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Conserved domains on  [gi|759495860|ref|WP_043216691|]
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MULTISPECIES: plasmid partitioning protein RepB C-terminal domain-containing protein [Burkholderia]

Protein Classification

ParB_N_like and RepB domain-containing protein( domain architecture ID 11445134)

ParB_N_like and RepB domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParB_N_like cd16411
ParB N-terminal, parA -binding, domain of bacterial and plasmid parABS partitioning systems; ...
 13-102 1.07e-45

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: 149.29  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  13 IPVSQIEVINPRERNGRVFNEIVDNIKTIGLKKPILVTPRVTAAGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDED 92
Cdd:cd16411    1 IPIDDIRVLNPRSRNRKIFREIVESIATVGLKRPITVRRRSSDDGGYKYDLVCGQGRLEAFKALGETEIPAIVVDVDEED 80

                         90
                 ....*....|
gi 759495860  93 AYVMSLTENI 102
Cdd:cd16411   81 ALLMSLVENI 90
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
 6-228 2.51e-34

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: 124.72  E-value: 2.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   6 QPGEIRMIPVSQIEV--INPRER-NGRVFNEIVDNIKTIGLKKPILVTPRvtaaGIEKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:COG1475    3 EGEEIREIPIDKIVPspYNPRRTfDEEALEELAASIREHGLLQPILVRPL----GDGRYEIIAGERRLRAAKLLGLETVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  83 ALVVHVSDEDAYVMSLTENIARRQCRPIERLAGI-RLLQEQGYAPKVIAEKTGLTSTYVHGILTLLRQGEErLVVAVEKG 161
Cdd:COG1475   79 AIVRDLDDEEALELALIENLQREDLNPLEEARAYqRLLEEFGLTQEEIAERLGKSRSEVSNLLRLLKLPPE-VQEALREG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759495860 162 LVPLNAALMIVGAgdDDAEIQAALQEAYESGKLRGKQlmsARRVIERRKALGKSTAHNMSSKSAAVT 228
Cdd:COG1475  158 KLSLGHARALAAL--SDPERQEELAEKIIEEGLSVRE---TEELVKALAKDLARLERRLSELGTKVK 219
 
Name Accession Description Interval E-value
ParB_N_like cd16411
ParB N-terminal, parA -binding, domain of bacterial and plasmid parABS partitioning systems; ...
 13-102 1.07e-45

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: 149.29  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  13 IPVSQIEVINPRERNGRVFNEIVDNIKTIGLKKPILVTPRVTAAGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDED 92
Cdd:cd16411    1 IPIDDIRVLNPRSRNRKIFREIVESIATVGLKRPITVRRRSSDDGGYKYDLVCGQGRLEAFKALGETEIPAIVVDVDEED 80

                         90
                 ....*....|
gi 759495860  93 AYVMSLTENI 102
Cdd:cd16411   81 ALLMSLVENI 90
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
 6-228 2.51e-34

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: 124.72  E-value: 2.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   6 QPGEIRMIPVSQIEV--INPRER-NGRVFNEIVDNIKTIGLKKPILVTPRvtaaGIEKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:COG1475    3 EGEEIREIPIDKIVPspYNPRRTfDEEALEELAASIREHGLLQPILVRPL----GDGRYEIIAGERRLRAAKLLGLETVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  83 ALVVHVSDEDAYVMSLTENIARRQCRPIERLAGI-RLLQEQGYAPKVIAEKTGLTSTYVHGILTLLRQGEErLVVAVEKG 161
Cdd:COG1475   79 AIVRDLDDEEALELALIENLQREDLNPLEEARAYqRLLEEFGLTQEEIAERLGKSRSEVSNLLRLLKLPPE-VQEALREG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759495860 162 LVPLNAALMIVGAgdDDAEIQAALQEAYESGKLRGKQlmsARRVIERRKALGKSTAHNMSSKSAAVT 228
Cdd:COG1475  158 KLSLGHARALAAL--SDPERQEELAEKIIEEGLSVRE---TEELVKALAKDLARLERRLSELGTKVK 219
parB_part TIGR00180
ParB/RepB/Spo0J family partition protein; This model represents the most well-conserved core ...
 6-147 1.96e-16

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: 75.88  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860    6 QPGEIRMIPVSQIEVINPRERNGRV---FNEIVDNIKTIGLKKPILVTPRVTAAGieKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:TIGR00180   1 VAEGLIEIDIDLLQPNPYQPRKDFSeesLAELIESIKEQGQLQPILVRKHPDQPG--RYEIIAGERRWRAAKLAGLKTIP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759495860   83 ALVVHVSDEDAYVMSLTENIARRQCRPIER-LAGIRLLQEQGYAPKVIAEKTGLTSTYVHGILTLL 147
Cdd:TIGR00180  79 AIVRELDDEQMLADALIENIQREDLSPIEEaQAYKRLLEKFSMTQEDLAKKIGKSRAHITNLLRLL 144
ParB smart00470
ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ...
 11-102 7.01e-13

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: 63.09  E-value: 7.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860    11 RMIPVSQIEVI--NPRERNGRVFNEIVDNIKTIGLKKPILVTPRVTaagieKYLLVCGEGRLKAFRTLGEATIPALVVHV 88
Cdd:smart00470   1 VEVPIEKLRPNpdQPRLTSEESLEELAESIKENGLLQPIIVRPNDG-----RYEIIDGERRLRAAKLLGLKEVPVIVRDL 75

                           90
                   ....*....|....
gi 759495860    89 SDEDAYVMSLTENI 102
Cdd:smart00470  76 DDEEAIALSLEENI 89
RepB pfam07506
RepB plasmid partitioning protein; This family includes proteins with sequence similarity to ...
 103-267 1.72e-12

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: 64.80  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  103 ARRQCRPIERLAGIRLLQEQGYAPKVIAEKTGLTSTYVHG-----ILTLLRQGEERLVVAVEKGLVPLNAALMIvgAGDD 177
Cdd:pfam07506   1 ARADLSFIERARFAARLLERGVPRAEIAAALGLDPQTVSKmvaraIPEGICPEEEALLKDVETGIAAFGLARKI--GRDR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  178 DAEIQAAL------QEAYESGKLRGKQLMSARRVIERRKALGKSTAH--NMSSKSAAVTTsSLVRTYEREvERQKSMVRK 249
Cdd:pfam07506  79 WVELAELLaaaknvESAYFRALLADTRFSQLVKPLRPKRIKGVSGKSaaRPEGKWARLQT-AVLAIYEDE-GRQTLHLKA 156

                         170
                  ....*....|....*...
gi 759495860  250 AEFAQQRLLFVVGALRQL 267
Cdd:pfam07506 157 AEGYLDRLLFNTRFGRYL 174
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
 11-102 8.32e-10

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: 54.59  E-value: 8.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   11 RMIPVSQIEVINPRERNGRV--FNEIVDNIKTIGLKKPILVTPrvTAAGIekYLLVCGEGRLKAFRTLGEATIPALVVHV 88
Cdd:pfam02195   1 EEVPISKLRPNPDQPRKDSEesLEELAASIKKRGLLQPIIVRK--TPDGR--YEIIAGERRLRAAKLLGLKEVPVIVREI 76

                          90
                  ....*....|....
gi 759495860   89 SDEDAYVMSLTENI 102
Cdd:pfam02195  77 DDEEAIALSLIENI 90
PRK13832 PRK13832
plasmid partitioning protein; Provisional
 37-184 3.77e-07

plasmid partitioning protein; Provisional


Pssm-ID: 184353 [Multi-domain]  Cd Length: 520  Bit Score: 51.25  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  37 NIKTIGLKKPILVTPRVTaaGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDEDAYVMSLTENIARRQCRPIERLAGI 116
Cdd:PRK13832  34 TIKAVGIVQPPVVSPEED--GGNGYIIQAGHRRVKQAIAAGLEEIEVLVTEAANDNGAMRSMVENIAREPLNPVDQWRAI 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860 117 RLLQEQGYAPKVIAEKTGLTSTYVHGiLTLLRQGEERLVVAVEKGLVPLNAALMIVGAG--DDDAEIQAA 184
Cdd:PRK13832 112 ERLVALGWTEEAIAVALALPVRQIRK-LRLLANVLPAMLDHMAKGDMPNEQQLRTIAAAslDEQKEVWKA 180
PRK13866 PRK13866
plasmid partitioning protein RepB; Provisional
 31-130 5.60e-05

plasmid partitioning protein RepB; Provisional


Pssm-ID: 172387 [Multi-domain]  Cd Length: 336  Bit Score: 44.18  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  31 FNEIVDNIKTIGLKKPILVTPRVTAAGieKYLLVCGEGRLKAFRTLGEAtIPALVVHVSDEDAYVMSLTENIARRQCRPI 110
Cdd:PRK13866  90 FEQLEASISQEGQQVPILVRPHPEAAG--RYQIVYGRRRLRAAVNLRRE-VSAIVRNLTDRELVVAQGRENLDRADLSFI 166

                         90       100
                 ....*....|....*....|.
gi 759495860 111 ERLAGIRLLQEQGY-APKVIA 130
Cdd:PRK13866 167 EKALFALRLEDAGFdRATIIA 187
 
Name Accession Description Interval E-value
ParB_N_like cd16411
ParB N-terminal, parA -binding, domain of bacterial and plasmid parABS partitioning systems; ...
 13-102 1.07e-45

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: 149.29  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  13 IPVSQIEVINPRERNGRVFNEIVDNIKTIGLKKPILVTPRVTAAGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDED 92
Cdd:cd16411    1 IPIDDIRVLNPRSRNRKIFREIVESIATVGLKRPITVRRRSSDDGGYKYDLVCGQGRLEAFKALGETEIPAIVVDVDEED 80

                         90
                 ....*....|
gi 759495860  93 AYVMSLTENI 102
Cdd:cd16411   81 ALLMSLVENI 90
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
 6-228 2.51e-34

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: 124.72  E-value: 2.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   6 QPGEIRMIPVSQIEV--INPRER-NGRVFNEIVDNIKTIGLKKPILVTPRvtaaGIEKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:COG1475    3 EGEEIREIPIDKIVPspYNPRRTfDEEALEELAASIREHGLLQPILVRPL----GDGRYEIIAGERRLRAAKLLGLETVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  83 ALVVHVSDEDAYVMSLTENIARRQCRPIERLAGI-RLLQEQGYAPKVIAEKTGLTSTYVHGILTLLRQGEErLVVAVEKG 161
Cdd:COG1475   79 AIVRDLDDEEALELALIENLQREDLNPLEEARAYqRLLEEFGLTQEEIAERLGKSRSEVSNLLRLLKLPPE-VQEALREG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759495860 162 LVPLNAALMIVGAgdDDAEIQAALQEAYESGKLRGKQlmsARRVIERRKALGKSTAHNMSSKSAAVT 228
Cdd:COG1475  158 KLSLGHARALAAL--SDPERQEELAEKIIEEGLSVRE---TEELVKALAKDLARLERRLSELGTKVK 219
SPO0J_N cd16393
Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member; ...
 10-104 2.56e-17

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: 75.60  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  10 IRMIPVSQIEVI--NPRerngRVFN-----EIVDNIKTIGLKKPILVTPrvtaAGIEKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:cd16393    1 VQEIPIDKIRPNpyQPR----KEFDeealkELAESIKEHGLLQPIVVRK----VGDGRYEIIAGERRWRAAKLAGLTEIP 72

                         90       100
                 ....*....|....*....|..
gi 759495860  83 ALVVHVSDEDAYVMSLTENIAR 104
Cdd:cd16393   73 AIVRDLDDEEALELALIENIQR 94
parB_part TIGR00180
ParB/RepB/Spo0J family partition protein; This model represents the most well-conserved core ...
 6-147 1.96e-16

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: 75.88  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860    6 QPGEIRMIPVSQIEVINPRERNGRV---FNEIVDNIKTIGLKKPILVTPRVTAAGieKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:TIGR00180   1 VAEGLIEIDIDLLQPNPYQPRKDFSeesLAELIESIKEQGQLQPILVRKHPDQPG--RYEIIAGERRWRAAKLAGLKTIP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759495860   83 ALVVHVSDEDAYVMSLTENIARRQCRPIER-LAGIRLLQEQGYAPKVIAEKTGLTSTYVHGILTLL 147
Cdd:TIGR00180  79 AIVRELDDEQMLADALIENIQREDLSPIEEaQAYKRLLEKFSMTQEDLAKKIGKSRAHITNLLRLL 144
Noc_N cd16396
nucleoid occlusion protein, N-terminal domain, and related domains of the ParB partitioning ...
 8-102 9.40e-15

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: 68.40  E-value: 9.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   8 GEIRMIPVSQIeVINPrERNGRVFN-----EIVDNIKTIGLKKPILVTPRVTaagiEKYLLVCGEGRLKAFRTLGEATIP 82
Cdd:cd16396    1 GEVLEIPVADI-IPNP-YQPRKEFDeeeieELAESIKEHGLLQPIVVRKTKD----GGYEIVAGERRWRAAKLLGWEKIP 74

                         90       100
                 ....*....|....*....|
gi 759495860  83 ALVVHVSDEDAYVMSLTENI 102
Cdd:cd16396   75 AIIRDLSDKEALEIALIENL 94
ParB smart00470
ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ...
 11-102 7.01e-13

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: 63.09  E-value: 7.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860    11 RMIPVSQIEVI--NPRERNGRVFNEIVDNIKTIGLKKPILVTPRVTaagieKYLLVCGEGRLKAFRTLGEATIPALVVHV 88
Cdd:smart00470   1 VEVPIEKLRPNpdQPRLTSEESLEELAESIKENGLLQPIIVRPNDG-----RYEIIDGERRLRAAKLLGLKEVPVIVRDL 75

                           90
                   ....*....|....
gi 759495860    89 SDEDAYVMSLTENI 102
Cdd:smart00470  76 DDEEAIALSLEENI 89
RepB pfam07506
RepB plasmid partitioning protein; This family includes proteins with sequence similarity to ...
 103-267 1.72e-12

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: 64.80  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  103 ARRQCRPIERLAGIRLLQEQGYAPKVIAEKTGLTSTYVHG-----ILTLLRQGEERLVVAVEKGLVPLNAALMIvgAGDD 177
Cdd:pfam07506   1 ARADLSFIERARFAARLLERGVPRAEIAAALGLDPQTVSKmvaraIPEGICPEEEALLKDVETGIAAFGLARKI--GRDR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  178 DAEIQAAL------QEAYESGKLRGKQLMSARRVIERRKALGKSTAH--NMSSKSAAVTTsSLVRTYEREvERQKSMVRK 249
Cdd:pfam07506  79 WVELAELLaaaknvESAYFRALLADTRFSQLVKPLRPKRIKGVSGKSaaRPEGKWARLQT-AVLAIYEDE-GRQTLHLKA 156

                         170
                  ....*....|....*...
gi 759495860  250 AEFAQQRLLFVVGALRQL 267
Cdd:pfam07506 157 AEGYLDRLLFNTRFGRYL 174
PRTRC_parB TIGR03734
PRTRC system ParB family protein; A novel genetic system characterized by six major proteins, ...
 22-119 3.26e-12

PRTRC system ParB family protein; A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family the member related to ParB, and is designated PRTRC system ParB family protein.


Pssm-ID: 274755 [Multi-domain]  Cd Length: 554  Bit Score: 66.66  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   22 NPRER-NGRVFNEIVDNIKTIGLKKPILVTPrvtAAGIEKYLLVCGEGRLKAFRTLG--EATIPALVVHVSDEDAYVMSL 98
Cdd:TIGR03734   7 NPRRYfDPAEMAELVESIRAKGVLQPILVRP---VPGSDLYEVVAGERRYRAALEVFgeDYDIPALIKVLTDEEAEAAAL 83

                          90       100
                  ....*....|....*....|..
gi 759495860   99 TENIARRQCRPIER-LAGIRLL 119
Cdd:TIGR03734  84 IENVQRADMSPAEEaEAAARLL 105
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
 11-102 8.32e-10

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: 54.59  E-value: 8.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860   11 RMIPVSQIEVINPRERNGRV--FNEIVDNIKTIGLKKPILVTPrvTAAGIekYLLVCGEGRLKAFRTLGEATIPALVVHV 88
Cdd:pfam02195   1 EEVPISKLRPNPDQPRKDSEesLEELAASIKKRGLLQPIIVRK--TPDGR--YEIIAGERRLRAAKLLGLKEVPVIVREI 76

                          90
                  ....*....|....
gi 759495860   89 SDEDAYVMSLTENI 102
Cdd:pfam02195  77 DDEEAIALSLIENI 90
PRK13832 PRK13832
plasmid partitioning protein; Provisional
 37-184 3.77e-07

plasmid partitioning protein; Provisional


Pssm-ID: 184353 [Multi-domain]  Cd Length: 520  Bit Score: 51.25  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  37 NIKTIGLKKPILVTPRVTaaGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDEDAYVMSLTENIARRQCRPIERLAGI 116
Cdd:PRK13832  34 TIKAVGIVQPPVVSPEED--GGNGYIIQAGHRRVKQAIAAGLEEIEVLVTEAANDNGAMRSMVENIAREPLNPVDQWRAI 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860 117 RLLQEQGYAPKVIAEKTGLTSTYVHGiLTLLRQGEERLVVAVEKGLVPLNAALMIVGAG--DDDAEIQAA 184
Cdd:PRK13832 112 ERLVALGWTEEAIAVALALPVRQIRK-LRLLANVLPAMLDHMAKGDMPNEQQLRTIAAAslDEQKEVWKA 180
KorB_N_like cd16398
ParB-like partition protein of low copy number plasmid RK2, N-terminal domain and related ...
 22-104 4.42e-07

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: 47.26  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  22 NPR-ERNGRVFNEIVDNIKTIGLKKPILVTPRVTAAGieKYLLVCGEGRLKAFRTLGEATIPALVVHVSDEDAYVMsltE 100
Cdd:cd16398   10 NPRtEFDEEKIEELAASIKERGVKSPISVRPHPEKPG--KYIINHGARRYRASKWAGLKTIPAFIDNDHDDFDQVI---E 84


                 ....
gi 759495860 101 NIAR 104
Cdd:cd16398   85 NIQR 88
RepB_like_N cd16405
plasmid segregation replication protein B like protein, N-terminal domain; RepB, found on ...
 31-101 4.72e-07

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: 47.15  E-value: 4.72e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759495860  31 FNEIVDNIKTIGLKKPILVTPRVTAAGieKYLLVCGEGRLKAFRTLGeatIP--ALVVHVSDEDAYVMSLTEN 101
Cdd:cd16405   24 FEELKESIRESGQQVPILVRPHPEEGG--RYEIVYGHRRLRACRELG---LPvrAIVRELSDEELVVAQGQEN 91
ParB_N_Srx cd16387
ParB N-terminal domain and sulfiredoxin protein-related families; The ParB N-terminal domain ...
 33-84 5.72e-07

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: 45.66  E-value: 5.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759495860  33 EIVDNIKTIGLKKPILVTPRVTaagiEKYLLVCGEGRLKAFRTLGEATIPAL 84
Cdd:cd16387    7 ELAESIREHGVLQPIIVRPLPD----GRYEIIAGERRWRAAKLAGLTTIPVV 54
ParB_N_like cd16409
ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems; This family ...
 32-101 6.11e-07

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: 46.14  E-value: 6.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  32 NEIVDNIKTIGLKKPILVTPRvtaaGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDEDAYVMSLTEN 101
Cdd:cd16409    7 EALAQSIAEHGLLTPITVRQD----PGGRYTLIAGAHRLAAAKLLGWDTIDAIIVKADDLEAELLEIDEN 72
ParB_N_like cd16406
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
 32-105 3.31e-06

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: 44.43  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  32 NEIVDNIKTIGLKKPILVTPrVTAAGieKYLLVCGEGRLKAFRTLGEA-------TIPALVVHvsDEDAYVMSLTENIAR 104
Cdd:cd16406    7 EELAASIAAHGLLQNLVVRP-AKKKG--RYEVVAGGRRLRALQLLAERgrlpadyPVPVKVVP--DADALEASLAENVQR 81


                 .
gi 759495860 105 R 105
Cdd:cd16406   82 E 82
ParB_N_like cd16410
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
 33-101 3.71e-06

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: 44.11  E-value: 3.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  33 EIVDNIKTIGLKKPILVTPrvtaagieKYLLVCGEGRLKAFRTLGEATIPALVVHVSDE-DAYVMSLTEN 101
Cdd:cd16410   19 ALAESIKRHGLLNPIVVTP--------DNELIAGERRLEAAKLLGWETIEVRVMDIEDEkEKLELEIEEN 80
ParB_N_like cd16408
ParB N-terminal, parA -binding, -like domain of bacterial and plasmid parABS partitioning ...
 31-96 1.02e-05

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: 43.00  E-value: 1.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759495860  31 FNEIVDNIKTIGLKKPILVTPRvtaaGIEKYLLVCGEGRLKAFRTLGEATIPALV-VHVSDEDAYVM 96
Cdd:cd16408   17 LEDMVESIKENGVLQPIIVRPI----EDGKYEILAGHNRVNAAKLAGLTTIPAIIkENLTDEEAKLI 79
ParB_N_like_MT cd16403
ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent ...
 18-96 1.06e-05

ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent methyltransferase; This family represents domains related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, fused to a variety of C-terminal domains, including S-adenosylmethionine-dependent methyltransferase-like domains. 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: 319260 [Multi-domain]  Cd Length: 88  Bit Score: 43.21  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  18 IEVINPRERNGRV-----FNEIVDNIKTIGLKKPILVTprvtaagiEKYLLVCGEGRLKAFRTLGEATIPALVV-HVSDE 91
Cdd:cd16403    2 IDDLKPYPRNARThsekqIEQLAASIREFGFTNPILVD--------EDGVIIAGHGRLLAAKLLGLKEVPVIRLdHLSEA 73


                 ....*..
gi 759495860  92 D--AYVM 96
Cdd:cd16403   74 QkrAYRI 80
PRK13866 PRK13866
plasmid partitioning protein RepB; Provisional
 31-130 5.60e-05

plasmid partitioning protein RepB; Provisional


Pssm-ID: 172387 [Multi-domain]  Cd Length: 336  Bit Score: 44.18  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  31 FNEIVDNIKTIGLKKPILVTPRVTAAGieKYLLVCGEGRLKAFRTLGEAtIPALVVHVSDEDAYVMSLTENIARRQCRPI 110
Cdd:PRK13866  90 FEQLEASISQEGQQVPILVRPHPEAAG--RYQIVYGRRRLRAAVNLRRE-VSAIVRNLTDRELVVAQGRENLDRADLSFI 166

                         90       100
                 ....*....|....*....|.
gi 759495860 111 ERLAGIRLLQEQGY-APKVIA 130
Cdd:PRK13866 167 EKALFALRLEDAGFdRATIIA 187
ParB_N_like cd16407
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
 33-96 1.42e-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: 319264 [Multi-domain]  Cd Length: 86  Bit Score: 39.81  E-value: 1.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759495860  33 EIVDNIKTIGLKKPILVTPRvtaaGIEKYLLVCGEGRLKAFRTLGEATIPALVVHVSDEDAYVM 96
Cdd:cd16407   22 ELVESIKENGVLTPIIVRPR----EDGGYEIISGHRRKRACELAGLETIPVIVREMDDDEAVIA 81
ParB_N_like_MT cd16402
ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent ...
 17-93 6.18e-04

ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent methyltransferase domain; This family represents domains related to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, fused to a variety of C-terminal domains, including S-adenosylmethionine-dependent methyltransferase-like domains and DUF4417. 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: 319259 [Multi-domain]  Cd Length: 87  Bit Score: 37.98  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  17 QIEVINPRERNGRVFNEIVD----NIKTIGLKKPILVTprvtaagiEKYLLVCGEGRLKAFRTLGEATIPALVV-HVSDE 91
Cdd:cd16402    1 KISELKPYENNPRNNDKAVEkvaeSIKEFGFLVPIVVD--------KNNVIVAGHTRYKAAKRLGLEEVPCIVAdDLTEE 72


                 ..
gi 759495860  92 DA 93
Cdd:cd16402   73 QI 74
SbnI_like_N cd16388
N-terminal domain of transcriptional regulators similar to SbnI; Siderophore staphylobactin ...
 10-90 6.38e-04

N-terminal domain of transcriptional regulators similar to SbnI; Siderophore staphylobactin biosynthesis protein SbnI of Staphylococcus aureus is a ParB/Spo0J like protein required for the expression of genes in the sbn operon, which is responsible for staphyloferrin B (SB) biosynthesis. SnbI forms dimers and binds DNA upstream of sdnD. SbnI binds heme, which inhibits DNA binding of SbnI, leading to a suppression of sbn operon expression.


Pssm-ID: 319247 [Multi-domain]  Cd Length: 77  Bit Score: 37.87  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759495860  10 IRMIPVSQIEVINPRERNgRVFNeIVDNIKTIG-LKKPILVTPrvtaAGIEKYLLVCGEGRLKAFRTLGEATIPALVVHV 88
Cdd:cd16388    1 LKLVPIEQIRLHEEHEPN-RLEK-LVERIEAEGvLRNPPIVTP----LQDGRYLILDGAHRTTALKKLGCKRIPVQVVDE 74


                 ..
gi 759495860  89 SD 90
Cdd:cd16388   75 ED 76
 
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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