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Conserved domains on  [gi|1181024740|ref|WP_084437407|]
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MULTISPECIES: MoxR family ATPase [Actinomycetaceae]

Protein Classification

AAA family ATPase( domain architecture ID 11431245)

AAA family ATPase with an AAA (ATPases Associated with various cellular Activities) domain functions as a modulator of stress response pathways and may have a chaperone-like role for the maturation of specific protein complexes or for the insertion of cofactors into proteins; similar to MoxR that is involved in the formation of active methanol dehydrogenase

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  16072036|11916378|15037234|17897320|18466635
SCOP:  2000039

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 68-361 9.47e-146

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: 414.18  E-value: 9.47e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  68 ALKAEIGKAVVGQDGATTGLIVALVAGGHALLEGVPGVAKTLLVRTLARALDVEMARIQFTPDLMPADITGSMVWDAGRS 147
Cdd:COG0714     5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 148 EFVFREGPVFTNLLLADEINRTPPKTQSALLESMEEHTVSIDGATRALPDPFMVIATQNPVEYEGTYPLPEAQLDRFLVK 227
Cdd:COG0714    85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 228 LELPLPSREAEIDIVARHQAGfnpmslAEAGIRPVAGAADIHAAAVAASRVEIAPAVMAYLVDVCRATRTSPAVRLGVSP 307
Cdd:COG0714   165 LYIGYPDAEEEREILRRHTGR------HLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSP 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181024740 308 RGATALLRTSRVWAFLQGRGFVTPDDVKTMAPVTLAHRLGLRAEANLEGITATD 361
Cdd:COG0714   239 RASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTADD 292
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 68-361 9.47e-146

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: 414.18  E-value: 9.47e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  68 ALKAEIGKAVVGQDGATTGLIVALVAGGHALLEGVPGVAKTLLVRTLARALDVEMARIQFTPDLMPADITGSMVWDAGRS 147
Cdd:COG0714     5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 148 EFVFREGPVFTNLLLADEINRTPPKTQSALLESMEEHTVSIDGATRALPDPFMVIATQNPVEYEGTYPLPEAQLDRFLVK 227
Cdd:COG0714    85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 228 LELPLPSREAEIDIVARHQAGfnpmslAEAGIRPVAGAADIHAAAVAASRVEIAPAVMAYLVDVCRATRTSPAVRLGVSP 307
Cdd:COG0714   165 LYIGYPDAEEEREILRRHTGR------HLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSP 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181024740 308 RGATALLRTSRVWAFLQGRGFVTPDDVKTMAPVTLAHRLGLRAEANLEGITATD 361
Cdd:COG0714   239 RASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTADD 292
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 96-225 2.94e-88

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 262.11  E-value: 2.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLARALDVEMARIQFTPDLMPADITGSMVWDAGRSEFVFREGPVFTNLLLADEINRTPPKTQS 175
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1181024740 176 ALLESMEEHTVSIDGATRALPDPFMVIATQNPVEYEGTYPLPEAQLDRFL 225
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFL 130
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 78-232 1.96e-08

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: 52.92  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  78 VGQDGATTGLIVAL--VAGGHALLEGVPGVAKTLLVRTLARAL---DVEMARIQ---FTPDLMPADITGSMVWDAGRSEF 149
Cdd:cd00009     1 VGQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNasdLLEGLVVAELFGHFLVRLLFELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 150 VFREGPVftnlLLADEINRTPPKTQSALLESMEEHTVsidgaTRALPDPFMVIATQNPVEYEgtyPLPEAQLDRFLVKLE 229
Cdd:cd00009    81 EKAKPGV----LFIDEIDSLSRGAQNALLRVLETLND-----LRIDRENVRVIGATNRPLLG---DLDRALYDRLDIRIV 148


                  ...
gi 1181024740 230 LPL 232
Cdd:cd00009   149 IPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 94-233 1.66e-03

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: 38.51  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740   94 GGHALLEGVPGVAKTLLVRTLARAL----------DVEMARIQFTPDLMPADITGSMVWDAGRS------EFVFREGPVf 157
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppgggviyiDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlalALARKLKPD- 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1181024740  158 tnLLLADEINRTPPKTQSALLESMEEHTVsidGATRALPDPFMVIATQNPVeyegTYPLPEAQLDRFLVKLELPLP 233
Cdd:smart00382  81 --VLILDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDE----KDLGPALLRRRFDRRIVLLLI 147
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 68-361 9.47e-146

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: 414.18  E-value: 9.47e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  68 ALKAEIGKAVVGQDGATTGLIVALVAGGHALLEGVPGVAKTLLVRTLARALDVEMARIQFTPDLMPADITGSMVWDAGRS 147
Cdd:COG0714     5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 148 EFVFREGPVFTNLLLADEINRTPPKTQSALLESMEEHTVSIDGATRALPDPFMVIATQNPVEYEGTYPLPEAQLDRFLVK 227
Cdd:COG0714    85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 228 LELPLPSREAEIDIVARHQAGfnpmslAEAGIRPVAGAADIHAAAVAASRVEIAPAVMAYLVDVCRATRTSPAVRLGVSP 307
Cdd:COG0714   165 LYIGYPDAEEEREILRRHTGR------HLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSP 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1181024740 308 RGATALLRTSRVWAFLQGRGFVTPDDVKTMAPVTLAHRLGLRAEANLEGITATD 361
Cdd:COG0714   239 RASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTADD 292
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 96-225 2.94e-88

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 262.11  E-value: 2.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLARALDVEMARIQFTPDLMPADITGSMVWDAGRSEFVFREGPVFTNLLLADEINRTPPKTQS 175
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1181024740 176 ALLESMEEHTVSIDGATRALPDPFMVIATQNPVEYEGTYPLPEAQLDRFL 225
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFL 130
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 293-364 2.19e-18

AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465538 [Multi-domain]  Cd Length: 73  Bit Score: 78.41  E-value: 2.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181024740 293 RATRTSPAVRLGVSP-RGATALLRTSRVWAFLQGRGFVTPDDVKTMAPVTLAHRlgLRAEANLEGITATDVVS 364
Cdd:pfam17863   1 LATRAHLAIALGVSPrRADLALLRAARALAALEGRDYVTPEDVKEAAPLVLAHR--LRREPEAEGETAEEILE 71
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 96-224 1.79e-17

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: 78.10  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLARALD---VEMarIQFTPDLMPADITGSMVWDAGRSEFV-------FREGPVftnlLLADE 165
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrpVFY--VQLTRDTTEEDLFGRRNIDPGGASWVdgplvraAREGEI----AVLDE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1181024740 166 INRTPPKTQSALLESMEE---HTVSIDGATRALPDPFMVIATQNPVEYEGTyPLPEAQLDRF 224
Cdd:pfam07728  75 INRANPDVLNSLLSLLDErrlLLPDGGELVKAAPDGFRLIATMNPLDRGLN-ELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 78-232 1.96e-08

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: 52.92  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  78 VGQDGATTGLIVAL--VAGGHALLEGVPGVAKTLLVRTLARAL---DVEMARIQ---FTPDLMPADITGSMVWDAGRSEF 149
Cdd:cd00009     1 VGQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNasdLLEGLVVAELFGHFLVRLLFELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 150 VFREGPVftnlLLADEINRTPPKTQSALLESMEEHTVsidgaTRALPDPFMVIATQNPVEYEgtyPLPEAQLDRFLVKLE 229
Cdd:cd00009    81 EKAKPGV----LFIDEIDSLSRGAQNALLRVLETLND-----LRIDRENVRVIGATNRPLLG---DLDRALYDRLDIRIV 148


                  ...
gi 1181024740 230 LPL 232
Cdd:cd00009   149 IPL 151
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 96-336 3.33e-07

MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350658 [Multi-domain]  Cd Length: 311  Bit Score: 51.57  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLA----RALDVEMARiqftpdLMPADITGSMVWDAGRSEFVFREGPvftnLLLA-------D 164
Cdd:cd17706    43 HILLVGDPGTAKSQILKYVLkiapRGVYTSGKG------SSGAGLTAAVVRDSETGEWYLEAGA----LVLAdggvcciD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 165 EINRTPPKTQSALLESMEEHTVSID--GATRALPDPFMVIATQNPVeyEGTYP----------LPEAQLDRF-LVKLELP 231
Cdd:cd17706   113 EFDKMKELDRTALHEAMEQQTISIAkaGIVTTLNARCSILAAANPK--GGRYNpklspieninLPSPLLSRFdLIFVIRD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 232 LPSREAEIDI---VARHQAGFNPMSLAEAGIRPVAGAADIHAAAVAASRVE---IAPAVMAYLVDVCRATRTSPAVR--L 303
Cdd:cd17706   191 DPDEERDEELaehIIDLHRGSDPEEQVKPEEDGIPIDIELLRKYILYARQIhpkISEEAREKLVRWYVELRKESERRstI 270

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1181024740 304 GVSPRGATALLRTSRVWAFLQGRGFVTPDDVKT 336
Cdd:cd17706   271 PITARQLESVIRLAEAHAKMRLSEVVTEEDVEE 303
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
276-346 4.73e-07

Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 50.90  E-value: 4.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1181024740 276 SRVEIAPAVMAYLVDVCratrtspaVRLGV-SPRGATALLRTSRVWAFLQGRGFVTPDDVKTMAPVTLAHRL 346
Cdd:COG1239   256 PEVTIPDELLRYIAELC--------IALGVdGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRL 319
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 98-232 4.87e-06

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 45.66  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  98 LLEGVPGVAKTLLVRTLARALDVEMARIQftpdlmPADITGSMVWDAGRS-----EFVFREGPVftnLLLADEI------ 166
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEIS------GSELVSKYVGESEKRlrelfEAAKKLAPC---VIFIDEIdalags 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181024740 167 -----NRTPPKTQSALLESMEEHTVSIdgatralpDPFMVIATQNPVEyegtyPLPEAQLDRFLVKLELPL 232
Cdd:pfam00004  73 rgsggDSESRRVVNQLLTELDGFTSSN--------SKVIVIAATNRPD-----KLDPALLGRFDRIIEFPL 130
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 91-245 4.54e-05

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 44.90  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  91 LVAGGHALLEGVPGVAKTLLVRTLARALDVEMARIQftpdlmPADITGSMVwdaGRSE----FVFRE----GPVftnLLL 162
Cdd:COG0464   188 LPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD------LSDLVSKYV---GETEknlrEVFDKarglAPC---VLF 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 163 ADEI-----NRTPPKTQ------SALLESMEEHTvsidgatralpDPFMVIATQNPVEYegtypLPEAQLDRFLVKLELP 231
Cdd:COG0464   256 IDEAdalagKRGEVGDGvgrrvvNTLLTEMEELR-----------SDVVVIAATNRPDL-----LDPALLRRFDEIIFFP 319

                         170
                  ....*....|....
gi 1181024740 232 LPSREAEIDIVARH 245
Cdd:COG0464   320 LPDAEERLEIFRIH 333
bpMoxR pfam20030
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ...
 72-119 5.38e-05

MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the MoxR-vWA-beta-propeller ternary systems, a class of NTP-dependent biological conflict systems.


Pssm-ID: 437862 [Multi-domain]  Cd Length: 205  Bit Score: 43.77  E-value: 5.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1181024740  72 EIGKAVVGQDGATTGLIVALVAGGHALLEGVPGVAKTLLVRTLARALD 119
Cdd:pfam20030   9 PLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLG 56
MCM8 cd17759
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a ...
 96-335 1.75e-04

DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a complex with Mcm9 that is required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350665 [Multi-domain]  Cd Length: 289  Bit Score: 42.91  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLA----RALDV---EMARIQFTPDLMPADITGSMVWDAGrsEFVFREGPVFTnlllADEINR 168
Cdd:cd17759    45 HVLIVGDPGLGKSQMLQAACniapRGVYVcgnTTTTSGLTVTLTKDGRSGDFALEAG--ALVLGDQGICG----IDEFDK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 169 TPPKtQSALLESMEEHTVSI--DGATRALPDPFMVIATQNPV--EYEGTYPLPE------AQLDRF-LVKLELPLPSREA 237
Cdd:cd17759   119 MGSQ-HQALLEAMEQQSVSLakAGVVCSLPARTSVIAAANPVggHYNKGKTVSEnlkmgpALLSRFdLVFILLDTPSEEH 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 238 EIDIVARHQAGFNPMSLAEAGIRPVAGAadihaaavaasrvEIAPAVMAYLVDVcrATRTSPAVRLGVSPRGATALLRTS 317
Cdd:cd17759   198 DHLLSEHHQLLRKYISYARQYVNPVLSK-------------DASEALQEFYLEL--RKQNQLADSSPITTRQLESLIRLT 262

                         250
                  ....*....|....*...
gi 1181024740 318 RVWAFLQGRGFVTPDDVK 335
Cdd:cd17759   263 EARARLELREEATKEDAE 280
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
77-118 3.36e-04

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 42.10  E-value: 3.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1181024740  77 VVGQDGATTGLIVALVAG--GHA-LLEGVPGVAKTLLVRTLARAL 118
Cdd:COG2812    12 VVGQEHVVRTLKNALASGrlAHAyLFTGPRGVGKTTLARILAKAL 56
MCM pfam00493
MCM P-loop domain;
96-245 4.69e-04

MCM P-loop domain;


Pssm-ID: 459830 [Multi-domain]  Cd Length: 224  Bit Score: 40.98  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLARALdvemARIQFTP--DLMPADITGSMVWDAGRSEFVFREGPvftnLLLA-------DEI 166
Cdd:pfam00493  59 NVLLVGDPGTAKSQLLKYVEKIA----PRAVYTSgkGSSAAGLTAAVVRDPVTGEFVLEAGA----LVLAdggvcciDEF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 167 NRTPPKTQSALLESMEEHTVSID--GATRALPDPFMVIATQNPVE--YEGTYP------LPEAQLDRF-LVKLELPLPSR 235
Cdd:pfam00493 131 DKMNDEDRVALHEAMEQQTISIAkaGIVATLNARCSILAAANPIFgrYDPKKSiaeninLPPPLLSRFdLIFVLLDKPDE 210

                         170
                  ....*....|
gi 1181024740 236 EAEIDIvARH 245
Cdd:pfam00493 211 EKDERL-AKH 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 94-233 1.66e-03

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: 38.51  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740   94 GGHALLEGVPGVAKTLLVRTLARAL----------DVEMARIQFTPDLMPADITGSMVWDAGRS------EFVFREGPVf 157
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppgggviyiDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlalALARKLKPD- 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1181024740  158 tnLLLADEINRTPPKTQSALLESMEEHTVsidGATRALPDPFMVIATQNPVeyegTYPLPEAQLDRFLVKLELPLP 233
Cdd:smart00382  81 --VLILDEITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDE----KDLGPALLRRRFDRRIVLLLI 147
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 98-187 2.72e-03

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family 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: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 38.15  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  98 LLEGVPGVAKTLLVRTLARALDVEMARIQFTpdlmpaDITGSMvwdAGRSEFVFREgpVFTN-------LLLADEINRTP 170
Cdd:cd19518    38 LLHGPPGCGKTMLANAIAGELKVPFLKISAT------EIVSGV---SGESEEKIRE--LFDQaisnapcIVFIDEIDAIT 106

                          90
                  ....*....|....*..
gi 1181024740 171 PKTQSALLEsMEEHTVS 187
Cdd:cd19518   107 PKRESAQRE-MERRIVS 122
MCM_arch cd17761
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ...
 96-261 2.74e-03

archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork


Pssm-ID: 350667 [Multi-domain]  Cd Length: 308  Bit Score: 39.36  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  96 HALLEGVPGVAKTLLVRTLARAldveMARIQFTP--DLMPADITGSMVWDAGRSEFVFREGPvftnLLLAD-------EI 166
Cdd:cd17761    44 HILLVGDPGTAKSQLLKYVSKV----APRAVYTTgkGSTAAGLTAAVVRDEGTGEWYLEAGA----LVLADkgiavvdEI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 167 NRTPPKTQSALLESMEEHTVSIDGA-------TRAlpdpfMVIATQNP-----VEYEG---TYPLPEAQLDRF---LVKL 228
Cdd:cd17761   116 DKMRKEDRSALHEAMEQQTISIAKAgivatlnARA-----AVLAAANPkfgrfDSYRPvaeQIDLPPTLLSRFdliFVLK 190

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1181024740 229 ELPLPSREAEI--DIVARHQAGfnPMSLAEAGIRP 261
Cdd:cd17761   191 DTPNEEKDRRLanHILDTHSGG--EMREIKPEIDP 223
MCM7 cd17758
DNA replication licensing factor Mcm7; Mcm7 is a helicase that play an important role in ...
 69-236 3.38e-03

DNA replication licensing factor Mcm7; Mcm7 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases.


Pssm-ID: 350664 [Multi-domain]  Cd Length: 306  Bit Score: 38.93  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  69 LKAEIGKAVVGQDGATTGLIVALVAGG-------------HALLEGVPGVAKTLLVRTLARAldveMARIQFTPDL--MP 133
Cdd:cd17758     2 LAASIAPEIYGHEDVKKALLLLLVGGVdkrgdgmkirgdiNICLMGDPGVAKSQLLKYICRI----APRSVYTTGRgsSG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740 134 ADITGSMVWDAGRSEFVFREGPvftnLLLAD-------EINRTPPKTQSALLESMEEHTVSID--GATRALPDPFMVIAT 204
Cdd:cd17758    78 VGLTAAVMKDPVTGEMTLEGGA----LVLADqgiccidEFDKMDESDRTAIHEVMEQQTISIAkaGITTTLNARTSILAA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1181024740 205 QNP--------VEYEGTYPLPEAQLDRF-LVKLELPLPSRE 236
Cdd:cd17758   154 ANPaygrynprRSPEQNINLPAALLSRFdLLFLILDKPDRD 194
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 98-206 5.09e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family 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: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 37.27  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181024740  98 LLEGVPGVAKTLLVRTLARALDVEMARIQftpdlmPADITGSMVwdaGRSEFVFREgpVFTN-------LLLADEINRTP 170
Cdd:cd19503    38 LLHGPPGTGKTLLARAVANEAGANFLSIS------GPSIVSKYL---GESEKNLRE--IFEEarshapsIIFIDEIDALA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1181024740 171 PKTQSALLEsMEEHTVS-----IDGATRAlpDPFMVIATQN 206
Cdd:cd19503   107 PKREEDQRE-VERRVVAqlltlMDGMSSR--GKVVVIAATN 144
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 68-123 8.00e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family 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: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 37.58  E-value: 8.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1181024740  68 ALKAEIGKAVVGQDGATTGLIVA-------LVAGGHA------------LLEGVPGVAKTLLVRTLARALDVEMA 123
Cdd:cd19497     5 EIKEHLDKYVIGQERAKKVLSVAvynhykrIRNNLKQkdddveleksniLLIGPTGSGKTLLAQTLAKILDVPFA 79
 
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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