWADEASLQLLAALLRLLESLPLLVV 167
COG3903 COG3903
Predicted ATPase [General function prediction only];
2-25 5.20e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 36.92  E-value: 5.20e-03
                        10        20
                ....*....|....*....|....
gi 13385098   2 SRHVFLTGPPGVGKTTLiqkAIEV 25
Cdd:COG3903 176 ARLVTLTGPGGVGKTRL---ALEV 196
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
2-28 5.86e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 36.75  E-value: 5.86e-03
                        10        20
                ....*....|....*....|....*..
gi 13385098   2 SRHVFLTGPPGVGKTTLIQKAIEVLQS 28
Cdd:COG1474  51 PSNVLIYGPTGTGKTAVAKYVLEELEE 77
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
 8-33 6.25e-03

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 36.20  E-value: 6.25e-03
                          10        20
                  ....*....|....*....|....*.
gi 13385098     8 TGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:pfam03029   2 VGPAGSGKTTFVGALSEILPLRGRPV 27
PRK04040 PRK04040
adenylate kinase; Provisional
 1-26 6.47e-03

adenylate kinase; Provisional


Pssm-ID: 235210  Cd Length: 188  Bit Score: 36.02  E-value: 6.47e-03
                         10        20
                 ....*....|....*....|....*.
gi 13385098    1 MSRHVFLTGPPGVGKTTLIQKAIEVL 26
Cdd:PRK04040   1 MMKVVVVTGVPGVGKTTVLNKALEKL 26
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 9-33 6.89e-03

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 36.09  E-value: 6.89e-03
                        10        20
                ....*....|....*....|....*
gi 13385098   9 GPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:cd01672   7 GIDGAGKTTLIELLAERLEARGYEV 31
AAA_19 pfam13245
AAA domain;
1-30 6.91e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 35.27  E-value: 6.91e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 13385098     1 MSRHVFLTGPPGVGKTTLIQKAIEVLQSSG 30
Cdd:pfam13245  10 PSKVVLLTGGPGTGKTTTIRHIVALLVALG 39
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 7-29 7.66e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 35.92  E-value: 7.66e-03
                        10        20
                ....*....|....*....|...
gi 13385098   7 LTGPPGVGKTTLIQKAIEVLQSS 29
Cdd:COG3267  48 LTGEVGTGKTTLLRRLLERLPDD 70
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 4-18 7.82e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 36.12  E-value: 7.82e-03
                          10
                  ....*....|....*
gi 13385098     4 HVFLTGPPGVGKTTL 18
Cdd:TIGR00635  32 HLLLYGPPGLGKTTL 46
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 4-18 8.99e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 35.17  E-value: 8.99e-03
                          10
                  ....*....|....*
gi 13385098     4 HVFLTGPPGVGKTTL 18
Cdd:pfam05496  35 HVLLYGPPGLGKTTL 49
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 4-33 9.56e-03

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 35.63  E-value: 9.56e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 13385098   4 HVFLTGPPGVGKTTLIQKAIEVLQSSGLPV 33
Cdd:cd03114  48 RVGITGPPGAGKSTLIEALGRLLREQGHRV 77
 
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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