TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing ...
83-283
2.14e-51
TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing proteins. It has a predominantly alpha-helical structure and contains an absolutely conserved glutamate. The presence of a conserved acidic residue suggests that it might chelate metal like TerB. These proteins occur in a two-gene operon containing an AAA+ ATPase and SF-II DNA helicase suggesting a role in stress-response or phage defence.
:
Pssm-ID: 433039 Cd Length: 204 Bit Score: 177.93 E-value: 2.14e-51
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ...
629-746
3.19e-28
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain displays multiple conserved acidic residues (TerBC). The presence of conserved acidic residues in both TerB-N and TerB-C suggests that they, like the TerB domain, might also chelate metals. These two domains may also occur together in the same protein independently of TerB.
:
Pssm-ID: 434814 [Multi-domain] Cd Length: 143 Bit Score: 110.53 E-value: 3.19e-28
TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing ...
83-283
2.14e-51
TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing proteins. It has a predominantly alpha-helical structure and contains an absolutely conserved glutamate. The presence of a conserved acidic residue suggests that it might chelate metal like TerB. These proteins occur in a two-gene operon containing an AAA+ ATPase and SF-II DNA helicase suggesting a role in stress-response or phage defence.
Pssm-ID: 433039 Cd Length: 204 Bit Score: 177.93 E-value: 2.14e-51
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ...
629-746
3.19e-28
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain displays multiple conserved acidic residues (TerBC). The presence of conserved acidic residues in both TerB-N and TerB-C suggests that they, like the TerB domain, might also chelate metals. These two domains may also occur together in the same protein independently of TerB.
Pssm-ID: 434814 [Multi-domain] Cd Length: 143 Bit Score: 110.53 E-value: 3.19e-28
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ...
487-593
3.20e-21
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins involved in tellurium resistance. The prototype of this CD is the Kp-terB protein from Klebsiella pneumoniae, whose 3D structure was recently determined. The biological function of terB and the mechanism responsible for tellurium resistance are unknown.
Pssm-ID: 143580 Cd Length: 111 Bit Score: 89.20 E-value: 3.20e-21
TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing ...
83-283
2.14e-51
TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing proteins. It has a predominantly alpha-helical structure and contains an absolutely conserved glutamate. The presence of a conserved acidic residue suggests that it might chelate metal like TerB. These proteins occur in a two-gene operon containing an AAA+ ATPase and SF-II DNA helicase suggesting a role in stress-response or phage defence.
Pssm-ID: 433039 Cd Length: 204 Bit Score: 177.93 E-value: 2.14e-51
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ...
629-746
3.19e-28
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain displays multiple conserved acidic residues (TerBC). The presence of conserved acidic residues in both TerB-N and TerB-C suggests that they, like the TerB domain, might also chelate metals. These two domains may also occur together in the same protein independently of TerB.
Pssm-ID: 434814 [Multi-domain] Cd Length: 143 Bit Score: 110.53 E-value: 3.19e-28
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ...
487-593
3.20e-21
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins involved in tellurium resistance. The prototype of this CD is the Kp-terB protein from Klebsiella pneumoniae, whose 3D structure was recently determined. The biological function of terB and the mechanism responsible for tellurium resistance are unknown.
Pssm-ID: 143580 Cd Length: 111 Bit Score: 89.20 E-value: 3.20e-21
tellurium resistance terB-like protein; This family consists of tellurium resistance terB ...
490-591
1.82e-13
tellurium resistance terB-like protein; This family consists of tellurium resistance terB proteins, N-terminal domain of heat shock DnaJ-like proteins, N-terminal domain of Mo-dependent nitrogenase-like proteins, C-terminal domain of ABC transporter ATP-binding proteins, C-terminal domain of serine/threonine protein kinase, and many hypothetical bacterial proteins. The function of this family is unknown.
Pssm-ID: 143581 [Multi-domain] Cd Length: 104 Bit Score: 67.00 E-value: 1.82e-13
N-terminal tellurium resistance protein terB-like domain of heat shock DnaJ-like proteins; ...
490-592
6.12e-03
N-terminal tellurium resistance protein terB-like domain of heat shock DnaJ-like proteins; Tellurium resistance terB-like domain of the DnaJ-like DjlA proteins. This family represents the terB-like domain of DjlA-like proteins, a subgroup of heat shock DnaJ-like proteins. Escherichia coli DjlA is a type III membrane protein with a small N-terminal transmembrane region and DnaJ-like domain on the extreme C-terminus. Overproduction has been shown to activate the RcsC pathway, which regulates the production of the capsular exopolysaccharide colanic acid. The specific function of this domain is unknown.
Pssm-ID: 143585 Cd Length: 106 Bit Score: 37.12 E-value: 6.12e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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