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Conserved domains on  [gi|14150100|ref|NP_115700|]
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cancer-related nucleoside-triphosphatase isoform 1 [Homo sapiens]

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 9.06e-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: 9.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100     4 HVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGlepppGKRECRVGQYV 82
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRRIGFKIVDLaSGEEGWLARVG-----AVSGPRVGKYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100    83 VDLTSFEQLALPVLRNADCSSGpgqrVCVIDEIGKMELFSQLFIQAVRQTLStPGTIILGTIPVPkgKPLALVEEIRNRK 162
Cdd:pfam03266  76 VNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SDSPLLEEIRRRE 148

                         170       180
                  ....*....|....*....|
gi 14150100   163 DVKVFNVTKENRNHLLPDIV 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 9.06e-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: 9.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100     4 HVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGlepppGKRECRVGQYV 82
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRRIGFKIVDLaSGEEGWLARVG-----AVSGPRVGKYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100    83 VDLTSFEQLALPVLRNADCSSGpgqrVCVIDEIGKMELFSQLFIQAVRQTLStPGTIILGTIPVPkgKPLALVEEIRNRK 162
Cdd:pfam03266  76 VNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SDSPLLEEIRRRE 148

                         170       180
                  ....*....|....*....|
gi 14150100   163 DVKVFNVTKENRNHLLPDIV 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 1.85e-63

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: 193.20  E-value: 1.85e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   5 VFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGLEPPpgkrecRVGQYVV 83
Cdd:cd19482   1 IFITGPPGVGKTTLVLKVAELLKESGLKVGGFYTPEVREGGKRIGFKIVDLaSGERGWLARVGAGSP------KVGKYGV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100  84 DLTSFEQLALPVLRNADCssgpGQRVCVIDEIGKMELFSQLFIQAVRQTLSTpGTIILGTIPVPKgkpLALVEEIRNRkd 163
Cdd:cd19482  75 DVDELEEIAVPALRRALE----EADVIIIDEIGPMELKSPKFREAVEEVLKS-DKPLLATVHRRS---YPRLAEIRGL-- 144

                       170
                ....*....|....*...
gi 14150100 164 VKVFNVTKENRNHLLPDI 181
Cdd:cd19482 145 GEVFWLTPENRDALPEEI 162
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
3-189 4.73e-53

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 167.00  E-value: 4.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGLEPPPgkrecRVGQY 81
Cdd:COG1618   1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRVGGFITPEVREGGRRVGFKLVDLaTGEEAILASVDIDSGP-----RVGKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100  82 VVDLTSFEQLALPVLRNADCSSgpgqRVCVIDEIGKMELFSQLFIQAVRQTLSTPgTIILGTIPVpkgKPLALVEEIRNR 161
Cdd:COG1618  76 GVDPEALEAIAVEALERALEEA----DLIVIDEIGKMELKSKGFREAIEEALDSD-KPVLATVHK---RSHPFLDEIRER 147

                       170       180
                ....*....|....*....|....*...
gi 14150100 162 KDVKVFNVTKENRNHLLPDIVTCVQSSR 189
Cdd:COG1618 148 GGVEVLEVTPENRDALPEEILELLREEL 175
PRK13695 PRK13695
NTPase;
5-182 3.28e-52

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 165.09  E-value: 3.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100    5 VFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGLEPPPgkrecRVGQYVV 83
Cdd:PRK13695   3 IGITGPPGVGKTTLVLKIAELLKEEGYKVGGFYTEEVREGGKRIGFKIIDLdTGEEGILARVGFPSRP-----RVGKYVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   84 DLTSFEQLALPVLRNADCSSgpgqRVCVIDEIGKMELFSQLFIQAVRQTLSTPGTIIlGTIP---VPKgkplaLVEEIRN 160
Cdd:PRK13695  78 NLEDLERIGIPALERALEEA----DVIIIDEIGKMELKSPKFVKAVEEVLDSEKPVI-ATLHrrsVHP-----FVQEIKS 147

                        170       180
                 ....*....|....*....|..
gi 14150100  161 RKDVKVFNVTKENRNHLLPDIV 182
Cdd:PRK13695 148 RPGGRVYELTPENRDSLPFEIL 169
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-68 4.27e-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: 38.89  E-value: 4.27e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100      3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPV----DGFYTEEVRQGGRRIGFDVVTLSGTRGPLSRVGLE 68
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGViyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 4-20 2.06e-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: 38.05  E-value: 2.06e-03
                          10
                  ....*....|....*..
gi 14150100     4 HVFLTGPPGVGKTTLIH 20
Cdd:TIGR00635  32 HLLLYGPPGLGKTTLAH 48
 
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 9.06e-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: 9.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100     4 HVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGlepppGKRECRVGQYV 82
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRRIGFKIVDLaSGEEGWLARVG-----AVSGPRVGKYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100    83 VDLTSFEQLALPVLRNADCSSGpgqrVCVIDEIGKMELFSQLFIQAVRQTLStPGTIILGTIPVPkgKPLALVEEIRNRK 162
Cdd:pfam03266  76 VNVESFEEIAVPALRRALEEAD----LIIIDEIGPMELKSKKFREAVREVLD-SGKPVLAVIHRR--SDSPLLEEIRRRE 148

                         170       180
                  ....*....|....*....|
gi 14150100   163 DVKVFNVTKENRNHLLPDIV 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 1.85e-63

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: 193.20  E-value: 1.85e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   5 VFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGLEPPpgkrecRVGQYVV 83
Cdd:cd19482   1 IFITGPPGVGKTTLVLKVAELLKESGLKVGGFYTPEVREGGKRIGFKIVDLaSGERGWLARVGAGSP------KVGKYGV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100  84 DLTSFEQLALPVLRNADCssgpGQRVCVIDEIGKMELFSQLFIQAVRQTLSTpGTIILGTIPVPKgkpLALVEEIRNRkd 163
Cdd:cd19482  75 DVDELEEIAVPALRRALE----EADVIIIDEIGPMELKSPKFREAVEEVLKS-DKPLLATVHRRS---YPRLAEIRGL-- 144

                       170
                ....*....|....*...
gi 14150100 164 VKVFNVTKENRNHLLPDI 181
Cdd:cd19482 145 GEVFWLTPENRDALPEEI 162
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
3-189 4.73e-53

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 167.00  E-value: 4.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGLEPPPgkrecRVGQY 81
Cdd:COG1618   1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRVGGFITPEVREGGRRVGFKLVDLaTGEEAILASVDIDSGP-----RVGKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100  82 VVDLTSFEQLALPVLRNADCSSgpgqRVCVIDEIGKMELFSQLFIQAVRQTLSTPgTIILGTIPVpkgKPLALVEEIRNR 161
Cdd:COG1618  76 GVDPEALEAIAVEALERALEEA----DLIVIDEIGKMELKSKGFREAIEEALDSD-KPVLATVHK---RSHPFLDEIRER 147

                       170       180
                ....*....|....*....|....*...
gi 14150100 162 KDVKVFNVTKENRNHLLPDIVTCVQSSR 189
Cdd:COG1618 148 GGVEVLEVTPENRDALPEEILELLREEL 175
PRK13695 PRK13695
NTPase;
5-182 3.28e-52

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 165.09  E-value: 3.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100    5 VFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTL-SGTRGPLSRVGLEPPPgkrecRVGQYVV 83
Cdd:PRK13695   3 IGITGPPGVGKTTLVLKIAELLKEEGYKVGGFYTEEVREGGKRIGFKIIDLdTGEEGILARVGFPSRP-----RVGKYVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   84 DLTSFEQLALPVLRNADCSSgpgqRVCVIDEIGKMELFSQLFIQAVRQTLSTPGTIIlGTIP---VPKgkplaLVEEIRN 160
Cdd:PRK13695  78 NLEDLERIGIPALERALEEA----DVIIIDEIGKMELKSPKFVKAVEEVLDSEKPVI-ATLHrrsVHP-----FVQEIKS 147

                        170       180
                 ....*....|....*....|..
gi 14150100  161 RKDVKVFNVTKENRNHLLPDIV 182
Cdd:PRK13695 148 RPGGRVYELTPENRDSLPFEIL 169
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 5-38 1.43e-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: 42.21  E-value: 1.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 14150100     5 VFLTGPPGVGKTTLIHK-ASEVLKSSGVPVDGFYT 38
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYlARALLKKLGLPKDSVYS 35
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 3-33 2.77e-05

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: 43.81  E-value: 2.77e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 14150100   3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPV 33
Cdd:COG0507 141 RVSVLTGGAGTGKTTTLRALLAALEALGLRV 171
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 3-51 4.95e-05

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: 41.75  E-value: 4.95e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 14150100   3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFD 51
Cdd:cd00009  20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF 68
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 5-47 9.59e-05

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 41.46  E-value: 9.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 14150100    5 VFLTGPPGVGKTTL------IHKASEVLKSSGVPVDGF--YTEEVRQGGRR 47
Cdd:PRK09270  36 VGIAGPPGAGKSTLaefleaLLQQDGELPAIQVPMDGFhlDNAVLDAHGLR 86
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
1-161 1.82e-04

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.11  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100   1 MARHVFLTGPPGVGKTTLIHK-ASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTlsgtrgplsrvgLEPPPGKRECRVG 79
Cdd:COG0470  17 LPHALLLHGPPGIGKTTLALAlARDLLCENPEGGKACGQCHSRLMAAGNHPDLLE------------LNPEEKSDQIGID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100  80 QyVVDLTSFEQLAlpvlrnadcSSGPGQRVCVIDEIGKMELFSQlfiQAVRQTLSTPG---TIILGTipvpkGKPLALVE 156
Cdd:COG0470  85 Q-IRELGEFLSLT---------PLEGGRKVVIIDEADAMNEAAA---NALLKTLEEPPkntPFILIA-----NDPSRLLP 146


                ....*
gi 14150100 157 EIRNR 161
Cdd:COG0470 147 TIRSR 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-68 4.27e-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: 38.89  E-value: 4.27e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150100      3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPV----DGFYTEEVRQGGRRIGFDVVTLSGTRGPLSRVGLE 68
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGViyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 3-26 4.93e-04

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: 39.77  E-value: 4.93e-04
                        10        20
                ....*....|....*....|....
gi 14150100   3 RHVFLTGPPGVGKTTLIHKASEVL 26
Cdd:COG0714  32 GHLLLEGVPGVGKTTLAKALARAL 55
COG3911 COG3911
Predicted ATPase [General function prediction only];
1-48 5.65e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 39.03  E-value: 5.65e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 14150100   1 MARHVFLTGPPGVGKTTLIhkasEVLKSSGVPVdgfyTEEVrqgGRRI 48
Cdd:COG3911   2 MTRRIVITGGPGSGKTTLL----NALARRGYAC----VPEA---GREI 38
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
4-20 1.20e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.57  E-value: 1.20e-03
                         10
                 ....*....|....*..
gi 14150100    4 HVFLTGPPGVGKTTLIH 20
Cdd:PRK00080  53 HVLLYGPPGLGKTTLAN 69
COG3899 COG3899
Predicted ATPase [General function prediction only];
2-33 1.32e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 39.07  E-value: 1.32e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 14150100    2 ARHVFLTGPPGVGKTTLIHKASEVLKSSGVPV 33
Cdd:COG3899  311 GELVLVSGEAGIGKSRLVRELARRARARGGRV 342
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 4-20 2.06e-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: 38.05  E-value: 2.06e-03
                          10
                  ....*....|....*..
gi 14150100     4 HVFLTGPPGVGKTTLIH 20
Cdd:TIGR00635  32 HLLLYGPPGLGKTTLAH 48
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 4-20 2.09e-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: 2.09e-03
                        10
                ....*....|....*..
gi 14150100   4 HVFLTGPPGVGKTTLIH 20
Cdd:COG2255  56 HVLLYGPPGLGKTTLAH 72
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 4-69 2.22e-03

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 36.89  E-value: 2.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14150100     4 HVFLTGPPGVGKTTLIHKASEVLKSSG---VPVDGFYTEEVRQGGRRIgfDVVTLSGTRGPLSRVGLEP 69
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPvfyVQLTRDTTEEDLFGRRNI--DPGGASWVDGPLVRAAREG 67
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 2-36 2.54e-03

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: 37.16  E-value: 2.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 14150100     2 ARHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGF 36
Cdd:pfam13604  18 DRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGL 52
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 3-33 3.07e-03

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: 36.38  E-value: 3.07e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 14150100   3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPV 33
Cdd:cd17933  13 RVSVLTGGAGTGKTTTLKALLAALEAEGKRV 43
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 5-50 5.10e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 36.15  E-value: 5.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14150100    5 VFLTGPPGVGKTTLIHKASEVLKSSGVPVD---------------GFYTEEVRQGGRRIGF 50
Cdd:PRK00889   7 VWFTGLSGAGKTTIARALAEKLREAGYPVEvldgdavrtnlskglGFSKEDRDTNIRRIGF 67
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 5-51 5.64e-03

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 36.22  E-value: 5.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 14150100   5 VFLTGPPGVGKTTLIHKASEVLKSSGVPV---DGfytEEVRQG-GRRIGFD 51
Cdd:COG0529  19 VWFTGLSGSGKSTLANALERRLFERGRHVyllDG---DNVRHGlNKDLGFS 66
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 4-20 5.68e-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: 35.94  E-value: 5.68e-03
                          10
                  ....*....|....*..
gi 14150100     4 HVFLTGPPGVGKTTLIH 20
Cdd:pfam05496  35 HVLLYGPPGLGKTTLAN 51
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 3-33 6.47e-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: 35.94  E-value: 6.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 14150100     3 RHVFLTGPPGVGKTTLIHKASEVLKSSGVPV 33
Cdd:pfam13191  25 PSVLLTGEAGTGKTTLLRELLRALERDGGYF 55
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 5-51 6.74e-03

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 35.53  E-value: 6.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 14150100   5 VFLTGPPGVGKTTLIHKASEVLKSSGVPV---DGfytEEVRQG-GRRIGFD 51
Cdd:cd02027   2 IWLTGLSGSGKSTIARALEEKLFQRGRPVyvlDG---DNVRHGlNKDLGFS 49
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 5-51 7.20e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 35.37  E-value: 7.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 14150100     5 VFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQG-GRRIGFD 51
Cdd:pfam01583   5 IWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGlNKDLGFS 52
PRK04040 PRK04040
adenylate kinase; Provisional
 1-27 8.92e-03

adenylate kinase; Provisional


Pssm-ID: 235210  Cd Length: 188  Bit Score: 35.64  E-value: 8.92e-03
                         10        20
                 ....*....|....*....|....*..
gi 14150100    1 MARHVFLTGPPGVGKTTLIHKASEVLK 27
Cdd:PRK04040   1 MMKVVVVTGVPGVGKTTVLNKALEKLK 27
 
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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