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Conserved domains on  [gi|18397831|ref|NP_564375|]
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sulfiredoxin [Arabidopsis thaliana]

Protein Classification

sulfiredoxin( domain architecture ID 11611623)

sulfiredoxin reduces and thereby reactivates peroxiredoxins after oxidative inactivation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Srx cd16395
Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and ...
 40-124 4.16e-41

Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems.


:

Pssm-ID: 319253 [Multi-domain]  Cd Length: 90  Bit Score: 131.20  E-value: 4.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLMRtrSNDQNKVKELMDSIRQI--GLQVPIDVIEV----DGTYYGFSGCHRYEAHQKLGLPTIRCKIR 113
Cdd:cd16395   1 VHEVPLSVIRRPLPP--VLDENKVQSLMETIKGIapGLLPPIDVLWVkgegGGYYYSFGGCHRYEAHKRLGRETIRCKII 78

                        90
                ....*....|.
gi 18397831 114 KGTKETLRHHL 124
Cdd:cd16395  79 KSTPSDLRVYL 89
 
Name Accession Description Interval E-value
Srx cd16395
Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and ...
 40-124 4.16e-41

Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems.


Pssm-ID: 319253 [Multi-domain]  Cd Length: 90  Bit Score: 131.20  E-value: 4.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLMRtrSNDQNKVKELMDSIRQI--GLQVPIDVIEV----DGTYYGFSGCHRYEAHQKLGLPTIRCKIR 113
Cdd:cd16395   1 VHEVPLSVIRRPLPP--VLDENKVQSLMETIKGIapGLLPPIDVLWVkgegGGYYYSFGGCHRYEAHKRLGRETIRCKII 78

                        90
                ....*....|.
gi 18397831 114 KGTKETLRHHL 124
Cdd:cd16395  79 KSTPSDLRVYL 89
COG5119 COG5119
Uncharacterized conserved protein, contains ParB-like nuclease domain [General function ...
 40-124 6.80e-39

Uncharacterized conserved protein, contains ParB-like nuclease domain [General function prediction only];


Pssm-ID: 444055  Cd Length: 87  Bit Score: 125.62  E-value: 6.80e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLmrTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTKET 119
Cdd:COG5119   4 IKEIPLNQIRRPL--PRQTDPQKVAALMESIAEEGLQEPIDVLEVDGQYYGFSGCHRYEACQRLGKETIRCRVRRAPRSV 81


                ....*
gi 18397831 120 LRHHL 124
Cdd:COG5119  82 LQKHL 86
ParB smart00470
ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ...
 41-121 1.56e-23

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: 86.59  E-value: 1.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831     41 VELPLEKIRRPLMRTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTKETL 120
Cdd:smart00470   1 VEVPIEKLRPNPDQPRLTSEESLEELAESIKENGLLQPIIVRPNDGRYEIIDGERRLRAAKLLGLKEVPVIVRDLDDEEA 80


                   .
gi 18397831    121 R 121
Cdd:smart00470  81 I 81
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
 41-120 1.39e-15

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: 66.53  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831    41 VELPLEKIRRPLMRTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYG-FSGCHRYEAHQKLGLPTIRCKIRKGTKET 119
Cdd:pfam02195   1 EEVPISKLRPNPDQPRKDSEESLEELAASIKKRGLLQPIIVRKTPDGRYEiIAGERRLRAAKLLGLKEVPVIVREIDDEE 80


                  .
gi 18397831   120 L 120
Cdd:pfam02195  81 A 81
 
Name Accession Description Interval E-value
Srx cd16395
Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and ...
 40-124 4.16e-41

Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems.


Pssm-ID: 319253 [Multi-domain]  Cd Length: 90  Bit Score: 131.20  E-value: 4.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLMRtrSNDQNKVKELMDSIRQI--GLQVPIDVIEV----DGTYYGFSGCHRYEAHQKLGLPTIRCKIR 113
Cdd:cd16395   1 VHEVPLSVIRRPLPP--VLDENKVQSLMETIKGIapGLLPPIDVLWVkgegGGYYYSFGGCHRYEAHKRLGRETIRCKII 78

                        90
                ....*....|.
gi 18397831 114 KGTKETLRHHL 124
Cdd:cd16395  79 KSTPSDLRVYL 89
COG5119 COG5119
Uncharacterized conserved protein, contains ParB-like nuclease domain [General function ...
 40-124 6.80e-39

Uncharacterized conserved protein, contains ParB-like nuclease domain [General function prediction only];


Pssm-ID: 444055  Cd Length: 87  Bit Score: 125.62  E-value: 6.80e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLmrTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTKET 119
Cdd:COG5119   4 IKEIPLNQIRRPL--PRQTDPQKVAALMESIAEEGLQEPIDVLEVDGQYYGFSGCHRYEACQRLGKETIRCRVRRAPRSV 81


                ....*
gi 18397831 120 LRHHL 124
Cdd:COG5119  82 LQKHL 86
ParB smart00470
ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ...
 41-121 1.56e-23

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: 86.59  E-value: 1.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831     41 VELPLEKIRRPLMRTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTKETL 120
Cdd:smart00470   1 VEVPIEKLRPNPDQPRLTSEESLEELAESIKENGLLQPIIVRPNDGRYEIIDGERRLRAAKLLGLKEVPVIVRDLDDEEA 80


                   .
gi 18397831    121 R 121
Cdd:smart00470  81 I 81
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
 41-120 1.39e-15

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: 66.53  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831    41 VELPLEKIRRPLMRTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYG-FSGCHRYEAHQKLGLPTIRCKIRKGTKET 119
Cdd:pfam02195   1 EEVPISKLRPNPDQPRKDSEESLEELAASIKKRGLLQPIIVRKTPDGRYEiIAGERRLRAAKLLGLKEVPVIVREIDDEE 80


                  .
gi 18397831   120 L 120
Cdd:pfam02195  81 A 81
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
 40-121 1.77e-12

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: 61.54  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLMRTRSN-DQNKVKELMDSIRQIGLQVPIDVIEVDGTYYG-FSGCHRYEAHQKLGLPTIRCKIRKGTK 117
Cdd:COG1475   7 IREIPIDKIVPSPYNPRRTfDEEALEELAASIREHGLLQPILVRPLGDGRYEiIAGERRLRAAKLLGLETVPAIVRDLDD 86


                ....
gi 18397831 118 ETLR 121
Cdd:COG1475  87 EEAL 90
ParB_N_like cd16409
ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems; This family ...
 59-114 1.96e-11

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: 55.38  E-value: 1.96e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18397831  59 DQNKVKELMDSIRQIGLQVPIDVIEV-DGTYYGFSGCHRYEAHQKLGLPTIRCKIRK 114
Cdd:cd16409   2 DPEHVEALAQSIAEHGLLTPITVRQDpGGRYTLIAGAHRLAAAKLLGWDTIDAIIVK 58
ParB_N_Srx cd16387
ParB N-terminal domain and sulfiredoxin protein-related families; The ParB N-terminal domain ...
 59-110 1.84e-10

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: 52.59  E-value: 1.84e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18397831  59 DQNKVKELMDSIRQIGLQVPIDVIEV-DGTYYGFSGCHRYEAHQKLGLPTIRC 110
Cdd:cd16387   1 DEEELEELAESIREHGVLQPIIVRPLpDGRYEIIAGERRWRAAKLAGLTTIPV 53
SPO0J_N cd16393
Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member; ...
 40-121 4.59e-10

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: 52.49  E-value: 4.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLMRTRSN-DQNKVKELMDSIRQIGLQVPIDVIEV-DGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTK 117
Cdd:cd16393   1 VQEIPIDKIRPNPYQPRKEfDEEALKELAESIKEHGLLQPIVVRKVgDGRYEIIAGERRWRAAKLAGLTEIPAIVRDLDD 80


                ....
gi 18397831 118 ETLR 121
Cdd:cd16393  81 EEAL 84
Noc_N cd16396
nucleoid occlusion protein, N-terminal domain, and related domains of the ParB partitioning ...
 40-121 1.65e-07

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: 45.68  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  40 IVELPLEKIRRPLMRTRSN-DQNKVKELMDSIRQIGLQVPIDVIE-VDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTK 117
Cdd:cd16396   3 VLEIPVADIIPNPYQPRKEfDEEEIEELAESIKEHGLLQPIVVRKtKDGGYEIVAGERRWRAAKLLGWEKIPAIIRDLSD 82


                ....
gi 18397831 118 ETLR 121
Cdd:cd16396  83 KEAL 86
ParB_N_like_MT cd16402
ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent ...
 44-121 4.77e-06

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: 41.83  E-value: 4.77e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18397831  44 PLEKIRrPLMRTRSNDQNKVKELMDSIRQIGLQVPIdVIEVDGTYygFSGCHRYEAHQKLGLPTIRCKIRKG-TKETLR 121
Cdd:cd16402   1 KISELK-PYENNPRNNDKAVEKVAESIKEFGFLVPI-VVDKNNVI--VAGHTRYKAAKRLGLEEVPCIVADDlTEEQIK 75
ParB_N_like cd16408
ParB N-terminal, parA -binding, -like domain of bacterial and plasmid parABS partitioning ...
 62-115 6.11e-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: 319265 [Multi-domain]  Cd Length: 84  Bit Score: 41.46  E-value: 6.11e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18397831  62 KVKELMDSIRQIGLQVPIDVIEV-DGTYYGFSGCHRYEAHQKLGLPTIRCKIRKG 115
Cdd:cd16408  16 RLEDMVESIKENGVLQPIIVRPIeDGKYEILAGHNRVNAAKLAGLTTIPAIIKEN 70
ParB_N_like cd16407
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
 65-113 2.35e-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: 37.11  E-value: 2.35e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18397831  65 ELMDSIRQIGLQVPIDVIEVDGTYYGF-SGCHRYEAHQKLGLPTIRCKIR 113
Cdd:cd16407  22 ELVESIKENGVLTPIIVRPREDGGYEIiSGHRRKRACELAGLETIPVIVR 71
ParB_N_like_MT cd16403
ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent ...
 44-115 4.81e-04

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: 36.67  E-value: 4.81e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18397831  44 PLEKIRRPLMRTRSNDQNKVKELMDSIRQIGLQVPIdVIEVDGTYygFSGCHRYEAHQKLGLPTIRCKIRKG 115
Cdd:cd16403   1 PIDDLKPYPRNARTHSEKQIEQLAASIREFGFTNPI-LVDEDGVI--IAGHGRLLAAKLLGLKEVPVIRLDH 69
pNOB8_ParB_N_like cd16404
pNOB8 ParB-like N-terminal domain, plasmid partitioning system protein domain; archaeal pNOB8 ...
 59-118 9.60e-04

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: 35.33  E-value: 9.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397831  59 DQNKVKELMDSIRQIGLQVPIDvieVDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTKE 118
Cdd:cd16404  13 TNEEFEELKESIRKNGIIVPII---VDQDGVIIDGHHRYRIAKELGIKEVPVIVYDFDDE 69
ParB_N_like cd16410
ParB N-terminal, parA-binding, -like domain of bacterial and plasmid parABS partitioning ...
 63-112 1.32e-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: 35.25  E-value: 1.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18397831  63 VKELMDSIRQIGLQVPIdVIEVDGTYygFSGCHRYEAHQKLGLPTIRCKI 112
Cdd:cd16410  17 IEALAESIKRHGLLNPI-VVTPDNEL--IAGERRLEAAKLLGWETIEVRV 63
KorB_N_like cd16398
ParB-like partition protein of low copy number plasmid RK2, N-terminal domain and related ...
 59-108 1.63e-03

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: 35.32  E-value: 1.63e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18397831  59 DQNKVKELMDSIRQIGLQVPIDVI---EVDGTYYGFSGCHRYEAHQKLGLPTI 108
Cdd:cd16398  16 DEEKIEELAASIKERGVKSPISVRphpEKPGKYIINHGARRYRASKWAGLKTI 68
 
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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