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Conserved domains on  [gi|556479301|ref|WP_023330881|]
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MULTISPECIES: colanic acid biosynthesis acetyltransferase WcaF [Enterobacter]

Protein Classification

putative colanic acid biosynthesis acetyltransferase( domain architecture ID 11499289)

putative colanic acid biosynthesis acetyltransferase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaF TIGR04008
colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl ...
 1-180 1.21e-133

colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species. This acetyltransferase is believed to catalyze the addition of the acetyl group that is attached through an O linkage to the first fucosyl residue of the colanic acid repetitive unit (E unit)


:

Pssm-ID: 188523  Cd Length: 180  Bit Score: 371.21  E-value: 1.21e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301    1 MQDLKGFSVPKGFRGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   81 GDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 556479301  161 LPANKVCRGNPAVVIRERVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
 
Name Accession Description Interval E-value
WcaF TIGR04008
colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl ...
 1-180 1.21e-133

colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species. This acetyltransferase is believed to catalyze the addition of the acetyl group that is attached through an O linkage to the first fucosyl residue of the colanic acid repetitive unit (E unit)


Pssm-ID: 188523  Cd Length: 180  Bit Score: 371.21  E-value: 1.21e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301    1 MQDLKGFSVPKGFRGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   81 GDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 556479301  161 LPANKVCRGNPAVVIRERVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
PRK10502 PRK10502
putative acyl transferase; Provisional
 1-182 1.82e-121

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 340.39  E-value: 1.82e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   1 MQDLKGFSVPKGFRGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:PRK10502   1 MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDYAWI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  81 GDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKS 160
Cdd:PRK10502  81 GDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160

                        170       180
                 ....*....|....*....|..
gi 556479301 161 LPANKVCRGNPAVVIRERVETD 182
Cdd:PRK10502 161 LPANTICRGNPAVPIRPRVETE 182
EPS_acetyl_HpsU NF038307
hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic ...
 14-171 5.53e-78

hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic acid biosynthesis acetyltransferase WcaF, which acts on a fucose residue in a disaccharide attached to a lipid carrier.


Pssm-ID: 439606  Cd Length: 178  Bit Score: 230.27  E-value: 5.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  14 RGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGEIT 93
Cdd:NF038307  14 RGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPWKVEIGDYSWIGDDVVLYSLDRIR 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556479301  94 IGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNP 171
Cdd:NF038307  94 IGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVAPGVKIGANAVIGARSSVFKDMPAGQVCWGSP 171
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 69-175 8.62e-58

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 176.64  E-value: 8.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  69 PWKLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDG 148
Cdd:cd05825    1 PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                         90       100
                 ....*....|....*....|....*..
gi 556479301 149 TVVGARSSVFKSLPANKVCRGNPAVVI 175
Cdd:cd05825   81 AVVGARSVVVRDLPAWTVYAGNPAVPV 107
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
46-182 7.11e-47

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 150.02  E-value: 7.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  46 LLRLFGAKIGKNVVIRPSVKItYPWKLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQH-FDITASP 124
Cdd:COG0110    3 LLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAtFPLRTGP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556479301 125 IVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRERVETD 182
Cdd:COG0110   82 VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
124-153 2.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 556479301  124 PIVIGEKCWLATDVFVAPGVSVGDGTVVGA 153
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WcaF TIGR04008
colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl ...
 1-180 1.21e-133

colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species. This acetyltransferase is believed to catalyze the addition of the acetyl group that is attached through an O linkage to the first fucosyl residue of the colanic acid repetitive unit (E unit)


Pssm-ID: 188523  Cd Length: 180  Bit Score: 371.21  E-value: 1.21e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301    1 MQDLKGFSVPKGFRGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   81 GDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 556479301  161 LPANKVCRGNPAVVIRERVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
PRK10502 PRK10502
putative acyl transferase; Provisional
 1-182 1.82e-121

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 340.39  E-value: 1.82e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   1 MQDLKGFSVPKGFRGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:PRK10502   1 MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDYAWI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  81 GDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKS 160
Cdd:PRK10502  81 GDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160

                        170       180
                 ....*....|....*....|..
gi 556479301 161 LPANKVCRGNPAVVIRERVETD 182
Cdd:PRK10502 161 LPANTICRGNPAVPIRPRVETE 182
EPS_acetyl_HpsU NF038307
hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic ...
 14-171 5.53e-78

hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic acid biosynthesis acetyltransferase WcaF, which acts on a fucose residue in a disaccharide attached to a lipid carrier.


Pssm-ID: 439606  Cd Length: 178  Bit Score: 230.27  E-value: 5.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  14 RGGNGIKVQLWWAVQATLFAWSPQILYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGEIT 93
Cdd:NF038307  14 RGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPWKVEIGDYSWIGDDVVLYSLDRIR 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556479301  94 IGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNP 171
Cdd:NF038307  94 IGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVAPGVKIGANAVIGARSSVFKDMPAGQVCWGSP 171
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 69-175 8.62e-58

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 176.64  E-value: 8.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  69 PWKLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDG 148
Cdd:cd05825    1 PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                         90       100
                 ....*....|....*....|....*..
gi 556479301 149 TVVGARSSVFKSLPANKVCRGNPAVVI 175
Cdd:cd05825   81 AVVGARSVVVRDLPAWTVYAGNPAVPV 107
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
46-182 7.11e-47

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 150.02  E-value: 7.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  46 LLRLFGAKIGKNVVIRPSVKItYPWKLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQH-FDITASP 124
Cdd:COG0110    3 LLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAtFPLRTGP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556479301 125 IVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRERVETD 182
Cdd:COG0110   82 VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 71-175 1.43e-29

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: 104.85  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  71 KLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFMSQHFDI----TASPIVIGEKCWLATDVFVAPGVSVG 146
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIeqgvTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 556479301 147 DGTVVGARSSVFKSLPANKVCRGNPAVVI 175
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 41-175 8.53e-24

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 91.71  E-value: 8.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  41 RWRAFLLRLFGaKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHdfmsqHFDI 120
Cdd:cd03357   33 ERRELLKELFG-SVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGH-----PLDP 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556479301 121 --------TASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVI 175
Cdd:cd03357  107 eernrgleYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 71-178 9.00e-19

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.53  E-value: 9.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  71 KLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSH-------DFMSQHFD-----ITASPIVIGEKCWLATDVF 138
Cdd:PRK09677  65 KLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgsfkhsdDFSSPNLPpdmrtLESSAVVIGQRVWIGENVT 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556479301 139 VAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRER 178
Cdd:PRK09677 145 ILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 43-182 1.65e-18

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 78.89  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  43 RAFLLRLFGaKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGEITIGANSVVSQKCYLCTGSHDFmsqHFDITA 122
Cdd:PRK09527  48 ESLIKEMFA-TVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPV---HHELRK 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556479301 123 S------PIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRERVETD 182
Cdd:PRK09527 124 NgemysfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRD 189
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 43-176 1.11e-16

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 73.69  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  43 RAFLLRLFGAkiGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGEITIGANsvvsqkCYLCTGSHDFMSQH-FDIT 121
Cdd:PRK10092  47 QQILADLFGQ--VTEAYIEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDN------CMLAPGVHIYTATHpLDPV 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556479301 122 A--------SPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIR 176
Cdd:PRK10092 119 ArnsgaelgKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 124-178 2.03e-11

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: 58.71  E-value: 2.03e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556479301 124 PIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRER 178
Cdd:cd03349   73 DVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 52-171 1.44e-09

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 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. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 54.80  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  52 AKIGKNVVIRPSVKITYpwkltlgdyawvgddavlytlgEITIGANSVVSQKCYL---CT-GSHDFMSQHFDITASpIVI 127
Cdd:cd03360   97 AVIGEGCVIMAGAVINP----------------------DARIGDNVIINTGAVIghdCViGDFVHIAPGVVLSGG-VTI 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 556479301 128 GEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNP 171
Cdd:cd03360  154 GEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 126-177 2.59e-08

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 51.25  E-value: 2.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556479301 126 VIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRE 177
Cdd:cd03352  152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 42-172 2.75e-08

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 52.45  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   42 WRAFLLRLFGAKIGKNVVIrpsvkitypwkltlgDYAWVGDdavlYTLgeITIGANSVVSQKCYLCTgsHDFMSQHFDIt 121
Cdd:TIGR02353 588 FLPAILRLLGVKIGRGVYI---------------DGTDLTE----RDL--VTIGDDSTLNEGSVIQT--HLFEDRVMKS- 643

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 556479301  122 aSPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFK--SLPANKVCRGNPA 172
Cdd:TIGR02353 644 -DTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 73-177 4.05e-08

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 50.10  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  73 TLGDYAWVGDDAVLYT-LGEITIGANSVVSQKCYLCTgSHDFmsqhfditasPIVIGEK-----------CWLATDVF-- 138
Cdd:cd04645   19 TLGEGSSVWFGAVLRGdVNPIRIGERTNIQDGSVLHV-DPGY----------PTIIGDNvtvghgavlhgCTIGDNCLig 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 556479301 139 ----VAPGVSVGDGTVVGARSSVF--KSLPANKVCRGNPAVVIRE 177
Cdd:cd04645   88 mgaiILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 92-172 1.16e-07

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 49.41  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   92 ITIGANSVVSQKCYL---CT-GSHDFMSQHFDITASpIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVC 167
Cdd:TIGR03570 118 VRIGDNVIINTGAIVehdCViGDFVHIAPGVTLSGG-VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVV 196


                  ....*
gi 556479301  168 RGNPA 172
Cdd:TIGR03570 197 VGVPA 201
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 54-162 1.60e-07

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 48.75  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  54 IGKNVVIRPSVKIT------YPwkLTLGDYAWVGDDAVLY--TLGE-ITIGANSVVSQKCylctgshdfmsqhfditasp 124
Cdd:cd03359   51 LSEGCVIRPPFKKFskgvafFP--LHIGDYVFIGENCVVNaaQIGSyVHIGKNCVIGRRC-------------------- 108

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 556479301 125 iVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVF-KSLP 162
Cdd:cd03359  109 -IIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFiGELP 146
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 24-173 3.09e-07

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 49.36  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   24 WWAVQaTLFAWSPQILYR---WRAFLLRLFGAKIGKNVVIRPSVKITYpwkltlgdyawvgddavlytlGEITIGANSVV 100
Cdd:TIGR02353  83 FWTVK-RLVDAAPTVLLSgspLYSLYLRALGAKIGKGVDIGSLPPVCT---------------------DLLTIGAGTIV 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556479301  101 SQKCYLCTGShdfmSQHFDITASPIVIGEKCWLATDVFVAPGVSVGDGTVVGARSSV--FKSLPANKVCRGNPAV 173
Cdd:TIGR02353 141 RKEVMLLGYR----AERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALqgGQSIPDGERWHGSPAQ 211
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 52-157 3.16e-06

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.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 43.39  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  52 AKIGKNVVIRPSVKItypwkltlGDYAWVGDDAvlytlgeiTIGANSVVsqkcylctgshdfMSQHFDITASPIVIGEKC 131
Cdd:cd00208    1 VFIGEGVKIHPKAVI--------RGPVVIGDNV--------NIGPGAVI-------------GAATGPNEKNPTIIGDNV 51

                         90       100
                 ....*....|....*....|....*.
gi 556479301 132 WLATDVFVAPGVSVGDGTVVGARSSV 157
Cdd:cd00208   52 EIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 50-171 4.41e-06

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 43.20  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  50 FGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYtlGEITIGANSVVSQKcylctgshdfmsQHfditaspIVIGE 129
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIY--QGVTLGGKGKGGGK------------RH-------PTIGD 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 556479301 130 KCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNP 171
Cdd:cd03354   60 NVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 53-176 6.37e-06

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 43.26  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  53 KIGKNVVIRPSVKItypwkltlGDYAWVGDDAVLYTLGEIT----IGANSVVSQKCYLCTGSHDFMSQhfditaSPIVIG 128
Cdd:cd03358    6 IIGTNVFIENDVKI--------GDNVKIQSNVSIYEGVTIEddvfIGPNVVFTNDLYPRSKIYRKWEL------KGTTVK 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 556479301 129 EKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIR 176
Cdd:cd03358   72 RGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 38-178 1.54e-05

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 43.15  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  38 ILYRWRAFLLRLF-------GAKIGKN--------VVIrpsvkitypwkltlGDYAWVGDDAVLYtlGEITIGANSVVSQ 102
Cdd:COG1045   51 LLARLLSERARFLtgidihpGATIGRGffidhgtgVVI--------------GETAVIGDNVTIY--QGVTLGGTGKEKG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301 103 KcylctgshdfmsQHfditasPiVIGEkcwlatDVFVAPG------VSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIR 176
Cdd:COG1045  115 K------------RH------P-TIGD------NVVIGAGakilgpITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169


                 ..
gi 556479301 177 ER 178
Cdd:COG1045  170 RK 171
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 126-177 4.67e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.70  E-value: 4.67e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556479301 126 VIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRE 177
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHRE 311
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-169 9.35e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.02  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  51 GAKIG-----KNVVIRPSVKITYpwkLT-LGDyAWVGDDAvlytlgeiTIGANSVvsqkcylcTGSHDFMSQHfditasP 124
Cdd:PRK14356 345 GARVGnfvemKKAVLGKGAKANH---LTyLGD-AEIGAGA--------NIGAGTI--------TCNYDGVNKH------R 398

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 556479301 125 IVIGEKCWLATD-VFVAPgVSVGDGTVVGARSSVFKSLPANK--VCRG 169
Cdd:PRK14356 399 TVIGEGAFIGSNtALVAP-VTIGDGALVGAGSVITKDVPDGSlaIARG 445
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 51-154 1.64e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.16  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  51 GAKIGKNVVIRPSVKItypwkltlGDYAWVGDDAVlytlgeitIGANSVVSQKCylctgshdfmsqhfditaspiVIGEK 130
Cdd:COG1044  108 SAKIGEGVSIGPFAVI--------GAGVVIGDGVV--------IGPGVVIGDGV---------------------VIGDD 150

                         90       100
                 ....*....|....*....|....
gi 556479301 131 CWLAtdvfvaPGVSVGDGTVVGAR 154
Cdd:COG1044  151 CVLH------PNVTIYERCVIGDR 168
PLN02739 PLN02739
serine acetyltransferase
 127-182 2.15e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 40.79  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556479301 127 IGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRERVETD 182
Cdd:PLN02739 260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQD 315
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 45-182 2.35e-04

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 40.89  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301   45 FLLRLFGAKIGKNVVIRPSVKITyPWKLTLGDYAWVGDDAVLytlGEITIGANSvvsqkcylctgshdfmsqhfdITASP 124
Cdd:TIGR02353 347 HWYRALGAKIGKVAEISSAQHEV-PDLTDIGEETFIADGLLM---GNARLSGGW---------------------FRLGR 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  125 IVIGEKCWLATDVFVAPGVSVGDGTVVGARSSVFKSLPANKVCR--GNPAVVIRERVETD 182
Cdd:TIGR02353 402 TRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGwlGSPPFELPRRVNRD 461
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 78-157 3.13e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 40.00  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  78 AWVGDDAvlyTLGE-ITIGANSVVSQKCylctgshdfmsqhfditaspiVIGEKCWLATDVFVAPGVSVGDGTVVGARSS 156
Cdd:COG1044  103 AVIDPSA---KIGEgVSIGPFAVIGAGV---------------------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVT 158


                 .
gi 556479301 157 V 157
Cdd:COG1044  159 I 159
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 73-182 6.46e-04

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.47  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  73 TLGDYAWVGDDAVLY-TLGEITIGANSVVSQKCYL-CTGSHdfmsqhfditasPIVIGEK-----------CWLATDVFV 139
Cdd:COG0663   30 TIGEDVSVWPGAVLRgDVGPIRIGEGSNIQDGVVLhVDPGY------------PLTIGDDvtighgailhgCTIGDNVLI 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556479301 140 A------PGVSVGDGTVVGARSSVF--KSLPANKVCRGNPAVVIRERVETD 182
Cdd:COG0663   98 GmgaivlDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTEEE 148
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 86-164 1.09e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.57  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  86 LYTLGEITIGANsvVSQKCYLCTGSHDFMSQHfditasPIVIGEKCWLATDV-FVAPgVSVGDGTVVGARSSVFKSLPAN 164
Cdd:PRK14355 367 LTYLGDATIGRN--VNIGCGTITCNYDGVKKH------RTVIEDDVFVGSDVqFVAP-VTVGRNSLIAAGTTVTKDVPPD 437
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 73-177 1.65e-03

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 37.35  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  73 TLGDYAWVGDDAVLY-TLGEITIGANSVVSQKCYLctgsHDFMSQHF------DITASPIV----IGEKCWLATDVFVAP 141
Cdd:cd04745   20 IIGKNCYIGPHASLRgDFGRIVIRDGANVQDNCVI----HGFPGQDTvleengHIGHGAILhgctIGRNALVGMNAVVMD 95

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 556479301 142 GVSVGDGTVVGARSSVfKS---LPANKVCRGNPAVVIRE 177
Cdd:cd04745   96 GAVIGEESIVGAMAFV-KAgtvIPPRSLIAGSPAKVIRE 133
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
124-153 2.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 556479301  124 PIVIGEKCWLATDVFVAPGVSVGDGTVVGA 153
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 78-157 3.74e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  78 AWVGDDAVLytlGE-ITIGANSVVSQKCylctgshdfmsqhfditaspiVIGEKCWLATDVFVAPGVSVGDGTVVGARSS 156
Cdd:PRK00892 107 AVIDPSAKI---GEgVSIGPNAVIGAGV---------------------VIGDGVVIGAGAVIGDGVKIGADCRLHANVT 162


                 .
gi 556479301 157 V 157
Cdd:PRK00892 163 I 163
PLN02357 PLN02357
serine acetyltransferase
 51-175 6.26e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 36.40  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  51 GAKIGKNVVIRPSVKITypwkltLGDYAWVGDDAVLytLGEITIGANSVVsqkcylCTGSHDFMSQHFDITASPIVIGEk 130
Cdd:PLN02357 232 GAKIGQGILLDHATGVV------IGETAVVGNNVSI--LHNVTLGGTGKQ------SGDRHPKIGDGVLIGAGTCILGN- 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 556479301 131 cwlatdvfvapgVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVI 175
Cdd:PLN02357 297 ------------ITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 52-154 6.41e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.27  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  52 AKIGKNVVIRPSVKItypwkltlGDYAWVGDDAVlytlgeitIGANSVVSQKCylctgshdfmsqhfditaspiVIGEKC 131
Cdd:PRK00892 113 AKIGEGVSIGPNAVI--------GAGVVIGDGVV--------IGAGAVIGDGV---------------------KIGADC 155

                         90       100
                 ....*....|....*....|...
gi 556479301 132 WLAtdvfvaPGVSVGDGTVVGAR 154
Cdd:PRK00892 156 RLH------ANVTIYHAVRIGNR 172
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-177 6.75e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 36.38  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  51 GAKIG-----KNVVIRPSVKI---TYpwkltLGDyAWVGDDAvlytlgeiTIGANSVvsqkcylcTGSHDFMSQHFdita 122
Cdd:PRK14353 327 GAKVGnfvevKNAKLGEGAKVnhlTY-----IGD-ATIGAGA--------NIGAGTI--------TCNYDGFNKHR---- 380

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556479301 123 spIVIGEKCWLATD-VFVAPgVSVGDGTVVGARSSVFKSLPANKVCRGNPAVVIRE 177
Cdd:PRK14353 381 --TEIGAGAFIGSNsALVAP-VTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 51-152 8.84e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 35.77  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556479301  51 GAKIGKNVVIRPSVKITYPwkLTLGDYAWVGDDAVLytLGEITIGANSVVSQKCYLCTGSHDFmsqHFDITASPIVIGEK 130
Cdd:PRK12461  11 SAKLGSGVEIGPFAVIGAN--VEIGDGTWIGPHAVI--LGPTRIGKNNKIHQGAVVGDEPQDF---TYKGEESRLEIGDR 83

                         90       100
                 ....*....|....*....|..
gi 556479301 131 CWLATDVFVAPGVSVGDGTVVG 152
Cdd:PRK12461  84 NVIREGVTIHRGTKGGGVTRIG 105
 
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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