MULTISPECIES: TerB N-terminal domain-containing protein [Pseudomonas syringae group]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
TerB_N | pfam13208 | TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing ... |
140-342 | 8.81e-86 | ||||
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: 271.54 E-value: 8.81e-86
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TerB_C | pfam15615 | TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ... |
679-833 | 3.86e-46 | ||||
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: 161.76 E-value: 3.86e-46
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terB | cd07176 | tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ... |
540-647 | 3.40e-22 | ||||
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: 92.29 E-value: 3.40e-22
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Phage_holin_3_6 | pfam07332 | Putative Actinobacterial Holin-X, holin superfamily III; Phage_holin_3_6 is a family of small ... |
10-62 | 2.88e-03 | ||||
Putative Actinobacterial Holin-X, holin superfamily III; Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion. : Pssm-ID: 462148 Cd Length: 113 Bit Score: 38.28 E-value: 2.88e-03
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Name | Accession | Description | Interval | E-value | ||||
TerB_N | pfam13208 | TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing ... |
140-342 | 8.81e-86 | ||||
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: 271.54 E-value: 8.81e-86
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TerB_C | pfam15615 | TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ... |
679-833 | 3.86e-46 | ||||
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: 161.76 E-value: 3.86e-46
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terB | cd07176 | tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ... |
540-647 | 3.40e-22 | ||||
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: 92.29 E-value: 3.40e-22
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TerB | COG3793 | Tellurite resistance protein TerB [Inorganic ion transport and metabolism]; |
525-648 | 8.73e-13 | ||||
Tellurite resistance protein TerB [Inorganic ion transport and metabolism]; Pssm-ID: 443007 [Multi-domain] Cd Length: 128 Bit Score: 65.77 E-value: 8.73e-13
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TerB | pfam05099 | Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins ... |
551-648 | 7.82e-05 | ||||
Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins from a a number of bacteria. Pssm-ID: 428302 Cd Length: 118 Bit Score: 42.94 E-value: 7.82e-05
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Phage_holin_3_6 | pfam07332 | Putative Actinobacterial Holin-X, holin superfamily III; Phage_holin_3_6 is a family of small ... |
10-62 | 2.88e-03 | ||||
Putative Actinobacterial Holin-X, holin superfamily III; Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion. Pssm-ID: 462148 Cd Length: 113 Bit Score: 38.28 E-value: 2.88e-03
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Name | Accession | Description | Interval | E-value | ||||
TerB_N | pfam13208 | TerB N-terminal domain; The TerB_N domain is found N-terminal to TerB, and TerB_C containing ... |
140-342 | 8.81e-86 | ||||
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: 271.54 E-value: 8.81e-86
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TerB_C | pfam15615 | TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ... |
679-833 | 3.86e-46 | ||||
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: 161.76 E-value: 3.86e-46
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terB | cd07176 | tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ... |
540-647 | 3.40e-22 | ||||
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: 92.29 E-value: 3.40e-22
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terB_like | cd07177 | tellurium resistance terB-like protein; This family consists of tellurium resistance terB ... |
547-645 | 2.04e-15 | ||||
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: 72.78 E-value: 2.04e-15
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TerB | COG3793 | Tellurite resistance protein TerB [Inorganic ion transport and metabolism]; |
525-648 | 8.73e-13 | ||||
Tellurite resistance protein TerB [Inorganic ion transport and metabolism]; Pssm-ID: 443007 [Multi-domain] Cd Length: 128 Bit Score: 65.77 E-value: 8.73e-13
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TerB | pfam05099 | Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins ... |
551-648 | 7.82e-05 | ||||
Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins from a a number of bacteria. Pssm-ID: 428302 Cd Length: 118 Bit Score: 42.94 E-value: 7.82e-05
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TerB2 | COG4103 | Tellurite resistance protein TerB [Inorganic ion transport and metabolism]; |
523-653 | 3.29e-04 | ||||
Tellurite resistance protein TerB [Inorganic ion transport and metabolism]; Pssm-ID: 443279 Cd Length: 149 Bit Score: 41.77 E-value: 3.29e-04
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Phage_holin_3_6 | pfam07332 | Putative Actinobacterial Holin-X, holin superfamily III; Phage_holin_3_6 is a family of small ... |
10-62 | 2.88e-03 | ||||
Putative Actinobacterial Holin-X, holin superfamily III; Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion. Pssm-ID: 462148 Cd Length: 113 Bit Score: 38.28 E-value: 2.88e-03
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terB_like_DjlA | cd07316 | N-terminal tellurium resistance protein terB-like domain of heat shock DnaJ-like proteins; ... |
547-641 | 3.46e-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: 37.89 E-value: 3.46e-03
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Blast search parameters | ||||
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