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Conserved domains on  [gi|1405516402|gb|AWV58911|]
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transferase [Enterococcus faecium]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 118-176 2.83e-05

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd04647:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 109  Bit Score: 41.29  E-value: 2.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405516402 118 SIICFKEIQFKDGCTVSWDTLFMDTDsHTIFELNTH-RILNKNNKIVIGKHCWIGAKSVI 176
Cdd:cd04647    15 VISAGGGITIGDNVLIGPNVTIYDHN-HDIDDPERPiEQGVTSAPIVIGDDVWIGANVVI 73
 
Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 118-176 2.83e-05

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 41.29  E-value: 2.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405516402 118 SIICFKEIQFKDGCTVSWDTLFMDTDsHTIFELNTH-RILNKNNKIVIGKHCWIGAKSVI 176
Cdd:cd04647    15 VISAGGGITIGDNVLIGPNVTIYDHN-HDIDDPERPiEQGVTSAPIVIGDDVWIGANVVI 73
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
77-176 4.84e-05

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 41.39  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405516402  77 ISIEGILRIQGPAFIAqGAHIDIRKNAVLDIGSKFNSTGKMSIicfkeiqfKDGCTVSWDTLFMdTDSHTIFELNTHRIL 156
Cdd:COG0110     9 ARIGDGVVIGPGVRIY-GGNITIGDNVYIGPGVTIDDPGGITI--------GDNVLIGPGVTIL-TGNHPIDDPATFPLR 78

                          90       100
                  ....*....|....*....|
gi 1405516402 157 NKnnKIVIGKHCWIGAKSVI 176
Cdd:COG0110    79 TG--PVTIGDDVWIGAGATI 96
 
Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 118-176 2.83e-05

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 41.29  E-value: 2.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405516402 118 SIICFKEIQFKDGCTVSWDTLFMDTDsHTIFELNTH-RILNKNNKIVIGKHCWIGAKSVI 176
Cdd:cd04647    15 VISAGGGITIGDNVLIGPNVTIYDHN-HDIDDPERPiEQGVTSAPIVIGDDVWIGANVVI 73
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
77-176 4.84e-05

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 41.39  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405516402  77 ISIEGILRIQGPAFIAqGAHIDIRKNAVLDIGSKFNSTGKMSIicfkeiqfKDGCTVSWDTLFMdTDSHTIFELNTHRIL 156
Cdd:COG0110     9 ARIGDGVVIGPGVRIY-GGNITIGDNVYIGPGVTIDDPGGITI--------GDNVLIGPGVTIL-TGNHPIDDPATFPLR 78

                          90       100
                  ....*....|....*....|
gi 1405516402 157 NKnnKIVIGKHCWIGAKSVI 176
Cdd:COG0110    79 TG--PVTIGDDVWIGAGATI 96
 
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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