Conserved Protein Domain Family
ParB_N_like_MT

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cd16401: ParB_N_like_MT 
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. 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.
Statistics
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PSSM-Id: 319258
View PSSM: cd16401
Aligned: 37 rows
Threshold Bit Score: 89.5872
Threshold Setting Gi: 530773457
Created: 4-Mar-2016
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
putative ParB
Feature 1:putative ParB Box II like motif [polypeptide binding site]
Evidence:
  • Comment:Motif identified in related ParB/Spo0J family proteins
  • Comment:partial match to Spo0J motif
  • Comment:Bacillus subtilis ParB Box II shown to be essential for DNA loop formation in vitro and Spo0J complex formation in vivo
  • Comment:Mutations in B. subtilis (R79A, R80A, R82A) incapacitate Spo0J spreading from parS sites
  • Comment:ParB box may interact with a negatively charged region of another Spo0J molecule
  • Citation:PMID 9915704

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                       # ## ##                          
gi 363613935  13 PAKYNPRkdlkPGDAEYEKLKRSIEQFGYVEPVIWNq---tTGNVVGGHQRLKVMEDMGTtEVDCVVVE-LDEAREKALN 88
gi 818331504  18 VATFNPRk---WDDAKKAKLRESIERFGLVDPLIVNsnparKNVLIGGHFRLLIARELGYkDVPVVYLDiPDIEKEKELN 94
gi 818588377  22 PSEYNPRs---WSKDAAGQLKESITRYGMVDPILVNsaperNGVLIGGHFRWAMAKELGItEVPVVYLNiPDLEKEKELN 98
gi 147887151  18 PALYNPRk---WSEEAIEQLTESVTRFGLVDPIIANgtpgrKNIVIGGHFRLKIAKDLGYqEVPVVYVDiADETKERELN 94
gi 818472080  18 PAEYNPRq---ASQKQIKHIRDSIRKFKMVEPIVVNgsperKNVIIGGHIRTKIWQELGHdTIPVHYID-LSLNDERELN 93
gi 818738960  18 PAVYNPRk---WDEKVLSDMKESISRFGLVDPLLVNgapdrRNIVIGGHLRLKIATLLGFtEIPVVYLHiPDIEREKELN 94
gi 818460841  16 FAEYNPRk---ITRSVIEQLKNSIKEFGMPVPIVINtykdrENVIIGGEKRVRAAIELGWkEVPCSTVN-LPLEKEKALN 91
gi 818369238  18 FAEYNPRk---WSSESKETLRKSLEENGFVDPVILNsaperMDVLIGGHFRVRQARELGYkEVPAIYLSiPDIEKEKKLN 94
gi 530768577   9 IKVNNPYl---RFNTNIDELKESIKTVGLINPIVINk----ENKLIAGGRRFSALKDLGWeEVPCIRVD-EEGLKEELIS 80
gi 524267475  12 PAPYNPRr---IEEQQIEQLKSSFNDIGFILPVLVNr---kNNVIIAGHQRTKTAKLCGItKIPVMYVDkIVLGDEIKFN 85

                 ....*....
Feature 1                 
gi 363613935  89 IALNKISGE 97
gi 818331504  95 LRLNKNVGE 103
gi 818588377  99 LRLNRNQGE 107
gi 147887151  95 LRLNRNLGE 103
gi 818472080  94 LRLNKNQAE 102
gi 818738960  95 LRLNKNVGA 103
gi 818460841  92 LALNKIEDQ 100
gi 818369238  95 LQLNRAIGE 103
gi 530768577  81 IDENLVRQN 89
gi 524267475  86 QLHNGIDKT 94

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