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Conserved domains on  [gi|499218398|ref|WP_010915938|]
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plasmid partitioning protein RepB [Mesorhizobium japonicum]

Protein Classification

plasmid partitioning protein RepB( domain architecture ID 11496881)

plasmid partitioning protein RepB is involved in replicon partitioning

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
partition_RepB TIGR03454
plasmid partitioning protein RepB; Members of this family are the RepB protein involved in ...
2-325 1.25e-149

plasmid partitioning protein RepB; Members of this family are the RepB protein involved in replicon partitioning. RepB is found, in general, as part of a repABC operon in plasmids and small chromosomes, separate from the main chromosome, in various bacteria. This model describes a rather narrow clade of proteins; it should be noted that additional homologs scoring below the trusted cutoff have very similar functions, although they may be named differently. [Mobile and extrachromosomal element functions, Plasmid functions]


:

Pssm-ID: 274586 [Multi-domain]  Cd Length: 325  Bit Score: 423.66  E-value: 1.25e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398    2 SRRDVLNGIFADTTRELAAANFSKEAdgGRVLAGPVRTMGLALDRMDQ---EARELREALKSGERVVELDPELIDGSFVR 78
Cdd:TIGR03454   1 SRKNLLGSLFSPAAAPASAPALGRPR--QRVSSGAVGAMGRSLGELSQkakRAEELEEQLAEGETVVELDPALIDPSFVR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   79 DRLDGEVPATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSDNELVVAQGIENTAR 158
Cdd:TIGR03454  79 DRLDSDDEDFADLVESIREHGQQVPILVRPHPEAEGRYQIAYGHRRLRAARELGRPVKAVVRELSDEELVIAQGQENAAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  159 KDLSYIERAVFALSLETHGFGRDLIMQALSTEKTELSKLLSVAKGIPGSLVKAIGAAPSMGRRRWMDIAEKITDPKAMEV 238
Cdd:TIGR03454 159 RDLSFIERALFAARLEDRGFDRDTIMAALSVDKTELSRMISVARRIPEELIEAIGPAPGIGRPRWMELAELLEHPGNDAE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  239 ARNAIHRPEFEALGSDERFMMVLAEVSKKPPREQTIS-EWKPNGGKVAAKIKDTGRAYTLSLKTAEADEgFGAYLTKRLD 317
Cdd:TIGR03454 239 ALDEVASAAFKALESDQRFEALFAALSKKAKRSPAATkSWKAADGSVLAKIKRTAKALTLTLKKKEAPE-FADFILERLD 317

                  ....*...
gi 499218398  318 DLYADWQA 325
Cdd:TIGR03454 318 DLYEEFRR 325
 
Name Accession Description Interval E-value
partition_RepB TIGR03454
plasmid partitioning protein RepB; Members of this family are the RepB protein involved in ...
2-325 1.25e-149

plasmid partitioning protein RepB; Members of this family are the RepB protein involved in replicon partitioning. RepB is found, in general, as part of a repABC operon in plasmids and small chromosomes, separate from the main chromosome, in various bacteria. This model describes a rather narrow clade of proteins; it should be noted that additional homologs scoring below the trusted cutoff have very similar functions, although they may be named differently. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274586 [Multi-domain]  Cd Length: 325  Bit Score: 423.66  E-value: 1.25e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398    2 SRRDVLNGIFADTTRELAAANFSKEAdgGRVLAGPVRTMGLALDRMDQ---EARELREALKSGERVVELDPELIDGSFVR 78
Cdd:TIGR03454   1 SRKNLLGSLFSPAAAPASAPALGRPR--QRVSSGAVGAMGRSLGELSQkakRAEELEEQLAEGETVVELDPALIDPSFVR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   79 DRLDGEVPATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSDNELVVAQGIENTAR 158
Cdd:TIGR03454  79 DRLDSDDEDFADLVESIREHGQQVPILVRPHPEAEGRYQIAYGHRRLRAARELGRPVKAVVRELSDEELVIAQGQENAAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  159 KDLSYIERAVFALSLETHGFGRDLIMQALSTEKTELSKLLSVAKGIPGSLVKAIGAAPSMGRRRWMDIAEKITDPKAMEV 238
Cdd:TIGR03454 159 RDLSFIERALFAARLEDRGFDRDTIMAALSVDKTELSRMISVARRIPEELIEAIGPAPGIGRPRWMELAELLEHPGNDAE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  239 ARNAIHRPEFEALGSDERFMMVLAEVSKKPPREQTIS-EWKPNGGKVAAKIKDTGRAYTLSLKTAEADEgFGAYLTKRLD 317
Cdd:TIGR03454 239 ALDEVASAAFKALESDQRFEALFAALSKKAKRSPAATkSWKAADGSVLAKIKRTAKALTLTLKKKEAPE-FADFILERLD 317

                  ....*...
gi 499218398  318 DLYADWQA 325
Cdd:TIGR03454 318 DLYEEFRR 325
PRK13866 PRK13866
plasmid partitioning protein RepB; Provisional
1-324 6.11e-88

plasmid partitioning protein RepB; Provisional


Pssm-ID: 172387 [Multi-domain]  Cd Length: 336  Bit Score: 267.21  E-value: 6.11e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   1 MSRRDVLNGIFADTTRELAAANFSKEADggRVLAGPVRTMGLALDRMDQEARE---LREALKSGERVVELDPELIDGSFV 77
Cdd:PRK13866   1 MSRKDAIDSLFLKKQPATDRTSVDKSAV--RVRTGAISAMGSSLQEMAEGAKAaarLQDQLAAGEAVVSLDPSMIDGSPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  78 RDRLDGEV-PATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSDNELVVAQGIENT 156
Cdd:PRK13866  79 ADRLPADVdPKFEQLEASISQEGQQVPILVRPHPEAAGRYQIVYGRRRLRAAVNLRREVSAIVRNLTDRELVVAQGRENL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398 157 ARKDLSYIERAVFALSLETHGFGRDLIMQALSTEKTELSKLLSVAKGIPGSLVKAIGAAPSMGRRRWMDIAEKITDPKAM 236
Cdd:PRK13866 159 DRADLSFIEKALFALRLEDAGFDRATIIAALSTDKADLSRYITVARGIPLNLATQIGPASKAGRSRWVALAEGLGKPKAT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398 237 EVARNAIHRPEFEALGSDERFMMVLAEVSKKP-PREQTISEWKPNGGKVAAKI-KDTGR-AYTLSLKTAEAdegFGAYLT 313
Cdd:PRK13866 239 DAIEAVLESEQFKHSDSDARFDLIFNAVSKPPaKRPKKVRAWSTPKGKKAATIrQETGRtALVFDEKLVPT---FGEYVA 315
                        330
                 ....*....|.
gi 499218398 314 KRLDDLYADWQ 324
Cdd:PRK13866 316 DQLDSLYAQFI 326
RepB_like_N cd16405
plasmid segregation replication protein B like protein, N-terminal domain; RepB, found on ...
67-155 2.70e-42

plasmid segregation replication protein B like protein, N-terminal domain; RepB, found on plasmids and secondary chromosomes, works along with repA in directing plasmid segregation, and has been shown in Rhizobium etli to require the parS centromere-like sequence for full transcriptional repression of the repABC operon, inducing plasmid incompatibility. RepA is a Walker-type ATPase that complexes with RepB to form DNA-protein complexes in the presence of ATP/ADP. RepC is an initiator protein for the plasmid. repA and repB are homologous to the parA and ParB genes of the parABS partitioning system found on primary chromosomes.


Pssm-ID: 319262 [Multi-domain]  Cd Length: 91  Bit Score: 141.53  E-value: 2.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  67 LDPELIDGSFVRDRL--DGEVPATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSD 144
Cdd:cd16405    1 LDPDLIDPSFIADRLedDFDDDEFEELKESIRESGQQVPILVRPHPEEGGRYEIVYGHRRLRACRELGLPVRAIVRELSD 80
                         90
                 ....*....|.
gi 499218398 145 NELVVAQGIEN 155
Cdd:cd16405   81 EELVVAQGQEN 91
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
59-243 4.61e-39

Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441084 [Multi-domain]  Cd Length: 241  Bit Score: 138.20  E-value: 4.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  59 KSGERVVELDPELIDGSFVRDRLDGEVPATDDIVRSIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLG-RKVRA 137
Cdd:COG1475    2 KEGEEIREIPIDKIVPSPYNPRRTFDEEALEELAASIREHGLLQPILVRPLGD--GRYEIIAGERRLRAAKLLGlETVPA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398 138 VVRRLSDNELVVAQGIENTARKDLSYIERAVFALSL-ETHGFGRDLIMQALSTEKTELSKLLSVAKgIPGSLVKAIGAAp 216
Cdd:COG1475   80 IVRDLDDEEALELALIENLQREDLNPLEEARAYQRLlEEFGLTQEEIAERLGKSRSEVSNLLRLLK-LPPEVQEALREG- 157
                        170       180
                 ....*....|....*....|....*..
gi 499218398 217 SMGRRRWMDIAeKITDPKAMEVARNAI 243
Cdd:COG1475  158 KLSLGHARALA-ALSDPERQEELAEKI 183
ParB smart00470
ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ...
65-155 1.28e-17

ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB also nicks supercoiled plasmid DNA preferably at sites with potential single-stranded character, like AT-rich regions and sequences that can form cruciform structures. ParB also exhibits 5-->3 exonuclease activity.


Pssm-ID: 214678 [Multi-domain]  Cd Length: 89  Bit Score: 76.57  E-value: 1.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398    65 VELDPELIDGSFVRDRLDGEvPATDDIVRSIEENGQEVPILVRQHPdleGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLS 143
Cdd:smart00470   1 VEVPIEKLRPNPDQPRLTSE-ESLEELAESIKENGLLQPIIVRPND---GRYEIIDGERRLRAAKLLGlKEVPVIVRDLD 76
                           90
                   ....*....|..
gi 499218398   144 DNELVVAQGIEN 155
Cdd:smart00470  77 DEEAIALSLEEN 88
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
65-155 5.46e-16

ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localizes to both poles of the predivisional cell following completion of DNA replication. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4.


Pssm-ID: 426651 [Multi-domain]  Cd Length: 90  Bit Score: 72.31  E-value: 5.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   65 VELDPELIDGSFVRDRLDGEvPATDDIVRSIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLS 143
Cdd:pfam02195   1 EEVPISKLRPNPDQPRKDSE-ESLEELAASIKKRGLLQPIIVRKTPD--GRYEIIAGERRLRAAKLLGlKEVPVIVREID 77
                          90
                  ....*....|..
gi 499218398  144 DNELVVAQGIEN 155
Cdd:pfam02195  78 DEEAIALSLIEN 89
 
Name Accession Description Interval E-value
partition_RepB TIGR03454
plasmid partitioning protein RepB; Members of this family are the RepB protein involved in ...
2-325 1.25e-149

plasmid partitioning protein RepB; Members of this family are the RepB protein involved in replicon partitioning. RepB is found, in general, as part of a repABC operon in plasmids and small chromosomes, separate from the main chromosome, in various bacteria. This model describes a rather narrow clade of proteins; it should be noted that additional homologs scoring below the trusted cutoff have very similar functions, although they may be named differently. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274586 [Multi-domain]  Cd Length: 325  Bit Score: 423.66  E-value: 1.25e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398    2 SRRDVLNGIFADTTRELAAANFSKEAdgGRVLAGPVRTMGLALDRMDQ---EARELREALKSGERVVELDPELIDGSFVR 78
Cdd:TIGR03454   1 SRKNLLGSLFSPAAAPASAPALGRPR--QRVSSGAVGAMGRSLGELSQkakRAEELEEQLAEGETVVELDPALIDPSFVR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   79 DRLDGEVPATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSDNELVVAQGIENTAR 158
Cdd:TIGR03454  79 DRLDSDDEDFADLVESIREHGQQVPILVRPHPEAEGRYQIAYGHRRLRAARELGRPVKAVVRELSDEELVIAQGQENAAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  159 KDLSYIERAVFALSLETHGFGRDLIMQALSTEKTELSKLLSVAKGIPGSLVKAIGAAPSMGRRRWMDIAEKITDPKAMEV 238
Cdd:TIGR03454 159 RDLSFIERALFAARLEDRGFDRDTIMAALSVDKTELSRMISVARRIPEELIEAIGPAPGIGRPRWMELAELLEHPGNDAE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  239 ARNAIHRPEFEALGSDERFMMVLAEVSKKPPREQTIS-EWKPNGGKVAAKIKDTGRAYTLSLKTAEADEgFGAYLTKRLD 317
Cdd:TIGR03454 239 ALDEVASAAFKALESDQRFEALFAALSKKAKRSPAATkSWKAADGSVLAKIKRTAKALTLTLKKKEAPE-FADFILERLD 317

                  ....*...
gi 499218398  318 DLYADWQA 325
Cdd:TIGR03454 318 DLYEEFRR 325
PRK13866 PRK13866
plasmid partitioning protein RepB; Provisional
1-324 6.11e-88

plasmid partitioning protein RepB; Provisional


Pssm-ID: 172387 [Multi-domain]  Cd Length: 336  Bit Score: 267.21  E-value: 6.11e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   1 MSRRDVLNGIFADTTRELAAANFSKEADggRVLAGPVRTMGLALDRMDQEARE---LREALKSGERVVELDPELIDGSFV 77
Cdd:PRK13866   1 MSRKDAIDSLFLKKQPATDRTSVDKSAV--RVRTGAISAMGSSLQEMAEGAKAaarLQDQLAAGEAVVSLDPSMIDGSPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  78 RDRLDGEV-PATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSDNELVVAQGIENT 156
Cdd:PRK13866  79 ADRLPADVdPKFEQLEASISQEGQQVPILVRPHPEAAGRYQIVYGRRRLRAAVNLRREVSAIVRNLTDRELVVAQGRENL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398 157 ARKDLSYIERAVFALSLETHGFGRDLIMQALSTEKTELSKLLSVAKGIPGSLVKAIGAAPSMGRRRWMDIAEKITDPKAM 236
Cdd:PRK13866 159 DRADLSFIEKALFALRLEDAGFDRATIIAALSTDKADLSRYITVARGIPLNLATQIGPASKAGRSRWVALAEGLGKPKAT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398 237 EVARNAIHRPEFEALGSDERFMMVLAEVSKKP-PREQTISEWKPNGGKVAAKI-KDTGR-AYTLSLKTAEAdegFGAYLT 313
Cdd:PRK13866 239 DAIEAVLESEQFKHSDSDARFDLIFNAVSKPPaKRPKKVRAWSTPKGKKAATIrQETGRtALVFDEKLVPT---FGEYVA 315
                        330
                 ....*....|.
gi 499218398 314 KRLDDLYADWQ 324
Cdd:PRK13866 316 DQLDSLYAQFI 326
RepB_like_N cd16405
plasmid segregation replication protein B like protein, N-terminal domain; RepB, found on ...
67-155 2.70e-42

plasmid segregation replication protein B like protein, N-terminal domain; RepB, found on plasmids and secondary chromosomes, works along with repA in directing plasmid segregation, and has been shown in Rhizobium etli to require the parS centromere-like sequence for full transcriptional repression of the repABC operon, inducing plasmid incompatibility. RepA is a Walker-type ATPase that complexes with RepB to form DNA-protein complexes in the presence of ATP/ADP. RepC is an initiator protein for the plasmid. repA and repB are homologous to the parA and ParB genes of the parABS partitioning system found on primary chromosomes.


Pssm-ID: 319262 [Multi-domain]  Cd Length: 91  Bit Score: 141.53  E-value: 2.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  67 LDPELIDGSFVRDRL--DGEVPATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRKVRAVVRRLSD 144
Cdd:cd16405    1 LDPDLIDPSFIADRLedDFDDDEFEELKESIRESGQQVPILVRPHPEEGGRYEIVYGHRRLRACRELGLPVRAIVRELSD 80
                         90
                 ....*....|.
gi 499218398 145 NELVVAQGIEN 155
Cdd:cd16405   81 EELVVAQGQEN 91
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
59-243 4.61e-39

Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441084 [Multi-domain]  Cd Length: 241  Bit Score: 138.20  E-value: 4.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  59 KSGERVVELDPELIDGSFVRDRLDGEVPATDDIVRSIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLG-RKVRA 137
Cdd:COG1475    2 KEGEEIREIPIDKIVPSPYNPRRTFDEEALEELAASIREHGLLQPILVRPLGD--GRYEIIAGERRLRAAKLLGlETVPA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398 138 VVRRLSDNELVVAQGIENTARKDLSYIERAVFALSL-ETHGFGRDLIMQALSTEKTELSKLLSVAKgIPGSLVKAIGAAp 216
Cdd:COG1475   80 IVRDLDDEEALELALIENLQREDLNPLEEARAYQRLlEEFGLTQEEIAERLGKSRSEVSNLLRLLK-LPPEVQEALREG- 157
                        170       180
                 ....*....|....*....|....*..
gi 499218398 217 SMGRRRWMDIAeKITDPKAMEVARNAI 243
Cdd:COG1475  158 KLSLGHARALA-ALSDPERQEELAEKI 183
parB_part TIGR00180
ParB/RepB/Spo0J family partition protein; This model represents the most well-conserved core ...
61-243 1.09e-29

ParB/RepB/Spo0J family partition protein; This model represents the most well-conserved core of a set of chromosomal and plasmid partition proteins related to ParB, including Spo0J, RepB, and SopB. Spo0J has been shown to bind a specific DNA sequence that, when introduced into a plasmid, can serve as partition site. Study of RepB, which has nicking-closing activity, suggests that it forms a transient protein-DNA covalent intermediate during the strand transfer reaction.


Pssm-ID: 272946 [Multi-domain]  Cd Length: 187  Bit Score: 112.09  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   61 GERVVELDPELIDGSFVRDRLDGEVPATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRK-VRAVV 139
Cdd:TIGR00180   2 AEGLIEIDIDLLQPNPYQPRKDFSEESLAELIESIKEQGQLQPILVRKHPDQPGRYEIIAGERRWRAAKLAGLKtIPAIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  140 RRLSDNELVVAQGIENTARKDLSYIERAVFALSLETHGFGR-DLIMQALSTEKTELSKLLSVAKgIPGSLVKAIGAAPSM 218
Cdd:TIGR00180  82 RELDDEQMLADALIENIQREDLSPIEEAQAYKRLLEKFSMTqEDLAKKIGKSRAHITNLLRLLK-LPSEIQSAIPEASGL 160
                         170       180
                  ....*....|....*....|....*..
gi 499218398  219 GRRRWMDIAEKITD-PKAME-VARNAI 243
Cdd:TIGR00180 161 LSSGHARLLLALKKkPKLQElLASIII 187
ParB smart00470
ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ...
65-155 1.28e-17

ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB also nicks supercoiled plasmid DNA preferably at sites with potential single-stranded character, like AT-rich regions and sequences that can form cruciform structures. ParB also exhibits 5-->3 exonuclease activity.


Pssm-ID: 214678 [Multi-domain]  Cd Length: 89  Bit Score: 76.57  E-value: 1.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398    65 VELDPELIDGSFVRDRLDGEvPATDDIVRSIEENGQEVPILVRQHPdleGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLS 143
Cdd:smart00470   1 VEVPIEKLRPNPDQPRLTSE-ESLEELAESIKENGLLQPIIVRPND---GRYEIIDGERRLRAAKLLGlKEVPVIVRDLD 76
                           90
                   ....*....|..
gi 499218398   144 DNELVVAQGIEN 155
Cdd:smart00470  77 DEEAIALSLEEN 88
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
65-155 5.46e-16

ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localizes to both poles of the predivisional cell following completion of DNA replication. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4.


Pssm-ID: 426651 [Multi-domain]  Cd Length: 90  Bit Score: 72.31  E-value: 5.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398   65 VELDPELIDGSFVRDRLDGEvPATDDIVRSIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLS 143
Cdd:pfam02195   1 EEVPISKLRPNPDQPRKDSE-ESLEELAASIKKRGLLQPIIVRKTPD--GRYEIIAGERRLRAAKLLGlKEVPVIVREID 77
                          90
                  ....*....|..
gi 499218398  144 DNELVVAQGIEN 155
Cdd:pfam02195  78 DEEAIALSLIEN 89
RepB pfam07506
RepB plasmid partitioning protein; This family includes proteins with sequence similarity to ...
157-322 4.42e-14

RepB plasmid partitioning protein; This family includes proteins with sequence similarity to the RepB partitioning protein of the large Ti (tumour-inducing) plasmids of Agrobacterium tumefaciens.


Pssm-ID: 311449  Cd Length: 185  Bit Score: 69.43  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  157 ARKDLSYIERAVFALSLETHGFGRDLIMQALSTEKTELSKllSVAKGIPGSL--------------VKAIGAAPSMGRRR 222
Cdd:pfam07506   1 ARADLSFIERARFAARLLERGVPRAEIAAALGLDPQTVSK--MVARAIPEGIcpeeeallkdvetgIAAFGLARKIGRDR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  223 WMDIAEKITDPKAMEVArnaihrpEFEALGSDERFMMVLAevSKKPPREQTIS---------EWKPNGGKVAAKIKDTGR 293
Cdd:pfam07506  79 WVELAELLAAAKNVESA-------YFRALLADTRFSQLVK--PLRPKRIKGVSgksaarpegKWARLQTAVLAIYEDEGR 149
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 499218398  294 AyTLSLKTAEA-------DEGFGAYLTKRLDDLYAD 322
Cdd:pfam07506 150 Q-TLHLKAAEGyldrllfNTRFGRYLARNLPELYEE 184
SPO0J_N cd16393
Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member; ...
94-161 1.70e-13

Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member; Spo0J (stage 0 sporulation protein J) is a ParB family member, a critical component of the ParABS-type bacterial chromosome segregation system. The Spo0J N-terminal region acts in protein-protein interaction and is adjacent to the DNA-binding domain that binds to parS sites. Two Spo0J bind per parS site, and Spo0J interacts with neighbors via the N-terminal domain to form oligomers via an Arginine-rich patch (RRXR). This superfamily represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319251 [Multi-domain]  Cd Length: 97  Bit Score: 65.58  E-value: 1.70e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499218398  94 SIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLSDNELVVAQGIENTARKDL 161
Cdd:cd16393   31 SIKEHGLLQPIVVRKVGD--GRYEIIAGERRWRAAKLAGlTEIPAIVRDLDDEEALELALIENIQREDL 97
ParB_N_like cd16407
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
89-150 2.25e-12

ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning systems; This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319264 [Multi-domain]  Cd Length: 86  Bit Score: 62.15  E-value: 2.25e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499218398  89 DDIVRSIEENGQEVPILVRqhPDLEGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLSDNELVVA 150
Cdd:cd16407   21 EELVESIKENGVLTPIIVR--PREDGGYEIISGHRRKRACELAGlETIPVIVREMDDDEAVIA 81
Noc_N cd16396
nucleoid occlusion protein, N-terminal domain, and related domains of the ParB partitioning ...
89-155 1.24e-11

nucleoid occlusion protein, N-terminal domain, and related domains of the ParB partitioning protein family; Nucleoid occlusion protein has been shown in Bacillus subtilis to bind to specific DNA sequences on the chromosome (Noc-binding DNA sequences, NBS), inhibiting cell division near the nucleoid and thereby protecting the chromosome. This N-terminal domain is related to the N-terminal domain of ParB/repB partitioning system proteins.


Pssm-ID: 319254 [Multi-domain]  Cd Length: 95  Bit Score: 60.31  E-value: 1.24e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499218398  89 DDIVRSIEENGQEVPILVRqhPDLEGRYQVAYGHRRLRAVRLLG-RKVRAVVRRLSDNELVVAQGIEN 155
Cdd:cd16396   28 EELAESIKEHGLLQPIVVR--KTKDGGYEIVAGERRWRAAKLLGwEKIPAIIRDLSDKEALEIALIEN 93
KorB_N_like cd16398
ParB-like partition protein of low copy number plasmid RK2, N-terminal domain and related ...
78-161 1.37e-11

ParB-like partition protein of low copy number plasmid RK2, N-terminal domain and related domains; KorB, a member of the ParB like family, is present on the low copy number, broad host range plasmid RK2. KorB encodes a gene product involved in segregation of RK2 and acts as a transcriptional regulator, down-regulating at least 6 RK2 operons. KorB binds RNA polymerase and acts cooperatively with several co-repressors in modulating transcription. KorB is comprised of 3 domains, including a beta-strand C-terminal domain similar to SH3 domains and an alpha helical central domain that interacts with operator DNA. In ParB of P1 and SopB of F, the N-terminal region is responsible for interaction with the parA component. However, korB interaction with the RK2 parA-equivalent IncC has been mapped to the central HTH motif. This family is related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319256 [Multi-domain]  Cd Length: 91  Bit Score: 59.97  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  78 RDRLDGEvpATDDIVRSIEENGQEVPILVRQHPDLEGRYQVAYGHRRLRAVRLLGRK-VRAVVRRLSDNelvVAQGIENT 156
Cdd:cd16398   12 RTEFDEE--KIEELAASIKERGVKSPISVRPHPEKPGKYIINHGARRYRASKWAGLKtIPAFIDNDHDD---FDQVIENI 86

                 ....*
gi 499218398 157 ARKDL 161
Cdd:cd16398   87 QREDL 91
ParB_N_Srx cd16387
ParB N-terminal domain and sulfiredoxin protein-related families; The ParB N-terminal domain ...
89-134 5.14e-09

ParB N-terminal domain and sulfiredoxin protein-related families; The ParB N-terminal domain/Sulfiredoxin (Srx) superfamily contains proteins with diverse activities. Many of the families are involved in segregation and competition between plasmids and chromosomes. Several families share similar activities with the N-terminal domain of ParB (Spo0J in Bacillus subtilis), a DNA-binding component of the prokaryotic parABS partitioning system. Also within this superfamily is sulfiredoxin (Srx; reactivator of oxidatively inactivated 2-cys peroxiredoxins), RepB N-terminal domain (plasmid segregation replication protein B like protein), nucleoid occlusion protein, KorB N-terminal domain partition protein of low copy number plasmid RK2, irbB (immunoglobulin-binding regulator that activates eib genes), N-terminal domain of sopB protein (promotes proper partitioning of F1 plasmid), fertility inhibition factors OSA and FiwA,DNA sulfur modification protein DndB, and a ParB-like toxin domain. Other activities includes a StrR (regulator in the streptomycin biosynthetic gene cluster), and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators sbnI (Staphylococcus aureus siderophore biosynthetic gene cluster ). Nuclease activity has also been reported in Arabidopsis Srx.


Pssm-ID: 319246 [Multi-domain]  Cd Length: 54  Bit Score: 51.43  E-value: 5.14e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499218398  89 DDIVRSIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLGRK 134
Cdd:cd16387    6 EELAESIREHGVLQPIIVRPLPD--GRYEIIAGERRWRAAKLAGLT 49
ParB_N_like cd16408
ParB N-terminal, parA -binding, -like domain of bacterial and plasmid parABS partitioning ...
89-146 9.04e-07

ParB N-terminal, parA -binding, -like domain of bacterial and plasmid parABS partitioning systems; This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319265 [Multi-domain]  Cd Length: 84  Bit Score: 46.08  E-value: 9.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  89 DDIVRSIEENGQEVPILVRqhPDLEGRYQVAYGHRRLRAVRLLG-RKVRAVVRR-LSDNE 146
Cdd:cd16408   18 EDMVESIKENGVLQPIIVR--PIEDGKYEILAGHNRVNAAKLAGlTTIPAIIKEnLTDEE 75
pNOB8_ParB_N_like cd16404
pNOB8 ParB-like N-terminal domain, plasmid partitioning system protein domain; archaeal pNOB8 ...
89-134 4.97e-06

pNOB8 ParB-like N-terminal domain, plasmid partitioning system protein domain; archaeal pNOB8 ParB acts in a plasmid partitioning system made up of 3 parts: AspA, ParA motor protein, and ParB, which links ParA to the protein-DNA superhelix. As demonstrated in Sulfolobus, AspA spreads along DNA, which allows ParB binding, and links to the Walker-motif containing ParA motor protein. The Sulfolobus ParB C-terminal domain resembles eukaryotic segregation protein CenpA, and other histones. This family is related to the N-terminal domain of ParB (Spo0J in Bacillus subtilis), a DNA-binding component of the prokaryotic parABS partitioning system and related proteins.


Pssm-ID: 319261 [Multi-domain]  Cd Length: 69  Bit Score: 43.80  E-value: 4.97e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499218398  89 DDIVRSIEENGQEVPILVRQHpdlegrYQVAYGHRRLRAVRLLGRK 134
Cdd:cd16404   18 EELKESIRKNGIIVPIIVDQD------GVIIDGHHRYRIAKELGIK 57
ParB_N_like cd16411
ParB N-terminal, parA -binding, domain of bacterial and plasmid parABS partitioning systems; ...
89-155 5.76e-06

ParB N-terminal, parA -binding, domain of bacterial and plasmid parABS partitioning systems; This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319268 [Multi-domain]  Cd Length: 90  Bit Score: 44.13  E-value: 5.76e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499218398  89 DDIVRSIEENGQEVPILVRQHPDLEG--RYQVAYGHRRLRAVRLLGRK-VRAVVRRLSDNELVVAQGIEN 155
Cdd:cd16411   20 REIVESIATVGLKRPITVRRRSSDDGgyKYDLVCGQGRLEAFKALGETeIPAIVVDVDEEDALLMSLVEN 89
ParB_N_like cd16409
ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems; This family ...
91-155 7.47e-06

ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems; This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319266 [Multi-domain]  Cd Length: 74  Bit Score: 43.44  E-value: 7.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499218398  91 IVRSIEENGQEVPILVRQHPDleGRYQVAYGHRRLRAVRLLGRK-VRAVVRRLSDNELVVAQGIEN 155
Cdd:cd16409    9 LAQSIAEHGLLTPITVRQDPG--GRYTLIAGAHRLAAAKLLGWDtIDAIIVKADDLEAELLEIDEN 72
ParB_N_like cd16406
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
94-158 1.10e-04

ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning systems; This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319263 [Multi-domain]  Cd Length: 82  Bit Score: 40.19  E-value: 1.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499218398  94 SIEENGQEVPILVRQHPDlEGRYQVAYGHRRLRAVRLL-GRKVRAV-----VRRLSDNELVVAQGIENTAR 158
Cdd:cd16406   12 SIAAHGLLQNLVVRPAKK-KGRYEVVAGGRRLRALQLLaERGRLPAdypvpVKVVPDADALEASLAENVQR 81
ParB_N_like cd16410
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
77-134 9.35e-03

ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning systems; This family represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.


Pssm-ID: 319267 [Multi-domain]  Cd Length: 80  Bit Score: 34.87  E-value: 9.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499218398  77 VRDRLDGEVPATDDIVRSIEENGQEVPILVrqhpdlEGRYQVAYGHRRLRAVRLLGRK 134
Cdd:cd16410    6 VKKRIRKDLGDIEALAESIKRHGLLNPIVV------TPDNELIAGERRLEAAKLLGWE 57
 
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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