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Conserved domains on  [gi|489501909|ref|WP_003406805|]
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MULTISPECIES: MoxR family ATPase [Pseudomonas]

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 ...
 11-280 1.30e-127

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: 365.26  E-value: 1.30e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  11 AINEVVLGKEAQVRLAMTCLVGGGHLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILGTSVFDRDSGQFTF 90
Cdd:COG0714    9 EIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGEFEF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  91 HPGPIFAELVLADEINRATPKSQSALLEAMEEGQVSIEGATRLLPDPFFVIATQNPFSSGGTFALPESQLDRFMMRISMG 170
Cdd:COG0714   89 RPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLKLYIG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909 171 YPARAAEKALLLGESRRElLPRLQPILDHALLGQLQAQARQVRASDALVDYVLRLVEATRSQPQFAYGLSPRASLAILAA 250
Cdd:COG0714  169 YPDAEEEREILRRHTGRH-LAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSPRASIALLRA 247

                        250       260       270
                 ....*....|....*....|....*....|
gi 489501909 251 ARAWAMLLGREYVIPEDVQAVLPSVIGHRL 280
Cdd:COG0714  248 ARALALLDGRDYVTPDDVKAVAGPVLKHRL 277
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 11-280 1.30e-127

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: 365.26  E-value: 1.30e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  11 AINEVVLGKEAQVRLAMTCLVGGGHLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILGTSVFDRDSGQFTF 90
Cdd:COG0714    9 EIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGEFEF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  91 HPGPIFAELVLADEINRATPKSQSALLEAMEEGQVSIEGATRLLPDPFFVIATQNPFSSGGTFALPESQLDRFMMRISMG 170
Cdd:COG0714   89 RPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLKLYIG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909 171 YPARAAEKALLLGESRRElLPRLQPILDHALLGQLQAQARQVRASDALVDYVLRLVEATRSQPQFAYGLSPRASLAILAA 250
Cdd:COG0714  169 YPDAEEEREILRRHTGRH-LAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSPRASIALLRA 247

                        250       260       270
                 ....*....|....*....|....*....|
gi 489501909 251 ARAWAMLLGREYVIPEDVQAVLPSVIGHRL 280
Cdd:COG0714  248 ARALALLDGRDYVTPDDVKAVAGPVLKHRL 277
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 35-165 1.04e-83

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: 247.86  E-value: 1.04e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   35 HLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILGTSVFDRDSGQFTFHPGPIFAELVLADEINRATPKSQS 114
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489501909  115 ALLEAMEEGQVSIEGATRLLPDPFFVIATQNPFSSGGTFALPESQLDRFMM 165
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 19-171 1.66e-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: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  19 KEAQVRLAMTCLVGGGHLLIEDLPGMGKTTLSHALAKILGLSYQRI------QFTSDLLPGDILGTSVFDRDSGQFTFHP 92
Cdd:cd00009    5 EAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylnasDLLEGLVVAELFGHFLVRLLFELAEKAK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489501909  93 GPIfaelVLADEINRATPKSQSALLEAMEEGQVSIEGATRLlpdpFFVIATQNPFSsggtFALPESQLDRFMMRISMGY 171
Cdd:cd00009   85 PGV----LFIDEIDSLSRGAQNALLRVLETLNDLRIDRENV----RVIGATNRPLL----GDLDRALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 33-148 1.26e-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: 41.59  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909    33 GGHLLIEDLPGMGKTTLSHALAKILGLSYQRIQF--TSDLLPGDILGTSVFDRDSGQFTFHPGPIFAE-----------L 99
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLalalarklkpdV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 489501909   100 VLADEINRATPKSQSALLEAMEEGQVSIEgatRLLPDPFFVIATQNPFS 148
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLL---LKSEKNLTVILTTNDEK 127
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 34-127 1.97e-04

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: 42.29  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   34 GHLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILG--TSVFDRDsgqftfhpgpifaeLVLADEINRATPK 111
Cdd:TIGR00635  31 DHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPGDLAAilTNLEEGD--------------VLFIDEIHRLSPA 96

                          90
                  ....*....|....*.
gi 489501909  112 SQSALLEAMEEGQVSI 127
Cdd:TIGR00635  97 VEELLYPAMEDFRLDI 112
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
35-143 2.91e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.04  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  35 HLLIEDLPGMGKTTLSHALAKILGLSyqrIQFTS-DLL--PGDILG--TSVFDRDsgqftfhpgpifaelVL-ADEINRA 108
Cdd:PRK00080  53 HVLLYGPPGLGKTTLANIIANEMGVN---IRITSgPALekPGDLAAilTNLEEGD---------------VLfIDEIHRL 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489501909 109 TPKSQSALLEAMEEGQVSI---EG----ATRL-LPdPFFVI-AT 143
Cdd:PRK00080 115 SPVVEEILYPAMEDFRLDImigKGpaarSIRLdLP-PFTLIgAT 157
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 11-280 1.30e-127

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: 365.26  E-value: 1.30e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  11 AINEVVLGKEAQVRLAMTCLVGGGHLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILGTSVFDRDSGQFTF 90
Cdd:COG0714    9 EIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGEFEF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  91 HPGPIFAELVLADEINRATPKSQSALLEAMEEGQVSIEGATRLLPDPFFVIATQNPFSSGGTFALPESQLDRFMMRISMG 170
Cdd:COG0714   89 RPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLKLYIG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909 171 YPARAAEKALLLGESRRElLPRLQPILDHALLGQLQAQARQVRASDALVDYVLRLVEATRSQPQFAYGLSPRASLAILAA 250
Cdd:COG0714  169 YPDAEEEREILRRHTGRH-LAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSPRASIALLRA 247

                        250       260       270
                 ....*....|....*....|....*....|
gi 489501909 251 ARAWAMLLGREYVIPEDVQAVLPSVIGHRL 280
Cdd:COG0714  248 ARALALLDGRDYVTPDDVKAVAGPVLKHRL 277
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 35-165 1.04e-83

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: 247.86  E-value: 1.04e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   35 HLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILGTSVFDRDSGQFTFHPGPIFAELVLADEINRATPKSQS 114
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489501909  115 ALLEAMEEGQVSIEGATRLLPDPFFVIATQNPFSSGGTFALPESQLDRFMM 165
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 35-163 1.50e-10

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: 58.07  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   35 HLLIEDLPGMGKTTLS-HALAKILGLSYQRIQFTSDLLPGDILGTsvFDRDSGQFTFHPGPIF-----AELVLADEINRA 108
Cdd:pfam07728   1 GVLLVGPPGTGKTELAeRLAAALSNRPVFYVQLTRDTTEEDLFGR--RNIDPGGASWVDGPLVraareGEIAVLDEINRA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489501909  109 TPKSQSALLEAMEEGQVSIEGATRLL---PDPFFVIATQNPFSSGGTFALPESQlDRF 163
Cdd:pfam07728  79 NPDVLNSLLSLLDERRLLLPDGGELVkaaPDGFRLIATMNPLDRGLNELSPALR-SRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 19-171 1.66e-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: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  19 KEAQVRLAMTCLVGGGHLLIEDLPGMGKTTLSHALAKILGLSYQRI------QFTSDLLPGDILGTSVFDRDSGQFTFHP 92
Cdd:cd00009    5 EAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylnasDLLEGLVVAELFGHFLVRLLFELAEKAK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489501909  93 GPIfaelVLADEINRATPKSQSALLEAMEEGQVSIEGATRLlpdpFFVIATQNPFSsggtFALPESQLDRFMMRISMGY 171
Cdd:cd00009   85 PGV----LFIDEIDSLSRGAQNALLRVLETLNDLRIDRENV----RVIGATNRPLL----GDLDRALYDRLDIRIVIPL 151
MCM pfam00493
MCM P-loop domain;
16-163 1.45e-07

MCM P-loop domain;


Pssm-ID: 459830 [Multi-domain]  Cd Length: 224  Bit Score: 51.38  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   16 VLGKEAqVRLAMTC-LVGGGH---------------LLIEDlPGMGKTTLSHALAKILglsyQRIQFTSdllpgdILGTS 79
Cdd:pfam00493  26 IYGHED-VKKAILLqLFGGVKkilpdgtrlrgdinvLLVGD-PGTAKSQLLKYVEKIA----PRAVYTS------GKGSS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   80 --------VFDRDSGQFTFHPGPifaeLVLA-------DEINRATPKSQSALLEAMEEGQVSIE--GATRLLPDPFFVIA 142
Cdd:pfam00493  94 aagltaavVRDPVTGEFVLEAGA----LVLAdggvcciDEFDKMNDEDRVALHEAMEQQTISIAkaGIVATLNARCSILA 169

                         170       180
                  ....*....|....*....|....*....
gi 489501909  143 TQNP----FSSGGTFA----LPESQLDRF 163
Cdd:pfam00493 170 AANPifgrYDPKKSIAeninLPPPLLSRF 198
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 10-163 8.10e-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: 49.65  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  10 SAINEVVLGKEAqVRLAMTC-LVGGGH---------------LLIEDlPGMGKTTLSHALAKILGLS-YQRIQFTSdlLP 72
Cdd:cd17706    4 DSIAPSIYGHED-VKKAVLLqLFGGVQkiledgtrirgdihiLLVGD-PGTAKSQILKYVLKIAPRGvYTSGKGSS--GA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  73 GdILGTSVFDRDSGQFTFHPGPifaeLVLA-------DEINRATPKSQSALLEAMEEGQVSIE--GATRLLPDPFFVIAT 143
Cdd:cd17706   80 G-LTAAVVRDSETGEWYLEAGA----LVLAdggvcciDEFDKMKELDRTALHEAMEQQTISIAkaGIVTTLNARCSILAA 154

                        170       180
                 ....*....|....*....|....*...
gi 489501909 144 QNP----FSSGGT----FALPESQLDRF 163
Cdd:cd17706  155 ANPkggrYNPKLSpienINLPSPLLSRF 182
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 257-296 5.89e-06

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: 43.36  E-value: 5.89e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 489501909  257 LLGREYVIPEDVQAVLPSVIGHRLRERSDPTGHGGGALVQ 296
Cdd:pfam17863  32 LEGRDYVTPEDVKEAAPLVLAHRLRREPEAEGETAEEILE 71
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 33-148 1.26e-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: 41.59  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909    33 GGHLLIEDLPGMGKTTLSHALAKILGLSYQRIQF--TSDLLPGDILGTSVFDRDSGQFTFHPGPIFAE-----------L 99
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLalalarklkpdV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 489501909   100 VLADEINRATPKSQSALLEAMEEGQVSIEgatRLLPDPFFVIATQNPFS 148
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLL---LKSEKNLTVILTTNDEK 127
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 34-127 1.97e-04

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: 42.29  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   34 GHLLIEDLPGMGKTTLSHALAKILGLSYQRIQFTSDLLPGDILG--TSVFDRDsgqftfhpgpifaeLVLADEINRATPK 111
Cdd:TIGR00635  31 DHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPGDLAAilTNLEEGD--------------VLFIDEIHRLSPA 96

                          90
                  ....*....|....*.
gi 489501909  112 SQSALLEAMEEGQVSI 127
Cdd:TIGR00635  97 VEELLYPAMEDFRLDI 112
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
35-143 2.91e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.04  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  35 HLLIEDLPGMGKTTLSHALAKILGLSyqrIQFTS-DLL--PGDILG--TSVFDRDsgqftfhpgpifaelVL-ADEINRA 108
Cdd:PRK00080  53 HVLLYGPPGLGKTTLANIIANEMGVN---IRITSgPALekPGDLAAilTNLEEGD---------------VLfIDEIHRL 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489501909 109 TPKSQSALLEAMEEGQVSI---EG----ATRL-LPdPFFVI-AT 143
Cdd:PRK00080 115 SPVVEEILYPAMEDFRLDImigKGpaarSIRLdLP-PFTLIgAT 157
bpMoxR pfam20030
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ...
 3-207 3.00e-04

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: 41.07  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909    3 RKLDACLSAINEVVLGKEAQVRLAMTCLVGGGHLLIEDLPGMGKTTLSHALAKILG---LSYQRIQFTSdllPGDILGTs 79
Cdd:pfam20030   1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLGgryFEYLLTRFTE---PNELFGP- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   80 vFD----RDSGQFTFHPGPI-FAELVLADEINRATPKSQSALLEAMEEGQVSIEGATRLLPDPFFVIATQnpfssggtfA 154
Cdd:pfam20030  77 -FDirklREGELVTNTEGMLpEASLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASN---------H 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489501909  155 LPESQ-----LDRFMMRISMGYPARAAEKALLLGESRRELLPRL-QPILDHALLGQLQA 207
Cdd:pfam20030 147 LPEDEalaalFDRFLLRVKCDNVPPDQLEAVLAAGWKLERRPVTtRPSIAAAEIRELQQ 205
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 42-167 7.66e-04

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: 38.73  E-value: 7.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   42 PGMGKTTLSHALAKILGLSYQRIQfTSDLLPGDILGTSVFDRDSGQFTFHPGPIfaeLVLADEINRATPKSQSALLEAME 121
Cdd:pfam00004   7 PGTGKTTLAKAVAKELGAPFIEIS-GSELVSKYVGESEKRLRELFEAAKKLAPC---VIFIDEIDALAGSRGSGGDSESR 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489501909  122 EGQ----VSIEGATRLLPDPFFVIATQNPFSsggtfaLPESQLDRFMMRI 167
Cdd:pfam00004  83 RVVnqllTELDGFTSSNSKVIVIAATNRPDK------LDPALLGRFDRII 126
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 35-127 8.78e-04

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: 39.02  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909   35 HLLIEDLPGMGKTTLSHALAKILGLSyqrIQFTSDLL---PGDILG--TSVFDRDsgqftfhpgpifaelVL-ADEINRA 108
Cdd:pfam05496  35 HVLLYGPPGLGKTTLANIIANEMGVN---IRITSGPAierPGDLAAilTNLEPGD---------------VLfIDEIHRL 96

                          90
                  ....*....|....*....
gi 489501909  109 TPKSQSALLEAMEEGQVSI 127
Cdd:pfam05496  97 NRAVEEILYPAMEDFRLDI 115
MCM_arch cd17761
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ...
 35-211 1.15e-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: 40.13  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  35 HLLIEDLPGMGKTTLSHALAKILglsyQRIQFTS--DLLPGDILGTSVFDRDSGQFTFHPGPifaeLVLAD-------EI 105
Cdd:cd17761   44 HILLVGDPGTAKSQLLKYVSKVA----PRAVYTTgkGSTAAGLTAAVVRDEGTGEWYLEAGA----LVLADkgiavvdEI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909 106 NRATPKSQSALLEAMEEGQVSIE--GATRLLPDPFFVIATQNP----FSSGGTFA----LPESQLDRF-MMRISMGYPAR 174
Cdd:cd17761  116 DKMRKEDRSALHEAMEQQTISIAkaGIVATLNARAAVLAAANPkfgrFDSYRPVAeqidLPPTLLSRFdLIFVLKDTPNE 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489501909 175 AAEKAL---LLGESRRELLPRLQPILDHALLGQLQAQARQ 211
Cdd:cd17761  196 EKDRRLanhILDTHSGGEMREIKPEIDPDLLRKYIAYARK 235
MCM8 cd17759
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a ...
 35-225 2.20e-03

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: 39.05  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  35 HLLIEDLPGMGKTTLSHALAKILGLS-YQRIQFTSDllPGDILGTSvFDRDSGQFTFHPGPifaeLVLA-------DEIN 106
Cdd:cd17759   45 HVLIVGDPGLGKSQMLQAACNIAPRGvYVCGNTTTT--SGLTVTLT-KDGRSGDFALEAGA----LVLGdqgicgiDEFD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909 107 RATPKSQsALLEAMEEGQVSIE--GATRLLPDPFFVIATQNP----FSSGGTFA----LPESQLDRF-MMRISMGYPARA 175
Cdd:cd17759  118 KMGSQHQ-ALLEAMEQQSVSLAkaGVVCSLPARTSVIAAANPvgghYNKGKTVSenlkMGPALLSRFdLVFILLDTPSEE 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489501909 176 AEKAL---------LLGESRRELLPRLQPildhallgqlqaqarqvRASDALVDYVLRL 225
Cdd:cd17759  197 HDHLLsehhqllrkYISYARQYVNPVLSK-----------------DASEALQEFYLEL 238
Mcm2 COG1241
DNA replicative helicase MCM subunit Mcm2, Cdc46/Mcm family [Replication, recombination and ...
 36-127 4.36e-03

DNA replicative helicase MCM subunit Mcm2, Cdc46/Mcm family [Replication, recombination and repair];


Pssm-ID: 440854 [Multi-domain]  Cd Length: 682  Bit Score: 38.63  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489501909  36 LLIEDlPGMGKTtlshalakilglsyQRIQFTSDLLPGdilgtSVF------------------DRDSGQFTFHPGpifA 97
Cdd:COG1241  319 LLVGD-PGTAKS--------------QLLRYAARLAPR-----GVYtsgkgstaagltaaavrdDFGTGRWTLEAG---A 375

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489501909  98 eLVLA-------DEINRATPKSQSALLEAMEEGQVSI 127
Cdd:COG1241  376 -LVLAdgglaciDELDKMREEDRSALHEAMEQQTISI 411
 
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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