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Conserved domains on  [gi|504153035|ref|WP_014362998|]
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acetyltransferase [Rickettsia rickettsii]

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 ...
30-104 1.59e-09

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 cd03349:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 145  Bit Score: 52.16  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504153035  30 NIIVGDYTYYNDanhpekfeYENVRGAYFvkLIIGKFCAIAMGTSIVLL------------------------------- 78
Cdd:cd03349    1 NISVGDYSYGSG--------PDCDVGGDK--LSIGKFCSIAPGVKIGLGgnhptdwvstypfyifggeweddakfddwps 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504153035  79 ---------------SVILQ----------------------------------RYRFPDEIVEQLLEIQWWDWD 104
Cdd:cd03349   71 kgdviigndvwighgATILPgvtigdgaviaagavvtkdvppyaivggnpakviRYRFDEETIERLLALKWWDWP 145
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
30-104 1.59e-09

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 52.16  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504153035  30 NIIVGDYTYYNDanhpekfeYENVRGAYFvkLIIGKFCAIAMGTSIVLL------------------------------- 78
Cdd:cd03349    1 NISVGDYSYGSG--------PDCDVGGDK--LSIGKFCSIAPGVKIGLGgnhptdwvstypfyifggeweddakfddwps 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504153035  79 ---------------SVILQ----------------------------------RYRFPDEIVEQLLEIQWWDWD 104
Cdd:cd03349   71 kgdviigndvwighgATILPgvtigdgaviaagavvtkdvppyaivggnpakviRYRFDEETIERLLALKWWDWP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
84-121 5.15e-07

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 46.30  E-value: 5.15e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 504153035   84 RYRFPDEIVEQLLEIQWWDWDYDKITRNIPAIVRADIE 121
Cdd:TIGR03308 160 RRRFPPEIAARIEALAWWDWDHETLREALPDFRDLPAE 197
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
30-104 1.59e-09

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 52.16  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504153035  30 NIIVGDYTYYNDanhpekfeYENVRGAYFvkLIIGKFCAIAMGTSIVLL------------------------------- 78
Cdd:cd03349    1 NISVGDYSYGSG--------PDCDVGGDK--LSIGKFCSIAPGVKIGLGgnhptdwvstypfyifggeweddakfddwps 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504153035  79 ---------------SVILQ----------------------------------RYRFPDEIVEQLLEIQWWDWD 104
Cdd:cd03349   71 kgdviigndvwighgATILPgvtigdgaviaagavvtkdvppyaivggnpakviRYRFDEETIERLLALKWWDWP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
84-121 5.15e-07

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 46.30  E-value: 5.15e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 504153035   84 RYRFPDEIVEQLLEIQWWDWDYDKITRNIPAIVRADIE 121
Cdd:TIGR03308 160 RRRFPPEIAARIEALAWWDWDHETLREALPDFRDLPAE 197
 
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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