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Conserved domains on  [gi|2071640709|gb|QXV07656|]
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MTH1187 family thiamine-binding protein [Staphylococcus epidermidis]

Protein Classification

thiamine-binding protein( domain architecture ID 10487226)

thiamine-binding protein may play a role in protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thiamine_BP pfam01910
Thiamine-binding protein; The crystal structure of two of these members shows that this domain ...
 4-99 4.11e-38

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: 123.01  E-value: 4.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   4 VDVVVIPVGTEGPSVSKYIAEIQTKLNEFKqqgkIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRIDD 83
Cdd:pfam01910   1 VDISVIPLGTGGTSVSKYVAKAIEVLKESG----LKYELGPMGTTIEGEWDEVMEVVKKAHEAVFEAGAPRVSTVIKIDD 76

                          90
                  ....*....|....*.
gi 2071640709  84 RRDKSRKMNDKLKSVQ 99
Cdd:pfam01910  77 RRDKEQTMEEKVKSVE 92
 
Name Accession Description Interval E-value
Thiamine_BP pfam01910
Thiamine-binding protein; The crystal structure of two of these members shows that this domain ...
 4-99 4.11e-38

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: 123.01  E-value: 4.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   4 VDVVVIPVGTEGPSVSKYIAEIQTKLNEFKqqgkIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRIDD 83
Cdd:pfam01910   1 VDISVIPLGTGGTSVSKYVAKAIEVLKESG----LKYELGPMGTTIEGEWDEVMEVVKKAHEAVFEAGAPRVSTVIKIDD 76

                          90
                  ....*....|....*.
gi 2071640709  84 RRDKSRKMNDKLKSVQ 99
Cdd:pfam01910  77 RRDKEQTMEEKVKSVE 92
TIGR00106 TIGR00106
uncharacterized protein, MTH1187 family; This protein has been crystallized in both ...
 2-102 5.20e-38

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: 122.95  E-value: 5.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   2 AIVDVVVIPVGTEGPSVSKYIAEIQTKLNEfkqqGKIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRI 81
Cdd:TIGR00106   1 VIAEVSIIPIGTVGASVSSYVAAAIEVLKE----SGLKYELHPMGTLIEGDLDELFEAIKAIHEAVLEKGSDRVYTSIKI 76

                          90       100
                  ....*....|....*....|.
gi 2071640709  82 DDRRDKSRKMNDKLKSVQKHL 102
Cdd:TIGR00106  77 DTRTDKHRTLRDKVKAVEEKI 97
YqgV COG0011
Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and ...
 2-103 5.88e-36

Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and metabolism];


Pssm-ID: 439782  Cd Length: 98  Bit Score: 117.90  E-value: 5.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   2 AIVDVVVIPVGTeGPSVSKYIAEIQTKLNEFKqqgkIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRI 81
Cdd:COG0011     1 VIVEISVIPLGT-GESVSEYVAEAIEVIRESG----LKYEVTPMGTTIEGELDELMAVVKKAHEALFEAGAPRVSTVIKI 75

                          90       100
                  ....*....|....*....|..
gi 2071640709  82 DDRRDKSRKMNDKLKSVQKHLD 103
Cdd:COG0011    76 DDRRDKEGTMEEKVESVEEKLG 97
 
Name Accession Description Interval E-value
Thiamine_BP pfam01910
Thiamine-binding protein; The crystal structure of two of these members shows that this domain ...
 4-99 4.11e-38

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: 123.01  E-value: 4.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   4 VDVVVIPVGTEGPSVSKYIAEIQTKLNEFKqqgkIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRIDD 83
Cdd:pfam01910   1 VDISVIPLGTGGTSVSKYVAKAIEVLKESG----LKYELGPMGTTIEGEWDEVMEVVKKAHEAVFEAGAPRVSTVIKIDD 76

                          90
                  ....*....|....*.
gi 2071640709  84 RRDKSRKMNDKLKSVQ 99
Cdd:pfam01910  77 RRDKEQTMEEKVKSVE 92
TIGR00106 TIGR00106
uncharacterized protein, MTH1187 family; This protein has been crystallized in both ...
 2-102 5.20e-38

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: 122.95  E-value: 5.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   2 AIVDVVVIPVGTEGPSVSKYIAEIQTKLNEfkqqGKIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRI 81
Cdd:TIGR00106   1 VIAEVSIIPIGTVGASVSSYVAAAIEVLKE----SGLKYELHPMGTLIEGDLDELFEAIKAIHEAVLEKGSDRVYTSIKI 76

                          90       100
                  ....*....|....*....|.
gi 2071640709  82 DDRRDKSRKMNDKLKSVQKHL 102
Cdd:TIGR00106  77 DTRTDKHRTLRDKVKAVEEKI 97
YqgV COG0011
Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and ...
 2-103 5.88e-36

Thiamin-binding stress-response protein YqgV, UPF0045 family [Coenzyme transport and metabolism];


Pssm-ID: 439782  Cd Length: 98  Bit Score: 117.90  E-value: 5.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071640709   2 AIVDVVVIPVGTeGPSVSKYIAEIQTKLNEFKqqgkIDYQLTPMNTLIEGDLKDLFEVIQAIHELPFDKGLDRVCTNIRI 81
Cdd:COG0011     1 VIVEISVIPLGT-GESVSEYVAEAIEVIRESG----LKYEVTPMGTTIEGELDELMAVVKKAHEALFEAGAPRVSTVIKI 75

                          90       100
                  ....*....|....*....|..
gi 2071640709  82 DDRRDKSRKMNDKLKSVQKHLD 103
Cdd:COG0011    76 DDRRDKEGTMEEKVESVEEKLG 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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