septum site-determining protein MinD [Proteus mirabilis]
Protein Classification
septum site-determining protein MinD( domain architecture ID 11484970)
septum site-determining protein MinD, one of the three protein products of the min operon, is a membrane ATPase required for proper placement of the cell division site at the midcell position through the activation and regulation of MinC and MinE
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK10818 | PRK10818 | septum site-determining protein MinD; |
1-270 | 0e+00 | |||||
septum site-determining protein MinD; : Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 554.93 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PRK10818 | PRK10818 | septum site-determining protein MinD; |
1-270 | 0e+00 | |||||
septum site-determining protein MinD; Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 554.93 E-value: 0e+00
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| MinD | COG2894 | Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
1-267 | 0e+00 | |||||
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 498.04 E-value: 0e+00
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| minD_bact | TIGR01968 | septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
2-269 | 2.41e-135 | |||||
septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division] Pssm-ID: 131023 [Multi-domain] Cd Length: 261 Bit Score: 382.46 E-value: 2.41e-135
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| MinD | cd02036 | septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
3-246 | 9.69e-132 | |||||
septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein. Pssm-ID: 349756 [Multi-domain] Cd Length: 236 Bit Score: 372.31 E-value: 9.69e-132
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| CbiA | pfam01656 | CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-227 | 8.66e-40 | |||||
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family. Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 137.86 E-value: 8.66e-40
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| ParA_partition | NF041546 | ParA family partition ATPase; |
4-182 | 8.70e-09 | |||||
ParA family partition ATPase; Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 54.10 E-value: 8.70e-09
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| ArsA_halo | NF041417 | arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
9-138 | 2.19e-04 | |||||
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms. Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 42.17 E-value: 2.19e-04
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| ArsA_halo | NF041417 | arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
6-40 | 5.13e-03 | |||||
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms. Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 37.94 E-value: 5.13e-03
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| Name | Accession | Description | Interval | E-value | |||||
| PRK10818 | PRK10818 | septum site-determining protein MinD; |
1-270 | 0e+00 | |||||
septum site-determining protein MinD; Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 554.93 E-value: 0e+00
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| MinD | COG2894 | Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
1-267 | 0e+00 | |||||
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 498.04 E-value: 0e+00
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| minD_bact | TIGR01968 | septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
2-269 | 2.41e-135 | |||||
septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division] Pssm-ID: 131023 [Multi-domain] Cd Length: 261 Bit Score: 382.46 E-value: 2.41e-135
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| MinD | cd02036 | septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
3-246 | 9.69e-132 | |||||
septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein. Pssm-ID: 349756 [Multi-domain] Cd Length: 236 Bit Score: 372.31 E-value: 9.69e-132
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| minD | CHL00175 | septum-site determining protein; Validated |
1-268 | 8.34e-89 | |||||
septum-site determining protein; Validated Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 265.10 E-value: 8.34e-89
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| minD_arch | TIGR01969 | cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
3-268 | 8.00e-46 | |||||
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown. Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 154.12 E-value: 8.00e-46
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| CbiA | pfam01656 | CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-227 | 8.66e-40 | |||||
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family. Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 137.86 E-value: 8.66e-40
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| CpaE | COG4963 | Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
2-267 | 5.33e-38 | |||||
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 136.78 E-value: 5.33e-38
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| ParA | COG1192 | ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
2-247 | 9.66e-36 | |||||
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility]; Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 128.05 E-value: 9.66e-36
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| FlhG | COG0455 | MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
18-252 | 1.39e-35 | |||||
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility]; Pssm-ID: 440223 [Multi-domain] Cd Length: 230 Bit Score: 126.93 E-value: 1.39e-35
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| FlhG-like | cd02038 | MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
3-229 | 1.47e-29 | |||||
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly. Pssm-ID: 349758 [Multi-domain] Cd Length: 230 Bit Score: 111.12 E-value: 1.47e-29
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| Mrp | COG0489 | Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
2-162 | 3.68e-24 | |||||
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 98.34 E-value: 3.68e-24
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| CpaE-like | cd03111 | pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
3-235 | 2.61e-22 | |||||
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome. Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 91.96 E-value: 2.61e-22
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| AAA_31 | pfam13614 | AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
2-146 | 8.13e-18 | |||||
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop. Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 78.78 E-value: 8.13e-18
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| BY-kinase | cd05387 | bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
2-160 | 3.53e-16 | |||||
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity. Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 74.53 E-value: 3.53e-16
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| ParAB_family | cd02042 | partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
3-194 | 4.38e-16 | |||||
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition. Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 72.57 E-value: 4.38e-16
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| CooC | COG3640 | CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
4-238 | 3.67e-14 | |||||
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 70.20 E-value: 3.67e-14
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| eps_fam | TIGR01007 | capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
3-122 | 3.69e-11 | |||||
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 60.91 E-value: 3.69e-11
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| cellulose_yhjQ | TIGR03371 | cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
1-228 | 4.23e-11 | |||||
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 274549 [Multi-domain] Cd Length: 246 Bit Score: 61.59 E-value: 4.23e-11
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| ArsA | COG0003 | Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
1-53 | 2.90e-10 | |||||
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; Pssm-ID: 439774 Cd Length: 299 Bit Score: 59.45 E-value: 2.90e-10
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| ParA | pfam10609 | NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
3-247 | 1.03e-09 | |||||
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits. Pssm-ID: 431392 [Multi-domain] Cd Length: 246 Bit Score: 57.46 E-value: 1.03e-09
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| TadZ-like | cd17869 | pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ... |
3-144 | 1.11e-09 | |||||
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. Pssm-ID: 349778 [Multi-domain] Cd Length: 219 Bit Score: 57.16 E-value: 1.11e-09
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| Mrp_NBP35 | cd02037 | Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
3-59 | 2.33e-09 | |||||
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase. Pssm-ID: 349757 [Multi-domain] Cd Length: 213 Bit Score: 55.97 E-value: 2.33e-09
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| SIMIBI | cd01983 | SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
3-164 | 2.36e-09 | |||||
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 53.59 E-value: 2.36e-09
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| ArsA | cd02035 | Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
3-53 | 2.65e-09 | |||||
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence. Pssm-ID: 349755 [Multi-domain] Cd Length: 250 Bit Score: 56.36 E-value: 2.65e-09
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| ParA_partition | NF041546 | ParA family partition ATPase; |
4-182 | 8.70e-09 | |||||
ParA family partition ATPase; Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 54.10 E-value: 8.70e-09
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| ArsA_ATPase | pfam02374 | Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
3-40 | 4.02e-08 | |||||
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell. Pssm-ID: 396792 Cd Length: 302 Bit Score: 53.12 E-value: 4.02e-08
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| SIMIBI_bact_arch | cd03110 | bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
4-212 | 7.91e-08 | |||||
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown. Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 52.00 E-value: 7.91e-08
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| CooC1 | cd02034 | accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
3-246 | 9.71e-08 | |||||
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function. Pssm-ID: 349754 [Multi-domain] Cd Length: 249 Bit Score: 51.54 E-value: 9.71e-08
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| PRK13869 | PRK13869 | plasmid-partitioning protein RepA; Provisional |
3-185 | 7.93e-07 | |||||
plasmid-partitioning protein RepA; Provisional Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 49.67 E-value: 7.93e-07
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| MipZ | pfam09140 | ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
3-137 | 1.25e-06 | |||||
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation. Pssm-ID: 401181 [Multi-domain] Cd Length: 262 Bit Score: 48.60 E-value: 1.25e-06
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| arsen_driv_ArsA | TIGR04291 | arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
5-33 | 1.78e-06 | |||||
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite). Pssm-ID: 275109 [Multi-domain] Cd Length: 566 Bit Score: 48.55 E-value: 1.78e-06
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| PRK11670 | PRK11670 | iron-sulfur cluster carrier protein ApbC; |
4-41 | 2.89e-06 | |||||
iron-sulfur cluster carrier protein ApbC; Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 47.73 E-value: 2.89e-06
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| partition_RepA | TIGR03453 | plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
4-200 | 1.32e-05 | |||||
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions] Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 45.74 E-value: 1.32e-05
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| PHA02518 | PHA02518 | ParA-like protein; Provisional |
3-40 | 1.08e-04 | |||||
ParA-like protein; Provisional Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 42.14 E-value: 1.08e-04
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| ArsA_halo | NF041417 | arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
9-138 | 2.19e-04 | |||||
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms. Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 42.17 E-value: 2.19e-04
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| PRK13886 | PRK13886 | conjugal transfer protein TraL; Provisional |
1-40 | 4.70e-04 | |||||
conjugal transfer protein TraL; Provisional Pssm-ID: 184370 Cd Length: 241 Bit Score: 40.48 E-value: 4.70e-04
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| chlL | PRK13185 | protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional |
1-40 | 5.20e-04 | |||||
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional Pssm-ID: 237293 Cd Length: 270 Bit Score: 40.72 E-value: 5.20e-04
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| arsen_driv_ArsA | TIGR04291 | arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
9-40 | 2.19e-03 | |||||
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite). Pssm-ID: 275109 [Multi-domain] Cd Length: 566 Bit Score: 39.30 E-value: 2.19e-03
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| chlL | CHL00072 | photochlorophyllide reductase subunit L |
10-40 | 4.07e-03 | |||||
photochlorophyllide reductase subunit L Pssm-ID: 177011 Cd Length: 290 Bit Score: 37.79 E-value: 4.07e-03
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| ArsA_halo | NF041417 | arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
6-40 | 5.13e-03 | |||||
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms. Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 37.94 E-value: 5.13e-03
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| NifH | cd02040 | nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
10-37 | 6.80e-03 | |||||
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia. Pssm-ID: 349759 Cd Length: 265 Bit Score: 37.11 E-value: 6.80e-03
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| Bchl-like | cd02032 | L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ... |
10-40 | 8.81e-03 | |||||
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen. Pssm-ID: 349752 Cd Length: 267 Bit Score: 36.89 E-value: 8.81e-03
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