| CP035375.1|QAV69192.1|266856_268392_-|DHA2-family-efflux-MFS-transporter-permease-subunit |
gnl|CDD|129794 |
TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].
|
5.76601e-82 |
| CP035375.1|QAV69198.1|274285_274750_-|single-stranded-DNA-binding-protein |
gnl|CDD|239942 |
cd04496, SSB_OBF, SSB_OBF: A subfamily of OB folds similar to the OB fold of ssDNA-binding protein (SSB). SSBs bind with high affinity to ssDNA. They bind to and protect ssDNA intermediates during DNA metabolic pathways. All bacterial and eukaryotic SSBs studied to date oligomerize to bring together four OB folds in their active state. The majority (e.g. Escherichia coli SSB) have a single OB fold per monomer, which oligomerize to form a homotetramer. However, Deinococcus and Thermus SSB proteins have two OB folds per monomer, which oligomerize to form a homodimer. Mycobacterium tuberculosis SSB varies in quaternary structure from E. coli SSB. It forms a dimer of dimers having a unique dimer interface, which lends the protein greater stability. Included in this group are OB folds similar to Escherichia coli PriB. E.coli PriB is homodimeric with each monomer having a single OB fold. It does not appear to form higher order oligomers. PriB is an essential protein for the replication restart at forks that have stalled at sites of DNA damage. It also plays a role in the assembly of primosome during replication initiation at the bacteriophage phiX174 origin. PriB physically interacts with SSB and binds ssDNA with high affinity.
|
6.94806e-16 |
| CP035375.1|QAV69203.1|281097_281853_+|protein-phosphatase-2C-domain-containing-protein |
gnl|CDD|379325 |
pfam13672, PP2C_2, Protein phosphatase 2C. Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.
|
8.60541e-41 |
| CP035375.1|QAV69188.1|262687_263461_+|rRNA-pseudouridine-synthase |
gnl|CDD|224108 |
COG1187, RsuA, 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthases [Translation, ribosomal structure and biogenesis].
|
9.7405e-83 |
| CP035375.1|QAV69191.1|265225_266746_+|ribosome-biogenesis-GTPase-Der |
gnl|CDD|179525 |
PRK03003, PRK03003, GTP-binding protein Der; Reviewed.
|
0 |
| CP035375.1|QAV69186.1|261206_262073_+|segregation/condensation-protein-A |
gnl|CDD|224273 |
COG1354, scpA, Rec8/ScpA/Scc1-like protein (kleisin family) [Replication, recombination, and repair].
|
5.44332e-46 |
| CP035375.1|QAV69194.1|269558_270275_+|thiamine-phosphate-synthase |
gnl|CDD|234590 |
PRK00043, thiE, thiamine phosphate synthase.
|
7.83959e-66 |
| CP035375.1|QAV69202.1|280416_281097_+|VWA-domain-containing-protein |
gnl|CDD|238741 |
cd01464, vWA_subfamily, VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.
|
2.30215e-53 |
| CP035375.1|QAV69187.1|262062_262701_+|SMC-Scp-complex-subunit-ScpB |
gnl|CDD|377219 |
pfam04079, SMC_ScpB, Segregation and condensation complex subunit ScpB. This is a family of prokaryotic proteins that form one of the subunits, ScpB, of the segregation and condensation complex, condensin, that plays a key role in the maintenance of the chromosome. In prokaryotes the complex consists of three proteins, SMC, ScpA (kleisin) and ScpB. ScpB dimerizes and binds to ScpA. As originally predicted, ScpB is structurally a winged-helix at both its N- and C-terminal halves. IN Bacillus subtilis,one Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complex ring-shaped assemblies.
|
3.865e-50 |
| CP035375.1|QAV69204.1|281881_283390_-|ATP-binding-protein |
gnl|CDD|225982 |
COG3451, VirB4, Type IV secretory pathway, VirB4 components [Intracellular trafficking and secretion].
|
1.23954e-10 |
| CP035375.1|QAV69196.1|272275_273508_-|site-specific-integrase |
gnl|CDD|271189 |
cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.
|
1.04116e-28 |
| CP035375.1|QAV69190.1|264536_265211_+|(d)CMP-kinase |
gnl|CDD|236546 |
PRK09518, PRK09518, bifunctional cytidylate kinase/GTPase Der; Reviewed.
|
5.40152e-64 |
| CP035375.1|QAV69197.1|273491_273710_-|DNA-binding-protein |
gnl|CDD|378935 |
pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.
|
3.67679e-09 |
| CP035375.1|QAV69199.1|274832_276614_-|type-VI-secretion-protein |
gnl|CDD|378923 |
pfam12696, TraG-D_C, TraM recognition site of TraD and TraG. This family includes both TraG and TraD as well as VirD4 proteins. TraG is essential for DNA transfer in bacterial conjugation. These proteins are thought to mediate interactions between the DNA-processing (Dtr) and the mating pair formation (Mpf) systems. This domain interacts with the relaxosome component TraM via the latter's tetramerisation domain. TraD is a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore.
|
1.3359e-30 |
| CP035375.1|QAV69189.1|263457_264540_+|prephenate-dehydrogenase |
gnl|CDD|235824 |
PRK06545, PRK06545, prephenate dehydrogenase; Validated.
|
9.45429e-117 |
| CP035375.1|QAV69195.1|270271_271837_+|bifunctional-hydroxymethylpyrimidine-kinase/phosphomethylpyrimidine-kinase |
gnl|CDD|237797 |
PRK14713, PRK14713, bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase.
|
0 |
| CP035375.1|QAV69193.1|268752_269562_+|hydroxyethylthiazole-kinase |
gnl|CDD|236477 |
PRK09355, PRK09355, hydroxyethylthiazole kinase; Validated.
|
3.41137e-102 |
| CP035375.1|QAV69201.1|277289_277718_+|DNA-binding-protein |
gnl|CDD|378935 |
pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.
|
1.94045e-12 |
