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Conserved domains on  [gi|624383990|gb|KBT42879|]
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methanol dehydrogenase transcriptional regulator MoxR2 [Mycobacterium tuberculosis 2233BH]

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

Graphical summary

 Zoom to residue level

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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 ...
 54-344 1.92e-153

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: 433.05  E-value: 1.92e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  54 ALRAEVAKAVVGQDGVISGLVIALLCRGHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLVYDARTA 133
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 134 EFVFRPGPVFTNLLLADEINRTPPKTQAALLEAMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLLK 213
Cdd:COG0714   85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 214 LNVTLPARDSEIAILDRHahgfDPRDLSAINPVAGPAELAAGREAVRHVLVANEVLGYIVDIVGATRSSPALQLGVSPRG 293
Cdd:COG0714  165 LYIGYPDAEEEREILRRH----TGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSPRA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 624383990 294 ATALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHRVMLRPEAELEGATPD 344
Cdd:COG0714  241 SIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTAD 291
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 54-344 1.92e-153

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: 433.05  E-value: 1.92e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  54 ALRAEVAKAVVGQDGVISGLVIALLCRGHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLVYDARTA 133
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 134 EFVFRPGPVFTNLLLADEINRTPPKTQAALLEAMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLLK 213
Cdd:COG0714   85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 214 LNVTLPARDSEIAILDRHahgfDPRDLSAINPVAGPAELAAGREAVRHVLVANEVLGYIVDIVGATRSSPALQLGVSPRG 293
Cdd:COG0714  165 LYIGYPDAEEEREILRRH----TGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSPRA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 624383990 294 ATALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHRVMLRPEAELEGATPD 344
Cdd:COG0714  241 SIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTAD 291
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 82-212 2.57e-85

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: 254.02  E-value: 2.57e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   82 HVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLVYDARTAEFVFRPGPVFTNLLLADEINRTPPKTQA 161
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 624383990  162 ALLEAMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLL 212
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 64-218 7.52e-09

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: 54.07  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  64 VGQDGVISgLVIALLCR---GHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQF--TPDLMPGDVTGSLV----YDARTAE 134
Cdd:cd00009    1 VGQEEAIE-ALREALELpppKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYlnASDLLEGLVVAELFghflVRLLFEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 135 FVFRPGPVftnlLLADEINRTPPKTQAALLEAMEErqvsVEGEPKPLPNPFIVAATQNPIEyegtYQLPEAQLDRFLLKL 214
Cdd:cd00009   80 AEKAKPGV----LFIDEIDSLSRGAQNALLRVLET----LNDLRIDRENVRVIGATNRPLL----GDLDRALYDRLDIRI 147


                 ....
gi 624383990 215 NVTL 218
Cdd:cd00009  148 VIPL 151
bchD PRK13406
magnesium chelatase subunit D; Provisional
 154-344 3.01e-04

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 42.70  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 154 RTPPKTQAALLEAMEERQVSVE--GEPKPLPNPFIVAATQNPIEYEGTyqLPEAQLDRFLLKLNvtlpardseiaiLDRH 231
Cdd:PRK13406 104 RLEPGTAARLAAALDTGEVRLErdGLALRLPARFGLVALDEGAEEDER--APAALADRLAFHLD------------LDGL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 232 AHGfdprdlSAINPVAGPAELAAGREAVRHVLVANEVLGYIVDIvgatrsspALQLGV-SPRGATALLGTARSWAWLSGR 310
Cdd:PRK13406 170 ALR------DAREIPIDADDIAAARARLPAVGPPPEAIAALCAA--------AAALGIaSLRAPLLALRAARAAAALAGR 235

                        170       180       190
                 ....*....|....*....|....*....|....
gi 624383990 311 DYVTPDDVKAMARPTLRHRVMLRPEAELEGATPD 344
Cdd:PRK13406 236 TAVEEEDLALAARLVLAPRATRLPAPPQPPEEEP 269
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 80-195 2.78e-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: 37.74  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990    80 RGHVLLEGVPGVAKTLIVRAMSAALQLEFKRV---------------QFTPDLMPGDVTGSLVYDARTA-EFVFRPGPVf 143
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqLLLIIVGGKKASGSGELRLRLAlALARKLKPD- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 624383990   144 tnLLLADEINRTPPKTQAALLEAMEERQvsVEGEPKPLPNPFIVAATQNPIE 195
Cdd:smart00382  81 --VLILDEITSLLDAEQEALLLLLEELR--LLLLLKSEKNLTVILTTNDEKD 128
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 64-174 6.45e-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: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   64 VGQDGVISGLVIALLCR-------GHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLvydarTAefv 136
Cdd:TIGR00635   7 IGQEKVKEQLQLFIEAAkmrqealDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPGDLAAIL-----TN--- 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 624383990  137 FRPGPVftnlLLADEINRTPPKTQAALLEAMEERQVSV 174
Cdd:TIGR00635  79 LEEGDV----LFIDEIHRLSPAVEELLYPAMEDFRLDI 112
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 54-344 1.92e-153

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: 433.05  E-value: 1.92e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  54 ALRAEVAKAVVGQDGVISGLVIALLCRGHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLVYDARTA 133
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 134 EFVFRPGPVFTNLLLADEINRTPPKTQAALLEAMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLLK 213
Cdd:COG0714   85 EFEFRPGPLFANVLLADEINRAPPKTQSALLEAMEERQVTIPGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLLK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 214 LNVTLPARDSEIAILDRHahgfDPRDLSAINPVAGPAELAAGREAVRHVLVANEVLGYIVDIVGATRSSPALQLGVSPRG 293
Cdd:COG0714  165 LYIGYPDAEEEREILRRH----TGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVRATREHPDLRKGPSPRA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 624383990 294 ATALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHRVMLRPEAELEGATPD 344
Cdd:COG0714  241 SIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHRLILSPEADAEGVTAD 291
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 82-212 2.57e-85

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: 254.02  E-value: 2.57e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   82 HVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLVYDARTAEFVFRPGPVFTNLLLADEINRTPPKTQA 161
Cdd:pfam07726   1 HVLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQKTREFEFRPGPVFANVLLADEINRAPPKTQS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 624383990  162 ALLEAMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLL 212
Cdd:pfam07726  81 ALLEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYPLPEAQLDRFLM 131
AAA_lid_2 pfam17863
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 278-350 3.27e-19

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: 80.72  E-value: 3.27e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624383990  278 ATRSSPALQLGVSPRGAT-ALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHRvmLRPEAELEGATPDGVLDGI 350
Cdd:pfam17863   2 ATRAHLAIALGVSPRRADlALLRAARALAALEGRDYVTPEDVKEAAPLVLAHR--LRREPEAEGETAEEILEEI 73
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 82-210 2.20e-18

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: 80.41  E-value: 2.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   82 HVLLEGVPGVAKTLIVRAMSAAL-QLEFKRVQFTPDLMPGDVTGSLVYDARTAEFVfrPGPVFTN-----LLLADEINRT 155
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWV--DGPLVRAaregeIAVLDEINRA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 624383990  156 PPKTQAALLEAMEERQVSVE---GEPKPLPNPFIVAATQNPIEYEGTYQLPeAQLDRF 210
Cdd:pfam07728  79 NPDVLNSLLSLLDERRLLLPdggELVKAAPDGFRLIATMNPLDRGLNELSP-ALRSRF 135
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
62-344 1.64e-13

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


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 70.55  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  62 AVVGQDGvisgLVIALLCR------GHVLLEGVPGVAKTLIVRAMSA--------------------------------- 102
Cdd:COG1239   10 AIVGQEE----MKLALLLNavdpgiGGVLIRGEKGTAKSTAVRALAAllppievvkgcpyncdpddpdelcpdcrerlaa 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 103 --ALQLEFKRVQF-------TPDlmpgDVTGSLvyDARTA----EFVFRPGpvftnlLLA---------DEINrtppktq 160
Cdd:COG1239   86 geELPTETRPVPVvelplgaTED----RVVGSL--DLEKAlkegEKAFEPG------LLArahrgilyvDEVN------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 161 aaLLE-----------AMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLpeaqLDRFLLKLNVTLPaRDSE--IAI 227
Cdd:COG1239  147 --LLDdhlvdvlldaaAMGRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQL----LDRFGLSVEVEGP-RDPEerVEI 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 228 LDRhahgfdpRDLSAINPVAGPAE-----------LAAGREAVRHVLVANEVLGYIVDIvgatrsspALQLGV-SPRGAT 295
Cdd:COG1239  220 VRR-------RLAFEADPEAFAAEyaeeqaelrerIAAARELLPEVTIPDELLRYIAEL--------CIALGVdGHRADI 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 624383990 296 ALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHRVMLRP--EAELEGATPD 344
Cdd:COG1239  285 VIARAARALAALEGRTEVTAEDIRRAAELALPHRLRRDPfeEPGLDEEPPP 335
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 64-218 7.52e-09

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: 54.07  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  64 VGQDGVISgLVIALLCR---GHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQF--TPDLMPGDVTGSLV----YDARTAE 134
Cdd:cd00009    1 VGQEEAIE-ALREALELpppKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYlnASDLLEGLVVAELFghflVRLLFEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 135 FVFRPGPVftnlLLADEINRTPPKTQAALLEAMEErqvsVEGEPKPLPNPFIVAATQNPIEyegtYQLPEAQLDRFLLKL 214
Cdd:cd00009   80 AEKAKPGV----LFIDEIDSLSRGAQNALLRVLET----LNDLRIDRENVRVIGATNRPLL----GDLDRALYDRLDIRI 147


                 ....
gi 624383990 215 NVTL 218
Cdd:cd00009  148 VIPL 151
bpMoxR pfam20030
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ...
 50-216 8.92e-07

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: 49.16  E-value: 8.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   50 DALLALRAEVAKAVVGQDGVISGLVIALLCRGHVLLEGVPGVAKTLIVRAMSAALQ---LEFKRVQFTPdlmPGDVTGSL 126
Cdd:pfam20030   1 RRLREVLRPLKTGFVGKDEIIDLLGLALVARENLFLLGPPGTAKSALVRRLAARLGgryFEYLLTRFTE---PNELFGPF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  127 vyDARTaefvFRPGPVFTN---------LLLADEINRTPPKTQAALLEAMEERQVSVEGEPKPLPNPFIVAATQnpieye 197
Cdd:pfam20030  78 --DIRK----LREGELVTNtegmlpeasLVFLDELFNANSAILNSLLMVLNERIFRRGKETRKLPALMFVGASN------ 145

                         170       180
                  ....*....|....*....|....
gi 624383990  198 gtyQLPE-----AQLDRFLLKLNV 216
Cdd:pfam20030 146 ---HLPEdealaALFDRFLLRVKC 166
MCM_arch cd17761
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ...
 80-327 1.40e-06

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: 49.37  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  80 RG--HVLLEGVPGVAKTLIVRAMSAALqlefKRVQFTP--DLMPGDVTGSLVYDARTAEFVFRPGPvftnLLLAD----- 150
Cdd:cd17761   40 RGdiHILLVGDPGTAKSQLLKYVSKVA----PRAVYTTgkGSTAAGLTAAVVRDEGTGEWYLEAGA----LVLADkgiav 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 151 --EINRTPPKTQAALLEAMEERQVSVE--GEPKPLPNPFIVAATQNP-----IEYEGTYQ---LPEAQLDRFLL---KLN 215
Cdd:cd17761  112 vdEIDKMRKEDRSALHEAMEQQTISIAkaGIVATLNARAAVLAAANPkfgrfDSYRPVAEqidLPPTLLSRFDLifvLKD 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 216 VTLPARDSEIA--ILDRHAHGfdprDLSAINPVAGPAEL----AAGREAVRHVLvANEVLGYIVDIVGATRSS---PALQ 286
Cdd:cd17761  192 TPNEEKDRRLAnhILDTHSGG----EMREIKPEIDPDLLrkyiAYARKNVRPVL-TEEAKQLIKDFYVEMRKSgqeTPSP 266

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 624383990 287 LGVSPRGATALLGTARSWAWLSGRDYVTPDDVKAMARPTLR 327
Cdd:cd17761  267 VPITARQLEALVRLSEASARMRLSQEVTLEDAERAIRIMLN 307
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 58-323 2.95e-06

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: 48.49  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  58 EVAKAVVGQ--DGVISGLVIALLCRG--HVLLEGVPGVAKTLIVRAMSAAlqleFKRVQFT-------PDLmpgdvTGSL 126
Cdd:cd17706   15 DVKKAVLLQlfGGVQKILEDGTRIRGdiHILLVGDPGTAKSQILKYVLKI----APRGVYTsgkgssgAGL-----TAAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 127 VYDARTAEFVFRPGPvftnLLLA-------DEINRTPPKTQAALLEAMEERQVSVE--GEPKPLPNPFIVAATQNPIeyE 197
Cdd:cd17706   86 VRDSETGEWYLEAGA----LVLAdggvcciDEFDKMKELDRTALHEAMEQQTISIAkaGIVTTLNARCSILAAANPK--G 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 198 GTYQ----------LPEAQLDRF---LLKLNVTLPARDSEIA--ILDRHAHGFDPR-DLSAINPVAGPAELaagreAVRH 261
Cdd:cd17706  160 GRYNpklspieninLPSPLLSRFdliFVIRDDPDEERDEELAehIIDLHRGSDPEEqVKPEEDGIPIDIEL-----LRKY 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624383990 262 VLVA--------NEVLGYIVDIVGATR--SSPALQLGVSPRGATALLGTARSWAWLSGRDYVTPDDVKAMAR 323
Cdd:cd17706  235 ILYArqihpkisEEAREKLVRWYVELRkeSERRSTIPITARQLESVIRLAEAHAKMRLSEVVTEEDVEEAIR 306
MCM pfam00493
MCM P-loop domain;
80-231 7.73e-06

MCM P-loop domain;


Pssm-ID: 459830 [Multi-domain]  Cd Length: 224  Bit Score: 46.37  E-value: 7.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   80 RG--HVLLEGVPGVAKTLIVRAMSAALQlefkRVQFT-------PDLmpgdvTGSLVYDARTAEFVFRPGPvftnLLLA- 149
Cdd:pfam00493  55 RGdiNVLLVGDPGTAKSQLLKYVEKIAP----RAVYTsgkgssaAGL-----TAAVVRDPVTGEFVLEAGA----LVLAd 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  150 ------DEINRTPPKTQAALLEAMEERQVSVE--GEPKPLPNPFIVAATQNPIeyEGTY----------QLPEAQLDRF- 210
Cdd:pfam00493 122 ggvcciDEFDKMNDEDRVALHEAMEQQTISIAkaGIVATLNARCSILAAANPI--FGRYdpkksiaeniNLPPPLLSRFd 199

                         170       180
                  ....*....|....*....|....*
gi 624383990  211 --LLKLNVTLPARDSEIA--ILDRH 231
Cdd:pfam00493 200 liFVLLDKPDEEKDERLAkhIVDLH 224
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 83-218 2.44e-05

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: 43.35  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   83 VLLEGVPGVAKTLIVRAMSAALQLEFKRVQfTPDLMPG--DVTGSLVydARTAEFVFRPGPVftnLLLADEI-------- 152
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEIS-GSELVSKyvGESEKRL--RELFEAAKKLAPC---VIFIDEIdalagsrg 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624383990  153 ---NRTPPKTQAALLEAMeerqvsvEGEPKPLPNPFIVAATQNPieyegtYQLPEAQLDRFLLKLNVTL 218
Cdd:pfam00004  75 sggDSESRRVVNQLLTEL-------DGFTSSNSKVIVIAATNRP------DKLDPALLGRFDRIIEFPL 130
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 80-267 1.12e-04

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: 43.75  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  80 RGHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQftpdlmPGDVTGSLVYD--ARTAEfVFR------PGpvftnLLLADE 151
Cdd:COG0464  191 PRGLLLYGPPGTGKTLLARALAGELGLPLIEVD------LSDLVSKYVGEteKNLRE-VFDkarglaPC-----VLFIDE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 152 I-----NRTPPKTQ------AALLEAMEERQVSVegepkplpnpFIVAATQNPIeyegtyQLPEAQLDRFLLKLNVTLPA 220
Cdd:COG0464  259 AdalagKRGEVGDGvgrrvvNTLLTEMEELRSDV----------VVIAATNRPD------LLDPALLRRFDEIIFFPLPD 322

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 624383990 221 RDSEIAILDRH------AHGFDPRDLSAINPVAGPAEL-AAGREAVRHVLVANE 267
Cdd:COG0464  323 AEERLEIFRIHlrkrplDEDVDLEELAEATEGLSGADIrNVVRRAALQALRLGR 376
MCM7 cd17758
DNA replication licensing factor Mcm7; Mcm7 is a helicase that play an important role in ...
 63-318 2.74e-04

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: 42.40  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  63 VVGQDGVISGLVIallcRG--HVLLEGVPGVAKTLIVRAMSAALQlefkRVQFTPDLMPGDV--TGSLVYDARTAEFVFR 138
Cdd:cd17758   25 VGGVDKRGDGMKI----RGdiNICLMGDPGVAKSQLLKYICRIAP----RSVYTTGRGSSGVglTAAVMKDPVTGEMTLE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 139 PGPvftnLLLA-------DEINRTPPKTQAALLEAMEERQVSVE--GEPKPLPNPFIVAATQNPIeyEGTY--------- 200
Cdd:cd17758   97 GGA----LVLAdqgicciDEFDKMDESDRTAIHEVMEQQTISIAkaGITTTLNARTSILAAANPA--YGRYnprrspeqn 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 201 -QLPEAQLDRF-LLKLNVTLPARDSEIA----ILDRHAHGFDP-RDLSAINPVAGPAELAAGREavRHVLVANEVLGYIV 273
Cdd:cd17758  171 iNLPAALLSRFdLLFLILDKPDRDNDLRlaehVTYVHQHNKQPdSDFEPLDPKLLRAYIALAKR--KRPTVPPALADYIV 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 624383990 274 DIVGATRSSPALQLG---VSPRGATALLGTARSWAWLSGRDYVTPDDV 318
Cdd:cd17758  249 QAYVEMRQEAKRSKDftfTTPRTLLAILRLSQALARLRLSDSVEIDDV 296
bchD PRK13406
magnesium chelatase subunit D; Provisional
 154-344 3.01e-04

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 42.70  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 154 RTPPKTQAALLEAMEERQVSVE--GEPKPLPNPFIVAATQNPIEYEGTyqLPEAQLDRFLLKLNvtlpardseiaiLDRH 231
Cdd:PRK13406 104 RLEPGTAARLAAALDTGEVRLErdGLALRLPARFGLVALDEGAEEDER--APAALADRLAFHLD------------LDGL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 232 AHGfdprdlSAINPVAGPAELAAGREAVRHVLVANEVLGYIVDIvgatrsspALQLGV-SPRGATALLGTARSWAWLSGR 310
Cdd:PRK13406 170 ALR------DAREIPIDADDIAAARARLPAVGPPPEAIAALCAA--------AAALGIaSLRAPLLALRAARAAAALAGR 235

                        170       180       190
                 ....*....|....*....|....*....|....
gi 624383990 311 DYVTPDDVKAMARPTLRHRVMLRPEAELEGATPD 344
Cdd:PRK13406 236 TAVEEEDLALAARLVLAPRATRLPAPPQPPEEEP 269
Mcm2 COG1241
DNA replicative helicase MCM subunit Mcm2, Cdc46/Mcm family [Replication, recombination and ...
 80-234 9.83e-04

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


Pssm-ID: 440854 [Multi-domain]  Cd Length: 682  Bit Score: 40.94  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  80 RG--HVLLEGVPGVAKTlivramsaalQLefkrVQFTPDLMPGDV------------TGSLVYD-ARTAEFVFRPGPvft 144
Cdd:COG1241  313 RGdiHILLVGDPGTAKS----------QL----LRYAARLAPRGVytsgkgstaaglTAAAVRDdFGTGRWTLEAGA--- 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 145 nLLLA-------DEINRTPPKTQAALLEAMEERQVSVE--GepkplpnpfIVA---------ATQNP-----IEYEG-TY 200
Cdd:COG1241  376 -LVLAdgglaciDELDKMREEDRSALHEAMEQQTISIAkaG---------IVAtlnarcsvlAAANPkygrfDPYEPiAE 445

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 624383990 201 Q--LPEAQLDRFLLKLNVT---LPARDSEIA--ILDRHAHG 234
Cdd:COG1241  446 QidLPPTLLSRFDLIFVLRdkpDEERDRELArhILKVHRAG 486
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
147-247 1.34e-03

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 40.60  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990 147 LLADEINRTPPKTQAALLEAMEERQVSVEGEPKPLPNPF-IVAATQNPIE---YEGTYQlpeaqlDRFLLKLNV----TL 218
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIrIIAATNRDLQamvKEGTFR------EDLFYRLNVihliLP 314

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 624383990 219 PARD--SEIAILDRHAHGF----DPRDLSAINPVA 247
Cdd:PRK11361 315 PLRDrrEDISLLANHFLQKfsseNQRDIIDIDPMA 349
Sigma54_activat pfam00158
Sigma-54 interaction domain;
146-190 1.76e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 38.54  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 624383990  146 LLLaDEINRTPPKTQAALLEAMEERQVSVEGEPKPLP-NPFIVAAT 190
Cdd:pfam00158  97 LFL-DEIGELPLELQAKLLRVLQEGEFERVGGTKPIKvDVRIIAAT 141
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 11-358 2.14e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 40.24  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   11 PPTQTPGAELPGYPPQAGGAPTAAPSGPHPHRAEAESARDALLALRAEVAKAVVGQDGVISGLVIALLCRGHVLLEGVPG 90
Cdd:COG3321   854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   91 VAKTLIVRAMSAALQLEFKRVQftPDLMPGDVTGSLVYDARTAEFVFRPGPVFTNLLLADEINRTPPKTQAALLEAMEER 170
Cdd:COG3321   934 ALAAAAAALLALAAAAAAAAAA--LAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALL 1011

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  171 QVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLLKLNVTLPARDSEIAILDRHAHGFDPRDLSAINPVAGPA 250
Cdd:COG3321  1012 LAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALA 1091

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990  251 ELAAGREAVRHVLVAN-EVLGYIVDIVGATRSSPALQLGVSPRGATALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHR 329
Cdd:COG3321  1092 AAALALALAALAAALLlLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAA 1171

                         330       340
                  ....*....|....*....|....*....
gi 624383990  330 VMLRPEAELEGATPDGVLDGILASVPVPR 358
Cdd:COG3321  1172 ALLLALALALAAALAAALAGLAALLLAAL 1200
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 80-195 2.78e-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: 37.74  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990    80 RGHVLLEGVPGVAKTLIVRAMSAALQLEFKRV---------------QFTPDLMPGDVTGSLVYDARTA-EFVFRPGPVf 143
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqLLLIIVGGKKASGSGELRLRLAlALARKLKPD- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 624383990   144 tnLLLADEINRTPPKTQAALLEAMEERQvsVEGEPKPLPNPFIVAATQNPIE 195
Cdd:smart00382  81 --VLILDEITSLLDAEQEALLLLLEELR--LLLLLKSEKNLTVILTTNDEKD 128
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 64-190 5.63e-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: 37.09  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   64 VGQDGVISGLVIAL---LCRG----HVLLEGVPGVAKTLIVRAMSAALQLEFkRVQFTPDL-MPGDVTGSLVYdartaef 135
Cdd:pfam05496  10 IGQEKVKENLKIFIeaaKQRGealdHVLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIeRPGDLAAILTN------- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624383990  136 vFRPGPVftnlLLADEINRTPPKTQAALLEAMEERQVSV---EGE-----PKPLPnPF-IVAAT 190
Cdd:pfam05496  82 -LEPGDV----LFIDEIHRLNRAVEEILYPAMEDFRLDIvigKGPsarsiRLDLP-PFtLVGAT 139
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 64-174 6.45e-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: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624383990   64 VGQDGVISGLVIALLCR-------GHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLvydarTAefv 136
Cdd:TIGR00635   7 IGQEKVKEQLQLFIEAAkmrqealDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPGDLAAIL-----TN--- 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 624383990  137 FRPGPVftnlLLADEINRTPPKTQAALLEAMEERQVSV 174
Cdd:TIGR00635  79 LEEGDV----LFIDEIHRLSPAVEELLYPAMEDFRLDI 112
 
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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