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Conserved domains on  [gi|1352183975|gb|AVI54991|]
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maltose O-acetyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

maltose O-acetyltransferase( domain architecture ID 11484575)

maltose O-acetyltransferase catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-183 4.07e-143

maltose O-acetyltransferase; Provisional


:

Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 394.95  E-value: 4.07e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80
Cdd:PRK10092    1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  81 FANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160
Cdd:PRK10092   81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                         170       180
                  ....*....|....*....|...
gi 1352183975 161 VVTKDVPDNVVVGGNPARIIKKL 183
Cdd:PRK10092  161 VVTKDVPDNVVVGGNPARIIKKL 183
 
Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-183 4.07e-143

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 394.95  E-value: 4.07e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80
Cdd:PRK10092    1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  81 FANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160
Cdd:PRK10092   81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                         170       180
                  ....*....|....*....|...
gi 1352183975 161 VVTKDVPDNVVVGGNPARIIKKL 183
Cdd:PRK10092  161 VVTKDVPDNVVVGGNPARIIKKL 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 13-180 1.89e-106

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: 302.03  E-value: 1.89e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  13 LYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNFFANFDCVMLDV 91
Cdd:cd03357     1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGEnVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  92 CPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVV 171
Cdd:cd03357    81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                  ....*....
gi 1352183975 172 VGGNPARII 180
Cdd:cd03357   161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
60-183 2.95e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 171.21  E-value: 2.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  60 AYIEPTFRCdYGYNIFLGNNFFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARnsGAELGKPVTIGNNVWIG 139
Cdd:COG0110    15 VVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDVWIG 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1352183975 140 GRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
Cdd:COG0110    92 AGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-177 1.24e-19

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: 81.77  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:TIGR03570 137 VIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198


                  ...
gi 1352183975 175 NPA 177
Cdd:TIGR03570 199 VPA 201
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 7-57 1.90e-19

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 77.15  E-value: 1.90e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975   7 KMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQV 57
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSV 51
 
Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-183 4.07e-143

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 394.95  E-value: 4.07e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80
Cdd:PRK10092    1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  81 FANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160
Cdd:PRK10092   81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                         170       180
                  ....*....|....*....|...
gi 1352183975 161 VVTKDVPDNVVVGGNPARIIKKL 183
Cdd:PRK10092  161 VVTKDVPDNVVVGGNPARIIKKL 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 13-180 1.89e-106

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: 302.03  E-value: 1.89e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  13 LYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNFFANFDCVMLDV 91
Cdd:cd03357     1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGEnVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  92 CPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVV 171
Cdd:cd03357    81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                  ....*....
gi 1352183975 172 VGGNPARII 180
Cdd:cd03357   161 AAGNPARVI 169
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-183 2.02e-62

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 191.76  E-value: 2.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNN 79
Cdd:PRK09527    2 NMSMTERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGEnAWVEPPVYFSYGSNIHIGRN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  80 FFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASG 159
Cdd:PRK09527   82 FYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAG 161

                         170       180
                  ....*....|....*....|....
gi 1352183975 160 AVVTKDVPDNVVVGGNPARIIKKL 183
Cdd:PRK09527  162 SVVTKDIPPNVVAAGVPCRVIREI 185
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
60-183 2.95e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 171.21  E-value: 2.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  60 AYIEPTFRCdYGYNIFLGNNFFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARnsGAELGKPVTIGNNVWIG 139
Cdd:COG0110    15 VVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDVWIG 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1352183975 140 GRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
Cdd:COG0110    92 AGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 73-180 9.99e-47

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: 148.37  E-value: 9.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  73 NIFLGNNFFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAEL-GKPVTIGNNVWIGGRAVINPGVTIG 151
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVtSAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 1352183975 152 DNVVVASGAVVTKDVPDNVVVGGNPARII 180
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 73-182 1.68e-32

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: 113.41  E-value: 1.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  73 NIFLGN-NFFANFDCVMLDVcPIRIGDNCMLAPGVHIYT-ATHPID-----PVARNSGAELG----------KPVTIGNN 135
Cdd:cd03349     1 NISVGDySYGSGPDCDVGGD-KLSIGKFCSIAPGVKIGLgGNHPTDwvstyPFYIFGGEWEDdakfddwpskGDVIIGND 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1352183975 136 VWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
Cdd:cd03349    80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 93-180 8.52e-25

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: 92.67  E-value: 8.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  93 PIRIGDNCMLAPGVHIYTATHPIDPVARNSgaeLGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVV 172
Cdd:cd05825    23 PVTIGSDACISQGAYLCTGSHDYRSPAFPL---ITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVY 99


                  ....*...
gi 1352183975 173 GGNPARII 180
Cdd:cd05825   100 AGNPAVPV 107
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 71-181 9.14e-25

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: 92.95  E-value: 9.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  71 GYNIFLGNNFFANFDCVMLDVCPI----------RIGDNCMLAPGVhiyTATHPIDPVARNSGAELGKPVTIGNNVWIGG 140
Cdd:cd03358     2 GDNCIIGTNVFIENDVKIGDNVKIqsnvsiyegvTIEDDVFIGPNV---VFTNDLYPRSKIYRKWELKGTTVKRGASIGA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1352183975 141 RAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
Cdd:cd03358    79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10502 PRK10502
putative acyl transferase; Provisional
 62-181 9.84e-23

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 89.62  E-value: 9.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  62 IEPTFRCDYGYNIFLGNNFFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSgaeLGKPVTIGNNVWIGGR 141
Cdd:PRK10502   60 IRPSVRITYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDL---NTAPIVIGEGCWLAAD 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1352183975 142 AVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
Cdd:PRK10502  137 VFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 71-176 1.28e-21

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: 86.77  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  71 GYNIFLGNNFFANF------DCVmldvcpirIGDNCMLAPGVHIytathpidpvarnSGAelgkpVTIGNNVWIGGRAVI 144
Cdd:cd03360   112 NPDARIGDNVIINTgavighDCV--------IGDFVHIAPGVVL-------------SGG-----VTIGEGAFIGAGATI 165

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1352183975 145 NPGVTIGDNVVVASGAVVTKDVPDNVVVGGNP 176
Cdd:cd03360   166 IQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 96-182 9.69e-21

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: 83.98  E-value: 9.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  96 IGDNCMLAPGVhiyT--AThpidpvarnsGAELGKPV-TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVV 172
Cdd:COG1045    94 IGDNVTIYQGV---TlgGT----------GKEKGKRHpTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                          90
                  ....*....|
gi 1352183975 173 GGNPARIIKK 182
Cdd:COG1045   161 VGVPARIVKR 170
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-177 1.24e-19

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: 81.77  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:TIGR03570 137 VIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198


                  ...
gi 1352183975 175 NPA 177
Cdd:TIGR03570 199 VPA 201
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 7-57 1.90e-19

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 77.15  E-value: 1.90e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975   7 KMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQV 57
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSV 51
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 94-182 8.67e-19

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.53  E-value: 8.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  94 IRIGDNCMLAPGVHIYTATH------------PIDPVARNSGAElgkPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAV 161
Cdd:PRK09677   86 ITIGRDTLIASKVFITDHNHgsfkhsddfsspNLPPDMRTLESS---AVVIGQRVWIGENVTILPGVSIGNGCIVGANSV 162

                          90       100
                  ....*....|....*....|.
gi 1352183975 162 VTKDVPDNVVVGGNPARIIKK 182
Cdd:PRK09677  163 VTKSIPENTVIAGNPAKIIKK 183
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 95-176 1.92e-18

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: 75.94  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:cd03354    30 VIGDNCTIYQGVTL----------GGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVG 99


                  ..
gi 1352183975 175 NP 176
Cdd:cd03354   100 VP 101
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 74-163 2.73e-18

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: 74.98  E-value: 2.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  74 IFLGNNFFANFDCVMLDvcPIRIGDNCMLAPGVHIYTATHPidpvarnsgaELGKPVTIGNNVWIGGRAVINPGVTIGDN 153
Cdd:cd00208     1 VFIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDN 68

                          90
                  ....*....|
gi 1352183975 154 VVVASGAVVT 163
Cdd:cd00208    69 AVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-182 4.55e-17

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: 75.14  E-value: 4.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:cd03352   134 RIGENCLIAAQVGI-------------AGS-----TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195


                  ....*...
gi 1352183975 175 NPARIIKK 182
Cdd:cd03352   196 TPAQPHRE 203
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 51-183 6.00e-16

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: 70.90  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  51 ADLFGQVT---EAYIEP--TFRCDYGYnIFLGNNFfaNF-DCVMLDV---CPIRIGDNCMLAPGVHIYTAThpidpvarn 121
Cdd:cd04645    12 ATVIGDVTlgeGSSVWFgaVLRGDVNP-IRIGERT--NIqDGSVLHVdpgYPTIIGDNVTVGHGAVLHGCT--------- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352183975 122 sgaelgkpvtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVT--KDVPDNVVVGGNPARIIKKL 183
Cdd:cd04645    80 ----------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 51-183 1.10e-15

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 70.83  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  51 ADLFGQVT---EAYIEP--TFRCDYGYnIFLGNNffANF-DCVML---DVCPIRIGDNCMLAPGVHIytatHpidpvarn 121
Cdd:COG0663    23 AVVIGDVTigeDVSVWPgaVLRGDVGP-IRIGEG--SNIqDGVVLhvdPGYPLTIGDDVTIGHGAIL----H-------- 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352183975 122 sGAelgkpvTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVT--KDVPDNVVVGGNPARIIKKL 183
Cdd:COG0663    88 -GC------TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVREL 144
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-178 8.61e-14

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: 67.74  E-value: 8.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:COG1044   242 RIGEHTAIAAQVGI-------------AGS-----TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSG 303


                  ....
gi 1352183975 175 NPAR 178
Cdd:COG1044   304 SPAQ 307
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 95-179 1.09e-12

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: 63.99  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytaTHpiDPVARN-----SGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169
Cdd:cd03351   104 RIGNNNLLMAYVHV---AH--DCVIGNnvilaNNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPY 178

                          90
                  ....*....|
gi 1352183975 170 VVVGGNPARI 179
Cdd:cd03351   179 VIAAGNRARL 188
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 73-183 2.65e-12

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: 61.46  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  73 NIFLGNNFFANFDCVML-DVCPIRIGDNCMLAPGVHIytathpIDPVARNSGAELGKPVTIGNNVWI------------- 138
Cdd:cd03359    21 NIVLNGKTIIQSDVIIRgDLATVSIGRYCILSEGCVI------RPPFKKFSKGVAFFPLHIGDYVFIgencvvnaaqigs 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975 139 ----GGRAVINPGVTIGDNVVVASGAVVTKD--VPDNVVVGGNPARIIKKL 183
Cdd:cd03359    95 yvhiGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGEL 145
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-181 4.84e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.85  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPD-NVVVG 173
Cdd:PRK00892  245 VIGRHTAIAAQVGI-------------AGS-----TKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSS 306


                  ....*...
gi 1352183975 174 GNPARIIK 181
Cdd:PRK00892  307 GIPAQPNK 314
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 95-179 1.03e-10

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 58.49  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytAtHpiDPVARN-----SGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169
Cdd:COG1043   106 RIGDDNLLMAYVHV--A-H--DCVVGNnvilaNNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPY 180

                          90
                  ....*....|
gi 1352183975 170 VVVGGNPARI 179
Cdd:COG1043   181 VLAAGNPARL 190
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 132-183 1.69e-09

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 53.73  E-value: 1.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352183975 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVT--KDVPDNVVVGGNPARIIKKL 183
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 95-180 2.77e-09

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 54.57  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:TIGR01852 103 RIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEG 182


                  ....*.
gi 1352183975 175 NPARII 180
Cdd:TIGR01852 183 NRARLR 188
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-162 3.69e-09

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: 54.64  E-value: 3.69e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162
Cdd:COG1044   128 VIGDGVVIGPGVVI------------------GDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-162 9.05e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.60  E-value: 9.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162
Cdd:PRK00892  132 VIGDGVVIGAGAVI------------------GDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-162 1.09e-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: 52.41  E-value: 1.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162
Cdd:cd03352    21 VIGDGVVIGPGVVI------------------GDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
95-179 1.32e-08

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 52.79  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytaTHpiDPVARN-----SGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169
Cdd:PRK05289  107 RIGDNNLLMAYVHV---AH--DCVVGNhvilaNNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPY 181

                          90
                  ....*....|
gi 1352183975 170 VVVGGNPARI 179
Cdd:PRK05289  182 VLAEGNPARL 191
PRK10191 PRK10191
putative acyl transferase; Provisional
 121-179 3.87e-08

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 49.89  E-value: 3.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975 121 NSGAE-LGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARI 179
Cdd:PRK10191   84 NRGADnMACPH-IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
PLN02296 PLN02296
carbonate dehydratase
 86-183 4.10e-08

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 51.28  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  86 CVML-DVCPIRIG------DNCMlapgVHiytathpidpVARN--SGAELgkPVTIGNNVWIGGRAVINP---------- 146
Cdd:PLN02296   83 CVLRgDVNSISVGsgtniqDNSL----VH----------VAKTnlSGKVL--PTIIGDNVTIGHSAVLHGctvedeafvg 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1352183975 147 -GVTIGDNVV------VASGAVVTKD--VPDNVVVGGNPARIIKKL 183
Cdd:PLN02296  147 mGATLLDGVVvekhamVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-175 4.12e-07

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: 48.17  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTkdvpDNVVVGG 174
Cdd:cd03352     3 KIGENVSIGPNAVI------------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIY----EGCIIGD 60


                  .
gi 1352183975 175 N 175
Cdd:cd03352    61 R 61
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 103-173 4.51e-07

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: 48.48  E-value: 4.51e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352183975 103 APGVHiytATHPIDPVARnsgaelgkpvtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTkdvpDNVVVG 173
Cdd:COG1044    96 APGIH---PSAVIDPSAK-----------IGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIG----DGVVIG 148
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
129-158 4.94e-07

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 44.25  E-value: 4.94e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1352183975 129 PVTIGNNVWIGGRAVINPGVTIGDNVVVAS 158
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 95-179 5.25e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.09  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174
Cdd:PRK12461  103 RIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAG 182


                  ....*
gi 1352183975 175 NPARI 179
Cdd:PRK12461  183 HPTNV 187
PLN02357 PLN02357
serine acetyltransferase
 132-180 5.55e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 48.34  E-value: 5.55e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1352183975 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 103-175 7.68e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.83  E-value: 7.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352183975 103 APGVHiytATHPIDPVARnsgaelgkpvtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTkdvpDNVVVGGN 175
Cdd:PRK00892  100 AAGIH---PSAVIDPSAK-----------IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIG----DGVKIGAD 154
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-182 9.11e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 48.00  E-value: 9.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
Cdd:PRK14360  393 IGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
PLN02739 PLN02739
serine acetyltransferase
 89-181 9.79e-07

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 47.72  E-value: 9.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  89 LDVCPI-RIGDNCMLAPGVHIYTATHPI--DPVARNSGAELG--------KPVTIGNNVWIGGRAVINPGVTIGDNVVVA 157
Cdd:PLN02739  206 IDIHPAaRIGKGILLDHGTGVVIGETAVigDRVSILHGVTLGgtgketgdRHPKIGDGALLGACVTILGNISIGAGAMVA 285

                          90       100
                  ....*....|....*....|....
gi 1352183975 158 SGAVVTKDVPDNVVVGGNPARIIK 181
Cdd:PLN02739  286 AGSLVLKDVPSHSMVAGNPAKLIG 309
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-172 1.35e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVP--DNVVV 172
Cdd:PRK00892  114 KIGEGVSIGPNAVI------------------GAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRigNRVII 175
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 131-169 1.55e-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: 46.26  E-value: 1.55e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1352183975 131 TIGNNVWIG-GRAVINPgVTIGDNVVVASGAVVTKDVPDN 169
Cdd:cd03353   146 VIGDNVFIGsNSQLVAP-VTIGDGATIAAGSTITKDVPPG 184
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 131-181 1.95e-06

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: 46.94  E-value: 1.95e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352183975 131 TIGNNVWIGGRAV-INPgVTIGDNVVVASGAVVTKDVPDN-VVVGGNPARIIK 181
Cdd:COG1207   396 VIGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPAGaLAIARARQRNIE 447
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
130-164 2.01e-06

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 42.81  E-value: 2.01e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1352183975 130 VTIGNNVWIGGRAVInpGVTIGDNVVVASGAVVTK 164
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 68-177 2.28e-06

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: 46.67  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  68 CDYGYNIFLGNNFFANFDCVmldvcpiRIGDNCMLAPGVHIytATHPI-DPVARNSGaelgkpVTIGNNVWIGGRAVINP 146
Cdd:TIGR02353 598 VKIGRGVYIDGTDLTERDLV-------TIGDDSTLNEGSVI--QTHLFeDRVMKSDT------VTIGDGATLGPGAIVLY 662

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1352183975 147 GVTIGDNVVVASGAVVTK--DVPDNVVVGGNPA 177
Cdd:TIGR02353 663 GVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 131-183 2.37e-06

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: 45.44  E-value: 2.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1352183975 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK--DVPDNVVVGGNPARIIKKL 183
Cdd:cd04745    80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIREL 134
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-181 3.17e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 46.39  E-value: 3.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-173 3.78e-06

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: 45.78  E-value: 3.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTkdvpDNVVVG 173
Cdd:COG1044   110 KIGEGVSIGPFAVI------------------GAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY----ERCVIG 166
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 130-175 8.57e-06

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: 44.32  E-value: 8.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1352183975 130 VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTkdvpDNVVVGGN 175
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIG----DGVVIGDD 43
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
95-162 1.18e-05

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 44.32  E-value: 1.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352183975  95 RIGDNCMLAPGVHIytathpidpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162
Cdd:PRK05289   16 KIGENVEIGPFCVI------------------GPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
PLN02694 PLN02694
serine O-acetyltransferase
 132-180 1.18e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 44.25  E-value: 1.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1352183975 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 96-177 1.26e-05

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 43.14  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  96 IGDNCMLAPGVHIYTATHPIDpvarnsgaelGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK----------- 164
Cdd:cd03350    52 IGKNVHLSAGAVIGGVLEPLQ----------ATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretge 121

                          90
                  ....*....|....*...
gi 1352183975 165 ----DVPDN-VVVGGNPA 177
Cdd:cd03350   122 iyygRVPPGsVVVAGSLP 139
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 113-162 1.59e-05

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.85  E-value: 1.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352183975 113 HP---IDPvarnsGAEL------------GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162
Cdd:COG1043     5 HPtaiVDP-----GAKLgenveigpfcviGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-171 2.84e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.56  E-value: 2.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1352183975 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVV 171
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-169 4.24e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.90  E-value: 4.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1352183975 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169
Cdd:PRK14354  395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPED 433
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-181 4.37e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 43.06  E-value: 4.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352183975 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPD-NVVVGGNPARIIK 181
Cdd:PRK14359  369 IIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKgSLAISRAPQKNIK 420
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-180 7.14e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.23  E-value: 7.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVP-DNVVVGGNPARII 180
Cdd:PRK14352  401 TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPpGALAVSEGPQRNI 451
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 113-180 8.16e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.93  E-value: 8.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352183975 113 HP---IDPVAR-NSGAELG------KPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDvPDNVVVGGNPARII 180
Cdd:PRK12461    3 HPtavIDPSAKlGSGVEIGpfavigANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE-PQDFTYKGEESRLE 79
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 124-173 1.20e-04

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: 40.85  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352183975 124 AELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVP--DNVVVG 173
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVihPNVTIY 53
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 113-162 1.44e-04

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: 40.88  E-value: 1.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352183975 113 HP---IDPvarnsGAELGK------------PVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162
Cdd:cd03351     3 HPtaiVDP-----GAKIGEnveigpfcvigpNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 96-166 1.78e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 38.38  E-value: 1.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352183975  96 IGDNCMLAPGVHIytaTHPIdpvarnsgaeLGKPVTIGNNVWIGGrAVINPGVTIGDNVVVASGAVVTKDV 166
Cdd:cd03356    19 IGDNVRIGDGVTI---TNSI----------LMDNVTIGANSVIVD-SIIGDNAVIGENVRVVNLCIIGDDV 75
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 129-182 2.21e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.90  E-value: 2.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352183975 129 PVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
Cdd:PRK14357  383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
113-163 2.55e-04

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.47  E-value: 2.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352183975 113 HP---IDPvarnsGAELGKpvtignNVWIGGRAVINPGVTIGDNVVVASGAVVT 163
Cdd:PRK05289    6 HPtaiVEP-----GAKIGE------NVEIGPFCVIGPNVVIGDGTVIGSHVVID 48
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 96-172 4.44e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.01  E-value: 4.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352183975  96 IGDNCMLAPGvhiyTATHPIDpvarnsGAELGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVV 172
Cdd:PRK09451  372 IGDNVNIGAG----TITCNYD------GANKFKTI-IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 93-175 5.06e-04

Gamma carbonic anhydrases (CA): Carbonic anhydrases 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 distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 38.76  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  93 PIRIGDNCMLAPGVHIytatHPIDPVArnsgaelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK-DVPDNVV 171
Cdd:cd00710    42 PIIIGANVNIQDGVVI----HALEGYS----------VWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNaKVGDNCV 107


                  ....
gi 1352183975 172 VGGN 175
Cdd:cd00710   108 IGHN 111
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 93-175 6.91e-04

Dynactin 6 (or subunit p27): 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 p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the 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: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 38.46  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  93 PIRIGDNCMLAPGVHIytaTHPIDPvarnsGAELGKPVTIGNNVW-----------------IGGRAVINPGVTIGDNVV 155
Cdd:cd04646    38 PIIIGENNIIEEQVTI---VNKKPK-----DPAEPKPMIIGSNNVfevgckcealkignnnvFESKSFVGKNVIITDGCI 109

                          90       100
                  ....*....|....*....|..
gi 1352183975 156 VASGAVVTKD--VPDNVVVGGN 175
Cdd:cd04646   110 IGAGCKLPSSeiLPENTVIYGA 131
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 96-183 1.13e-03

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 38.25  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  96 IGDNCMLAPGVHIYTATHPIdpvarnsGAelgKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK-----DV---- 166
Cdd:PRK11830  153 IGKNVHLSGGVGIGGVLEPL-------QA---NPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiyDRetge 222

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1352183975 167 -------PDNVVVGGN-----------PARIIKKL 183
Cdd:PRK11830  223 vhygrvpAGSVVVPGSlpskdggyslyCAVIVKKV 257
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 129-177 1.70e-03

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: 38.19  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352183975 129 PVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKD--VPDNVVVGGNPA 177
Cdd:TIGR02353 160 PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGERWHGSPA 210
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 95-179 2.41e-03

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: 37.70  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  95 RIGDNCMLApGVHIytathpIDPvAR---NSGAELGKPVTIGNNVWIGGRAVINPGVTIG-----DNVVVASGAVVTKDV 166
Cdd:COG1207   243 RIAERLMRA-GVTI------IDP-ATtyiDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGpnctlKDSTIGDGVVIKYSV 314

                          90
                  ....*....|...
gi 1352183975 167 PDNVVVGGNpARI 179
Cdd:COG1207   315 IEDAVVGAG-ATV 326
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-169 6.77e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.26  E-value: 6.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1352183975 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169
Cdd:PRK14355  400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPD 437
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 98-173 7.98e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 36.00  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  98 DNCMLAPGVHIYTATHPIDPVARNSgaelgkpVTIGNNVWIGgRAVINPGVTIGDNVVVASG----AVVTKD--VPDNVV 171
Cdd:PRK05293  307 EHSVLFQGVQVGEGSVVKDSVIMPG-------AKIGENVVIE-RAIIGENAVIGDGVIIGGGkeviTVIGENevIGVGTV 378


                  ..
gi 1352183975 172 VG 173
Cdd:PRK05293  379 IG 380
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 96-177 9.64e-03

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: 35.88  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352183975  96 IGDNCMLAPGVHIYTATHpidpvarNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVG-- 173
Cdd:TIGR02353 375 IGEETFIADGLLMGNARL-------SGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGwl 447


                  ....
gi 1352183975 174 GNPA 177
Cdd:TIGR02353 448 GSPP 451
 
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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