RecName: Full=UPF0045 protein CPE1503
MTH1187 family thiamine-binding protein( domain architecture ID 10000254)
MTH1187 family thiamine-binding protein may play a role in protein-protein interactions; similar to Staphylococcus xylosus UPF0045 protein in glkA 3'region
List of domain hits
Name | Accession | Description | Interval | E-value | |||
YqgV | COG0011 | Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and ... |
4-95 | 5.33e-34 | |||
Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and metabolism]; : Pssm-ID: 439782 Cd Length: 98 Bit Score: 112.12 E-value: 5.33e-34
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Name | Accession | Description | Interval | E-value | |||
YqgV | COG0011 | Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and ... |
4-95 | 5.33e-34 | |||
Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and metabolism]; Pssm-ID: 439782 Cd Length: 98 Bit Score: 112.12 E-value: 5.33e-34
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Thiamine_BP | pfam01910 | Thiamine-binding protein; The crystal structure of two of these members shows that this domain ... |
6-95 | 2.63e-30 | |||
Thiamine-binding protein; The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6, shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative conditions this bacterium is under stress, and the transcriiptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family. Pssm-ID: 426506 Cd Length: 92 Bit Score: 102.60 E-value: 2.63e-30
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TIGR00106 | TIGR00106 | uncharacterized protein, MTH1187 family; This protein has been crystallized in both ... |
23-91 | 2.51e-11 | |||
uncharacterized protein, MTH1187 family; This protein has been crystallized in both Methanobacterium thermoautotrophicum and yeast, but its function remains unknown. Both crystal structures showed sulfate ions bound at the interface of two dimers to form a tetramer. [Unknown function, General] Pssm-ID: 272908 Cd Length: 97 Bit Score: 54.77 E-value: 2.51e-11
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Name | Accession | Description | Interval | E-value | |||
YqgV | COG0011 | Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and ... |
4-95 | 5.33e-34 | |||
Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and metabolism]; Pssm-ID: 439782 Cd Length: 98 Bit Score: 112.12 E-value: 5.33e-34
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Thiamine_BP | pfam01910 | Thiamine-binding protein; The crystal structure of two of these members shows that this domain ... |
6-95 | 2.63e-30 | |||
Thiamine-binding protein; The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6, shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative conditions this bacterium is under stress, and the transcriiptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family. Pssm-ID: 426506 Cd Length: 92 Bit Score: 102.60 E-value: 2.63e-30
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TIGR00106 | TIGR00106 | uncharacterized protein, MTH1187 family; This protein has been crystallized in both ... |
23-91 | 2.51e-11 | |||
uncharacterized protein, MTH1187 family; This protein has been crystallized in both Methanobacterium thermoautotrophicum and yeast, but its function remains unknown. Both crystal structures showed sulfate ions bound at the interface of two dimers to form a tetramer. [Unknown function, General] Pssm-ID: 272908 Cd Length: 97 Bit Score: 54.77 E-value: 2.51e-11
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Blast search parameters | ||||
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