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Conserved domains on  [gi|1606147600|gb|TFR41260|]
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colanic acid biosynthesis acetyltransferase WcaF [Escherichia coli]

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 8.92e-132

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: 366.21  E-value: 8.92e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  81 GDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 1606147600 161 LPANVVCRGHPAVVIRKRVE 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 8.92e-132

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: 366.21  E-value: 8.92e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  81 GDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 1606147600 161 LPANVVCRGHPAVVIRKRVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
PRK10502 PRK10502
putative acyl transferase; Provisional
 1-182 3.60e-119

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 334.61  E-value: 3.60e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:PRK10502    1 MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDYAWI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  81 GDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:PRK10502   81 GDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|..
gi 1606147600 161 LPANVVCRGHPAVVIRKRVETE 182
Cdd:PRK10502  161 LPANTICRGNPAVPIRPRVETE 182
EPS_acetyl_HpsU NF038307
hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic ...
 3-171 2.50e-77

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: 228.73  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   3 DLSGFSvpkgfRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGD 82
Cdd:NF038307    8 DQSWFD-----RGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPWKVEIGDYSWIGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  83 EVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLP 162
Cdd:NF038307   83 DVVLYSLDRIRIGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVAPGVKIGANAVIGARSSVFKDMP 162


                  ....*....
gi 1606147600 163 ANVVCRGHP 171
Cdd:NF038307  163 AGQVCWGSP 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 2.72e-57

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: 175.10  E-value: 2.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  69 PWKLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDG 148
Cdd:cd05825     1 PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                          90       100
                  ....*....|....*....|....*..
gi 1606147600 149 TVVGARSSVFKSLPANVVCRGHPAVVI 175
Cdd:cd05825    81 AVVGARSVVVRDLPAWTVYAGNPAVPV 107
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
46-182 2.28e-45

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 146.17  E-value: 2.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  46 LLRLFGAKIGKNVVIRPSVKItYPWKLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINAT-P 124
Cdd:COG0110     3 LLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTgP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1606147600 125 IVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRKRVETE 182
Cdd:COG0110    82 VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
124-153 4.67e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 4.67e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1606147600 124 PIVIGEKCWLATDVFVAPGVTIGDGTVVGA 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 8.92e-132

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: 366.21  E-value: 8.92e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  81 GDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 1606147600 161 LPANVVCRGHPAVVIRKRVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
PRK10502 PRK10502
putative acyl transferase; Provisional
 1-182 3.60e-119

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 334.61  E-value: 3.60e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:PRK10502    1 MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDYAWI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  81 GDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:PRK10502   81 GDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|..
gi 1606147600 161 LPANVVCRGHPAVVIRKRVETE 182
Cdd:PRK10502  161 LPANTICRGNPAVPIRPRVETE 182
EPS_acetyl_HpsU NF038307
hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic ...
 3-171 2.50e-77

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: 228.73  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600   3 DLSGFSvpkgfRGGNAIKVQLWWAVQATIFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGD 82
Cdd:NF038307    8 DQSWFD-----RGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPWKVEIGDYSWIGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  83 EVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLP 162
Cdd:NF038307   83 DVVLYSLDRIRIGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVAPGVKIGANAVIGARSSVFKDMP 162


                  ....*....
gi 1606147600 163 ANVVCRGHP 171
Cdd:NF038307  163 AGQVCWGSP 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 2.72e-57

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: 175.10  E-value: 2.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  69 PWKLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINATPIVIGEKCWLATDVFVAPGVTIGDG 148
Cdd:cd05825     1 PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                          90       100
                  ....*....|....*....|....*..
gi 1606147600 149 TVVGARSSVFKSLPANVVCRGHPAVVI 175
Cdd:cd05825    81 AVVGARSVVVRDLPAWTVYAGNPAVPV 107
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
46-182 2.28e-45

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 146.17  E-value: 2.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  46 LLRLFGAKIGKNVVIRPSVKItYPWKLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTINAT-P 124
Cdd:COG0110     3 LLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTgP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1606147600 125 IVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRKRVETE 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 9.45e-30

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: 105.23  E-value: 9.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  71 KLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHDHASQHFTIN----ATPIVIGEKCWLATDVFVAPGVTIG 146
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEqgvtSAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 1606147600 147 DGTVVGARSSVFKSLPANVVCRGHPAVVI 175
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 41-175 5.56e-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: 92.10  E-value: 5.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  41 RWRAFLLRLFGaKIGKNVVIRPSVKITYPWKLTLGDYAWVGdeVNLYTL--GEITIGAHSVISQKSYLCTGSH--DHAS- 115
Cdd:cd03357    33 ERRELLKELFG-SVGENVYIEPPFHCDYGYNIHIGDNFYAN--FNCTILdvAPVTIGDNVLIGPNVQIYTAGHplDPEEr 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600 116 QHFTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVI 175
Cdd:cd03357   110 NRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 71-178 2.23e-19

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 81.08  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  71 KLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCtgSHDHASQH--------------FTINATPIVIGEKCWLATD 136
Cdd:PRK09677   65 KLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFIT--DHNHGSFKhsddfsspnlppdmRTLESSAVVIGQRVWIGEN 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1606147600 137 VFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRKR 178
Cdd:PRK09677  143 VTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 36-177 2.81e-19

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 80.82  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  36 PQVLYRWRAFLLRLFGaKIGKNVVIRPSVKITYPWKLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHdhaS 115
Cdd:PRK09527   41 PSEVEKRESLIKEMFA-TVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGH---P 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1606147600 116 QHFTIN------ATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRK 177
Cdd:PRK09527  117 VHHELRkngemySFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 43-177 1.18e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 65.60  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  43 RAFLLRLFGAkiGKNVVIRPSVKITYPWKLTLGDYAWVGDEVNLYTLGEITIGAHSVISQKSYLCTGSHD------HASQ 116
Cdd:PRK10092   47 QQILADLFGQ--VTEAYIEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPldpvarNSGA 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606147600 117 HFtinATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRK 177
Cdd:PRK10092  125 EL---GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 124-182 1.08e-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: 59.48  E-value: 1.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1606147600 124 PIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRKRVETE 182
Cdd:cd03349    73 DVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEE 131
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 52-171 1.65e-11

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: 60.19  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  52 AKIGKNVVIRPSVKITYpwkltlgdYAWVGDEV--NLYTlgeiTIGAHSVIsqksylctGSHDHASQHFTINATpIVIGE 129
Cdd:cd03360    97 AVIGEGCVIMAGAVINP--------DARIGDNViiNTGA----VIGHDCVI--------GDFVHIAPGVVLSGG-VTIGE 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1606147600 130 KCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHP 171
Cdd:cd03360   156 GAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 92-172 1.83e-09

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: 54.42  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  92 ITIGAHSVISQKSYL---CT-GSHDHASQHFTINATpIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVC 167
Cdd:TIGR03570 118 VRIGDNVIINTGAIVehdCViGDFVHIAPGVTLSGG-VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVV 196


                  ....*
gi 1606147600 168 RGHPA 172
Cdd:TIGR03570 197 VGVPA 201
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-178 1.67e-08

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 52.80  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIG-----KNVVIRPSVKITYpwkLT-LGDyAWVGDEVNlytlgeitIGAHSVisqksylcTGSHDHASQHFTinatp 124
Cdd:PRK14356  345 GARVGnfvemKKAVLGKGAKANH---LTyLGD-AEIGAGAN--------IGAGTI--------TCNYDGVNKHRT----- 399

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1606147600 125 iVIGEKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPAN--VVCRGHPAVVIRKR 178
Cdd:PRK14356  400 -VIGEGAFIGSNtALVAP-VTIGDGALVGAGSVITKDVPDGslAIARGRQKNLPRKK 454
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 126-177 2.57e-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: 2.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1606147600 126 VIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRK 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 6.70e-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: 51.29  E-value: 6.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  42 WRAFLLRLFGAKIGKNVVIrpsvkitypwkltlgDYAWVgDEVNLYTLG-EITIGAHSVIsqksylctgsHDHASQHFTI 120
Cdd:TIGR02353 588 FLPAILRLLGVKIGRGVYI---------------DGTDL-TERDLVTIGdDSTLNEGSVI----------QTHLFEDRVM 641

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1606147600 121 NATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFK--SLPANVVCRGHPA 172
Cdd:TIGR02353 642 KSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 53-176 1.36e-07

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: 47.88  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  53 KIGKNVVIRPSVKItypwkltlGDYAWVGDEVNLYTLGEIT----IGAHSVISQKSYLctgshdHASQHFTINATPIVIG 128
Cdd:cd03358     6 IIGTNVFIENDVKI--------GDNVKIQSNVSIYEGVTIEddvfIGPNVVFTNDLYP------RSKIYRKWELKGTTVK 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1606147600 129 EKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIR 176
Cdd:cd03358    72 RGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 24-173 9.23e-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: 47.82  E-value: 9.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  24 WWAVQATIFAwSPQVLYR---WRAFLLRLFGAKIGKNVVIRPSVKITYPWkLTLGDYAWVGDEVNLYTlgeitigaHSVi 100
Cdd:TIGR02353  83 FWTVKRLVDA-APTVLLSgspLYSLYLRALGAKIGKGVDIGSLPPVCTDL-LTIGAGTIVRKEVMLLG--------YRA- 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606147600 101 sQKSYLCTGshdhasqhftinatPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSV--FKSLPANVVCRGHPAV 173
Cdd:TIGR02353 152 -ERGRLHTG--------------PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALqgGQSIPDGERWHGSPAQ 211
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 50-171 1.62e-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: 44.74  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  50 FGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGDEVNLYtlGEITIGAHSVISQKSYlctgshdhasqhftinatpIVIGE 129
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIY--QGVTLGGKGKGGGKRH-------------------PTIGD 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1606147600 130 KCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHP 171
Cdd:cd03354    60 NVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 51-164 3.56e-06

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 45.10  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIG-----KNVVIRPSVKI---TYpwkltLGDyAWVGDEVNlytlgeitIGAHSVisqksylcTGSHDHASQHFTIna 122
Cdd:cd03353    91 GVHIGnfveiKKSTIGEGSKAnhlSY-----LGD-AEIGEGVN--------IGAGTI--------TCNYDGVNKHRTV-- 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1606147600 123 tpivIGEKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPAN 164
Cdd:cd03353   147 ----IGDNVFIGSNsQLVAP-VTIGDGATIAAGSTITKDVPPG 184
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 38-178 5.88e-06

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: 44.30  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  38 VLYRWRAFLLRLF-------GAKIGKN--------VVIrpsvkitypwkltlGDYAWVGDEVNLYtlGEITIGAHSVISQ 102
Cdd:COG1045    51 LLARLLSERARFLtgidihpGATIGRGffidhgtgVVI--------------GETAVIGDNVTIY--QGVTLGGTGKEKG 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1606147600 103 KSYlctgshdhasqhftinatPiVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVIRKR 178
Cdd:COG1045   115 KRH------------------P-TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRK 171
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 73-182 9.42e-06

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: 43.55  E-value: 9.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  73 TLGDYAWV-------GDEvnlytlGEITIGAHSVISQKSYLctgshdHASQHFtinatPIVIGEK-----------CWLA 134
Cdd:cd04645    19 TLGEGSSVwfgavlrGDV------NPIRIGERTNIQDGSVL------HVDPGY-----PTIIGDNvtvghgavlhgCTIG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1606147600 135 TDVF------VAPGVTIGDGTVVGARSSVF--KSLPANVVCRGHPAVVIRKRVETE 182
Cdd:cd04645    82 DNCLigmgaiILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRELTDEE 137
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 78-175 1.44e-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: 44.24  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  78 AWVGDEVnlyTLGE-ITIGAHSVIsqksylctgsHDHAsqhftinatpiVIGEKCWLATDVFVAPGVTIGDGTVVGARSS 156
Cdd:COG1044   103 AVIDPSA---KIGEgVSIGPFAVI----------GAGV-----------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVT 158

                          90       100
                  ....*....|....*....|...
gi 1606147600 157 VFkslpANVV----CRGHPAVVI 175
Cdd:COG1044   159 IY----ERCVigdrVIIHSGAVI 177
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 54-162 1.54e-05

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: 42.97  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  54 IGKNVVIRPSVKI------TYPwkLTLGDYAWVGDE--VNLYTLGE-ITIGAHSVISQKSylctgshdhasqhftinatp 124
Cdd:cd03359    51 LSEGCVIRPPFKKfskgvaFFP--LHIGDYVFIGENcvVNAAQIGSyVHIGKNCVIGRRC-------------------- 108

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1606147600 125 iVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVF-KSLP 162
Cdd:cd03359   109 -IIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFiGELP 146
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 126-173 3.09e-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: 43.08  E-value: 3.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1606147600 126 VIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVVCRGHPAV 173
Cdd:COG1044   260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 52-157 3.24e-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.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 40.31  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  52 AKIGKNVVIRPSVKItypwkltlGDYAWVGDEVNlytlgeitIGAHSVIsqksylctgshdHASQHFTINAtPIVIGEKC 131
Cdd:cd00208     1 VFIGEGVKIHPKAVI--------RGPVVIGDNVN--------IGPGAVI------------GAATGPNEKN-PTIIGDNV 51

                          90       100
                  ....*....|....*....|....*.
gi 1606147600 132 WLATDVFVAPGVTIGDGTVVGARSSV 157
Cdd:cd00208    52 EIGANAVIHGGVKIGDNAVIGAGAVV 77
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-164 1.23e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.39  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIG-----KNVVIRPSVKI---TYpwkltLGDyAWVGDEVNlytlgeitIGAHSVisqksylcTGSHDHASQHFTina 122
Cdd:PRK14353  327 GAKVGnfvevKNAKLGEGAKVnhlTY-----IGD-ATIGAGAN--------IGAGTI--------TCNYDGFNKHRT--- 381

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1606147600 123 tpiVIGEKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPAN 164
Cdd:PRK14353  382 ---EIGAGAFIGSNsALVAP-VTIGDGAYIASGSVITEDVPDD 420
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 93-173 2.45e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  93 TIGAHSVIsqksylctgshdhASQhfTINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPA-NVVCRGHP 171
Cdd:PRK00892  245 VIGRHTAI-------------AAQ--VGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSSGIP 309


                  ..
gi 1606147600 172 AV 173
Cdd:PRK00892  310 AQ 311
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 51-169 2.56e-04

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 40.40  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIG-----KNVVIRPSVKI---TYpwkltLGDyAWVGDEVNlytlgeitIGAHSVisqksylcTGSHDHASQHFTina 122
Cdd:COG1207   341 GVKIGnfvevKNSTIGEGSKVnhlSY-----IGD-AEIGEGVN--------IGAGTI--------TCNYDGVNKHRT--- 395

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1606147600 123 tpiVIGEKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPAN--VVCRG 169
Cdd:COG1207   396 ---VIGDGAFIGSNtNLVAP-VTIGDGATIGAGSTITKDVPAGalAIARA 441
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-164 2.76e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 40.68  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIGKNVVIRPSVKItypwkltlGDYAWVGDEVnlytlgEI---TIGAHSVISQKSYL---------------CTGSHD 112
Cdd:PRK14360  319 GVKIGPYAHLRPEAQI--------GSNCRIGNFV------EIkksQLGEGSKVNHLSYIgdatlgeqvnigagtITANYD 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1606147600 113 HASQHFTinatpiVIGEKCWL-ATDVFVAPgVTIGDGTVVGARSSVFKSLPAN 164
Cdd:PRK14360  385 GVKKHRT------VIGDRSKTgANSVLVAP-ITLGEDVTVAAGSTITKDVPDN 430
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 45-180 2.94e-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: 40.50  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  45 FLLRLFGAKIGKNVVIRPSVKITyPWKLTLGDYAWVGDEVnlytlgeitigahsvisqksylCTGSHDHASQHFTINATp 124
Cdd:TIGR02353 347 HWYRALGAKIGKVAEISSAQHEV-PDLTDIGEETFIADGL----------------------LMGNARLSGGWFRLGRT- 402

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1606147600 125 iVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPA--NVVCRGHPAVVIRKRVE 180
Cdd:TIGR02353 403 -RIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVreGVGWLGSPPFELPRRVN 459
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
124-153 4.67e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 4.67e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1606147600 124 PIVIGEKCWLATDVFVAPGVTIGDGTVVGA 153
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 86-164 6.08e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  86 LYTLGEITIGAHSVISQKSYLCtgSHDHASQHFTinatpiVIGEKCWLATDV-FVAPgVTIGDGTVVGARSSVFKSLPAN 164
Cdd:PRK14355  367 LTYLGDATIGRNVNIGCGTITC--NYDGVKKHRT------VIEDDVFVGSDVqFVAP-VTVGRNSLIAAGTTVTKDVPPD 437
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-168 6.34e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 39.62  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  74 LGDyAWVGDEVNlytlgeitIGAHSVisqksylcTGSHDHASQHFTInatpivIGEKCWLATDV-FVAPgVTIGDGTVVG 152
Cdd:PRK09451  367 LGD-AEIGDNVN--------IGAGTI--------TCNYDGANKFKTI------IGDDVFVGSDTqLVAP-VTVGKGATIG 422

                          90
                  ....*....|....*...
gi 1606147600 153 ARSSVFKSLPAN--VVCR 168
Cdd:PRK09451  423 AGTTVTRDVAENelVISR 440
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 52-175 9.16e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.97  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  52 AKIGKNVVIRPSVKItypwkltlGDYAWVGDEVnlytlgeiTIGAHSVISQKSylctgshdhasqhftinatpiVIGEKC 131
Cdd:PRK00892  113 AKIGEGVSIGPNAVI--------GAGVVIGDGV--------VIGAGAVIGDGV---------------------KIGADC 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1606147600 132 WLatdvfvAPGVTIGDGTVVGARssvfkslpanvvCRGHPAVVI 175
Cdd:PRK00892  156 RL------HANVTIYHAVRIGNR------------VIIHSGAVI 181
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 126-180 1.73e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606147600 126 VIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFkslpANVV----------CRGHPAVVIRKRVE 180
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIG----AGAVigdgvkigadCRLHANVTIYHAVR 168
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-179 1.83e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  88 TLGE-ITIGAHSVIsqksylctGSHdhasqhftinatpIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVfkslpanvv 166
Cdd:PRK00892  114 KIGEgVSIGPNAVI--------GAG-------------VVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI--------- 163

                          90
                  ....*....|...
gi 1606147600 167 crgHPAVVIRKRV 179
Cdd:PRK00892  164 ---YHAVRIGNRV 173
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 73-182 2.52e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 36.93  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  73 TLGDYAWV-------GDEvnlytlGEITIGAHSVIsQksylctgshDHASQHfTINATPIVIGEK-----------CWLA 134
Cdd:COG0663    30 TIGEDVSVwpgavlrGDV------GPIRIGEGSNI-Q---------DGVVLH-VDPGYPLTIGDDvtighgailhgCTIG 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1606147600 135 TDVFVAPGVTIGDGTVVGARSSV--------FKSLPANVVCRGHPAVVIRKRVETE 182
Cdd:COG0663    93 DNVLIGMGAIVLDGAVIGDGSIVgagalvteGKVVPPGSLVVGSPAKVVRELTEEE 148
PLN02357 PLN02357
serine acetyltransferase
 51-175 2.74e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 37.55  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIGKNVVIRPSVKITypwkltLGDYAWVGDEVNLytLGEITIGAhsvisqKSYLCTGSHDHASQHFTINATPIVIGEk 130
Cdd:PLN02357  232 GAKIGQGILLDHATGVV------IGETAVVGNNVSI--LHNVTLGG------TGKQSGDRHPKIGDGVLIGAGTCILGN- 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1606147600 131 cwlatdvfvapgVTIGDGTVVGARSSVFKSLPANVVCRGHPAVVI 175
Cdd:PLN02357  297 ------------ITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-163 3.51e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.22  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIG-----KNVVIRPSVKITYpwkLTlgdyaWVGDEvnlyTLGEIT-IGAHSVisqksylcTGSHDHASQHFTinatp 124
Cdd:PRK14352  346 EGKLGafvetKNATIGRGTKVPH---LT-----YVGDA----DIGEHSnIGASSV--------FVNYDGVNKHRT----- 400

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1606147600 125 iVIGEKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPA 163
Cdd:PRK14352  401 -TIGSHVRTGSDtMFVAP-VTVGDGAYTGAGTVIREDVPP 438
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 51-152 3.95e-03

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 36.64  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606147600  51 GAKIGKNV------VIRPSVKItypwkltlGDYAWVGDEVNLytLGEITIGAHSVISQ----------------KSYLCT 108
Cdd:cd03351    11 GAKIGENVeigpfcVIGPNVEI--------GDGTVIGSHVVI--DGPTTIGKNNRIFPfasigeapqdlkykgePTRLEI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1606147600 109 GSHDHASQHFTIN-ATPI-----VIGEKCWLATDVFVAPGVTIGDGTVVG 152
Cdd:cd03351    81 GDNNTIREFVTIHrGTAQgggvtRIGNNNLLMAYVHVAHDCVIGNNVILA 130
 
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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