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Conserved domains on  [gi|488389215|ref|WP_002458600|]
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MULTISPECIES: general stress protein [Staphylococcus]

Protein Classification

general stress protein( domain architecture ID 10567727)

general stress protein similar to Bacillus subtilis general stress protein 17M that is induced by heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YflT pfam11181
Heat induced stress protein YflT domain; YflT is a heat induced protein. According to ...
 3-95 2.58e-13

Heat induced stress protein YflT domain; YflT is a heat induced protein. According to AlphaFold this domain is composed of a core of four beta strands that form a central beta sheet with alpha helices packed on both side. This family shows sequence similarity to pfam11821 which includes the ActD protein which forms an accessory component of the Alternative complex III which catalyzes the oxidation of membrane-bound quinol and the reduction of cytochrome c or an equivalent electron carrier. This suggests that members of this family may also be involved in forming larger redox complexes.


:

Pssm-ID: 463237  Cd Length: 99  Bit Score: 61.15  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488389215    3 KITVVNNQDELYKVINQKKSEGYLETELAVISKSKLHLDDLH-----NSQISLMATSGSFSDRMSRLLTGEDGEEAVLSR 77
Cdd:pfam11181   2 VVGVYETYEEAQKAVDELSDAGFPVDDIYIVGHDLDRVERITgrtdaNRVALSGALEGGWFGLFAGLFSGGDELRAKLSL 81

                          90
                  ....*....|....*...
gi 488389215   78 YDLTDNELEGYKQDILND 95
Cdd:pfam11181  82 LGLTEEEAEQYEEELDLG 99
 
Name Accession Description Interval E-value
YflT pfam11181
Heat induced stress protein YflT domain; YflT is a heat induced protein. According to ...
 3-95 2.58e-13

Heat induced stress protein YflT domain; YflT is a heat induced protein. According to AlphaFold this domain is composed of a core of four beta strands that form a central beta sheet with alpha helices packed on both side. This family shows sequence similarity to pfam11821 which includes the ActD protein which forms an accessory component of the Alternative complex III which catalyzes the oxidation of membrane-bound quinol and the reduction of cytochrome c or an equivalent electron carrier. This suggests that members of this family may also be involved in forming larger redox complexes.


Pssm-ID: 463237  Cd Length: 99  Bit Score: 61.15  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488389215    3 KITVVNNQDELYKVINQKKSEGYLETELAVISKSKLHLDDLH-----NSQISLMATSGSFSDRMSRLLTGEDGEEAVLSR 77
Cdd:pfam11181   2 VVGVYETYEEAQKAVDELSDAGFPVDDIYIVGHDLDRVERITgrtdaNRVALSGALEGGWFGLFAGLFSGGDELRAKLSL 81

                          90
                  ....*....|....*...
gi 488389215   78 YDLTDNELEGYKQDILND 95
Cdd:pfam11181  82 LGLTEEEAEQYEEELDLG 99
 
Name Accession Description Interval E-value
YflT pfam11181
Heat induced stress protein YflT domain; YflT is a heat induced protein. According to ...
 3-95 2.58e-13

Heat induced stress protein YflT domain; YflT is a heat induced protein. According to AlphaFold this domain is composed of a core of four beta strands that form a central beta sheet with alpha helices packed on both side. This family shows sequence similarity to pfam11821 which includes the ActD protein which forms an accessory component of the Alternative complex III which catalyzes the oxidation of membrane-bound quinol and the reduction of cytochrome c or an equivalent electron carrier. This suggests that members of this family may also be involved in forming larger redox complexes.


Pssm-ID: 463237  Cd Length: 99  Bit Score: 61.15  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488389215    3 KITVVNNQDELYKVINQKKSEGYLETELAVISKSKLHLDDLH-----NSQISLMATSGSFSDRMSRLLTGEDGEEAVLSR 77
Cdd:pfam11181   2 VVGVYETYEEAQKAVDELSDAGFPVDDIYIVGHDLDRVERITgrtdaNRVALSGALEGGWFGLFAGLFSGGDELRAKLSL 81

                          90
                  ....*....|....*...
gi 488389215   78 YDLTDNELEGYKQDILND 95
Cdd:pfam11181  82 LGLTEEEAEQYEEELDLG 99
 
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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