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Conserved domains on  [gi|491563915|ref|WP_005421501|]
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MULTISPECIES: accessory factor UbiK family protein [Aliivibrio]

Protein Classification

accessory factor UbiK family protein( domain architecture ID 10006814)

accessory factor UbiK family protein similar to ubiquinone biosynthesis accessory factor UbiK that is required for efficient ubiquinone (coenzyme Q) biosynthesis under aerobic conditions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiK COG2960
Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];
1-83 2.49e-29

Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];


:

Pssm-ID: 442200  Cd Length: 83  Bit Score: 99.48  E-value: 2.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563915  1 MFDPKKLEQVAKQIHESMPqPVKELGSDVEQKVRQVIQGQLNKLDVVSREEFDVQTQVLLRTRQKLTAMEQKLAELEEKL 80
Cdd:COG2960   1 MQDPKFFDDLAKLLSDALP-AAQGPRREVEKNVRAQLQSALSKLDLVTREEFDVQRAVLARTREKLEALEARLAELEAKL 79


                ...
gi 491563915 81 SEK 83
Cdd:COG2960  80 AAA 82
 
Name Accession Description Interval E-value
UbiK COG2960
Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];
1-83 2.49e-29

Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];


Pssm-ID: 442200  Cd Length: 83  Bit Score: 99.48  E-value: 2.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563915  1 MFDPKKLEQVAKQIHESMPqPVKELGSDVEQKVRQVIQGQLNKLDVVSREEFDVQTQVLLRTRQKLTAMEQKLAELEEKL 80
Cdd:COG2960   1 MQDPKFFDDLAKLLSDALP-AAQGPRREVEKNVRAQLQSALSKLDLVTREEFDVQRAVLARTREKLEALEARLAELEAKL 79


                ...
gi 491563915 81 SEK 83
Cdd:COG2960  80 AAA 82
BMFP pfam04380
Membrane fusogenic activity; BMFP consists of two structural domains, a coiled-coil C-terminal ...
 8-78 1.50e-20

Membrane fusogenic activity; BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro.


Pssm-ID: 461284  Cd Length: 70  Bit Score: 76.75  E-value: 1.50e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491563915   8 EQVAKQIHESMPQPVKeLGSDVEQKVRQVIQGQLNKLDVVSREEFDVQTQVLLRTRQKLTAMEQKLAELEE 78
Cdd:pfam04380  1 DDLAKQLSGALPAAAG-LRREVEKNVRARLQRALSKLDLVTREEFDVQRAVLARTREKLEALEARVAALEA 70
 
Name Accession Description Interval E-value
UbiK COG2960
Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];
1-83 2.49e-29

Ubiquinone biosynthesis accessory factor UbiK [Coenzyme transport and metabolism];


Pssm-ID: 442200  Cd Length: 83  Bit Score: 99.48  E-value: 2.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563915  1 MFDPKKLEQVAKQIHESMPqPVKELGSDVEQKVRQVIQGQLNKLDVVSREEFDVQTQVLLRTRQKLTAMEQKLAELEEKL 80
Cdd:COG2960   1 MQDPKFFDDLAKLLSDALP-AAQGPRREVEKNVRAQLQSALSKLDLVTREEFDVQRAVLARTREKLEALEARLAELEAKL 79


                ...
gi 491563915 81 SEK 83
Cdd:COG2960  80 AAA 82
BMFP pfam04380
Membrane fusogenic activity; BMFP consists of two structural domains, a coiled-coil C-terminal ...
 8-78 1.50e-20

Membrane fusogenic activity; BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro.


Pssm-ID: 461284  Cd Length: 70  Bit Score: 76.75  E-value: 1.50e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491563915   8 EQVAKQIHESMPQPVKeLGSDVEQKVRQVIQGQLNKLDVVSREEFDVQTQVLLRTRQKLTAMEQKLAELEE 78
Cdd:pfam04380  1 DDLAKQLSGALPAAAG-LRREVEKNVRARLQRALSKLDLVTREEFDVQRAVLARTREKLEALEARVAALEA 70
 
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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