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Conserved domains on  [gi|501636461|ref|WP_012607745|]
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lipoate protein ligase C-terminal domain-containing protein [Desulfurococcus amylolyticus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lip_prot_lig_C super family cl40162
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial ...
 12-71 6.51e-05

Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB pfam03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.


The actual alignment was detected with superfamily member pfam10437:

Pssm-ID: 431286 [Multi-domain]  Cd Length: 85  Bit Score: 37.83  E-value: 6.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501636461  12 TVSIDIEVEECAIRTIMFSGDFFayPEENIEKLEESLKNCR-NLECIDNAFKTVENTLFIG 71
Cdd:pfam10437 16 TIEVRLNVEKGIIKDIKIYGDFF--GPGDIEELEEALIGVRyEKEAIEKALEDIDLEEYFG 74
 
Name Accession Description Interval E-value
Lip_prot_lig_C pfam10437
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial ...
 12-71 6.51e-05

Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB pfam03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.


Pssm-ID: 431286 [Multi-domain]  Cd Length: 85  Bit Score: 37.83  E-value: 6.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501636461  12 TVSIDIEVEECAIRTIMFSGDFFayPEENIEKLEESLKNCR-NLECIDNAFKTVENTLFIG 71
Cdd:pfam10437 16 TIEVRLNVEKGIIKDIKIYGDFF--GPGDIEELEEALIGVRyEKEAIEKALEDIDLEEYFG 74
 
Name Accession Description Interval E-value
Lip_prot_lig_C pfam10437
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial ...
 12-71 6.51e-05

Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB pfam03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.


Pssm-ID: 431286 [Multi-domain]  Cd Length: 85  Bit Score: 37.83  E-value: 6.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501636461  12 TVSIDIEVEECAIRTIMFSGDFFayPEENIEKLEESLKNCR-NLECIDNAFKTVENTLFIG 71
Cdd:pfam10437 16 TIEVRLNVEKGIIKDIKIYGDFF--GPGDIEELEEALIGVRyEKEAIEKALEDIDLEEYFG 74
 
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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