hypothetical protein U926_02107 [Staphylococcus aureus 12S00881]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| staphy_B_SbnI | NF033589 | bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI; SbnI is a ... |
1-254 | 0e+00 | |||||
bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI; SbnI is a bifunctional protein involved in staphyloferrin B (staphylobactin) biosynthesis in Staphylococcus aureus and other members of the genus. It is a bifunctional protein. The N-terminal region is heme-binding, and loses the ability to bind DNA when heme is bound. Under low iron conditions, the biosynthesis operon for staphyloferrin B, a carboxylate-type siderophore, is derepressed. The C-terminal domain is a kinase that acts on free serine, producing O-phospho-L-serine, which is used as one of the precursors of staphyloferrin B. : Pssm-ID: 411211 Cd Length: 254 Bit Score: 516.62 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| staphy_B_SbnI | NF033589 | bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI; SbnI is a ... |
1-254 | 0e+00 | |||||
bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI; SbnI is a bifunctional protein involved in staphyloferrin B (staphylobactin) biosynthesis in Staphylococcus aureus and other members of the genus. It is a bifunctional protein. The N-terminal region is heme-binding, and loses the ability to bind DNA when heme is bound. Under low iron conditions, the biosynthesis operon for staphyloferrin B, a carboxylate-type siderophore, is derepressed. The C-terminal domain is a kinase that acts on free serine, producing O-phospho-L-serine, which is used as one of the precursors of staphyloferrin B. Pssm-ID: 411211 Cd Length: 254 Bit Score: 516.62 E-value: 0e+00
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| SbnI_like_N | cd16388 | N-terminal domain of transcriptional regulators similar to SbnI; Siderophore staphylobactin ... |
8-84 | 4.12e-39 | |||||
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: 130.70 E-value: 4.12e-39
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| Spo0J | COG1475 | Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ... |
6-76 | 1.22e-10 | |||||
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: 59.62 E-value: 1.22e-10
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| ParB | smart00470 | ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ... |
11-76 | 1.64e-08 | |||||
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: 50.77 E-value: 1.64e-08
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| ParBc | pfam02195 | ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ... |
9-76 | 2.66e-08 | |||||
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: 49.97 E-value: 2.66e-08
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| Name | Accession | Description | Interval | E-value | |||||
| staphy_B_SbnI | NF033589 | bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI; SbnI is a ... |
1-254 | 0e+00 | |||||
bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI; SbnI is a bifunctional protein involved in staphyloferrin B (staphylobactin) biosynthesis in Staphylococcus aureus and other members of the genus. It is a bifunctional protein. The N-terminal region is heme-binding, and loses the ability to bind DNA when heme is bound. Under low iron conditions, the biosynthesis operon for staphyloferrin B, a carboxylate-type siderophore, is derepressed. The C-terminal domain is a kinase that acts on free serine, producing O-phospho-L-serine, which is used as one of the precursors of staphyloferrin B. Pssm-ID: 411211 Cd Length: 254 Bit Score: 516.62 E-value: 0e+00
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| SbnI_like_N | cd16388 | N-terminal domain of transcriptional regulators similar to SbnI; Siderophore staphylobactin ... |
8-84 | 4.12e-39 | |||||
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: 130.70 E-value: 4.12e-39
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| ParB_Srx_like_nuclease | cd16400 | ParB/Srx_like nuclease and putative transcriptional regulators related to SbnI; This family ... |
10-76 | 1.90e-11 | |||||
ParB/Srx_like nuclease and putative transcriptional regulators related to SbnI; This family contains a Pyrococcus Furiosus enzyme reported to have DNA nuclease activity and resembles the N-terminal domain of ParB proteins of the parABS bacterial chromosome partitioning system. This sub-family also includes siderophore staphylobactin biosynthesis protein SbnI. 60% of the P. furiosus nuclease activity was retained at 90 degree C, suggesting a physiological role in the organism, which can grow in temperatures as high as 100 degrees Celsius. The protein has endo- and exo-nuclease activity vs. single- and double-stranded DNA, and nuclease activity was lost in methylated proteins prepared for structure solution. This family has a fairly well-conserved DGHHR motif that corresponds to the same structural position as the phosphorylation site (a portion of the ATP-Mg-binding site) of sulfiredoxin and the arginine-rich ParB BoxII of ParB. Pssm-ID: 319257 [Multi-domain] Cd Length: 72 Bit Score: 58.33 E-value: 1.90e-11
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| Spo0J | COG1475 | Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ... |
6-76 | 1.22e-10 | |||||
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: 59.62 E-value: 1.22e-10
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| ParB_N_Srx | cd16387 | ParB N-terminal domain and sulfiredoxin protein-related families; The ParB N-terminal domain ... |
27-76 | 3.00e-09 | |||||
ParB N-terminal domain and sulfiredoxin protein-related families; The ParB N-terminal domain/Sulfiredoxin (Srx) superfamily contains proteins with diverse activities. Many of the families are involved in segregation and competition between plasmids and chromosomes. Several families share similar activities with the N-terminal domain of ParB (Spo0J in Bacillus subtilis), a DNA-binding component of the prokaryotic parABS partitioning system. Also within this superfamily is sulfiredoxin (Srx; reactivator of oxidatively inactivated 2-cys peroxiredoxins), RepB N-terminal domain (plasmid segregation replication protein B like protein), nucleoid occlusion protein, KorB N-terminal domain partition protein of low copy number plasmid RK2, irbB (immunoglobulin-binding regulator that activates eib genes), N-terminal domain of sopB protein (promotes proper partitioning of F1 plasmid), fertility inhibition factors OSA and FiwA,DNA sulfur modification protein DndB, and a ParB-like toxin domain. Other activities includes a StrR (regulator in the streptomycin biosynthetic gene cluster), and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators sbnI (Staphylococcus aureus siderophore biosynthetic gene cluster ). Nuclease activity has also been reported in Arabidopsis Srx. Pssm-ID: 319246 [Multi-domain] Cd Length: 54 Bit Score: 51.82 E-value: 3.00e-09
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| ParB | smart00470 | ParB-like nuclease domain; Plasmid RK2 ParB preferentially cleaves single-stranded DNA. ParB ... |
11-76 | 1.64e-08 | |||||
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: 50.77 E-value: 1.64e-08
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| ParBc | pfam02195 | ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ... |
9-76 | 2.66e-08 | |||||
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: 49.97 E-value: 2.66e-08
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| pNOB8_ParB_N_like | cd16404 | pNOB8 ParB-like N-terminal domain, plasmid partitioning system protein domain; archaeal pNOB8 ... |
27-83 | 2.37e-05 | |||||
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: 41.49 E-value: 2.37e-05
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| ParB_N_like | cd16409 | ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems; This family ... |
31-75 | 5.09e-04 | |||||
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: 37.66 E-value: 5.09e-04
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| IbrB_like | cd16397 | immunoglobulin-binding regulator IbrB activates eib genes; IbrB (along with IbrA) activates ... |
7-67 | 6.99e-04 | |||||
immunoglobulin-binding regulator IbrB activates eib genes; IbrB (along with IbrA) activates immunoglobulin-binding eib genes in Escherichia coli. IbrB is related to the ParB N-terminal domain family, which includes DNA-binding proteins involved in chromosomal/plasmid segregation and transcriptional regulation, consistent with a possible mechanism for IbrB in DNA binding-related regulation of eib expression. The ParB like family is a diverse domain superfamily with structural and sequence similarity to ParB of bacterial chromosomes/plasmid parABS partitioning system and Sulfiredoxin (Srx), which is a reactivator of oxidatively inactivated 2-cys peroxiredoxins. Other families includes proteins related to StrR, a putative regulator in the biosynthetic gene cluster and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators SbnI (Staphylococcus aureus siderophore biosynthetic gene cluster ) and EdeB (Brevibacillus brevis antimicrobial peptide edeine biosynthetic cluster). Nuclease activity has also been reported in arabidopsis Srx. Pssm-ID: 319255 [Multi-domain] Cd Length: 100 Bit Score: 37.94 E-value: 6.99e-04
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| Noc_N | cd16396 | nucleoid occlusion protein, N-terminal domain, and related domains of the ParB partitioning ... |
42-75 | 2.61e-03 | |||||
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: 36.43 E-value: 2.61e-03
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| SPO0J_N | cd16393 | Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member; ... |
8-76 | 4.04e-03 | |||||
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: 35.92 E-value: 4.04e-03
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| ParB_N_like_MT | cd16403 | ParB N-terminal-like domain, some attached to C-terminal S-adenosylmethionine-dependent ... |
27-76 | 9.17e-03 | |||||
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: 34.35 E-value: 9.17e-03
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