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Conserved domains on  [gi|446517371|ref|WP_000594717|]
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serine acetyltransferase [Escherichia coli]

Protein Classification

serine acetyltransferase( domain architecture ID 10129656)

serine acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 86-184 1.09e-40

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: 133.33  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  86 YGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNV 165
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILG-NITIGDNV 79

                         90
                 ....*....|....*....
gi 446517371 166 KIGAMSFIMDDVPDNCTYV 184
Cdd:cd03354   80 KIGANAVVTKDVPANSTVV 98
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 86-184 1.09e-40

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: 133.33  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  86 YGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNV 165
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILG-NITIGDNV 79

                         90
                 ....*....|....*....
gi 446517371 166 KIGAMSFIMDDVPDNCTYV 184
Cdd:cd03354   80 KIGANAVVTKDVPANSTVV 98
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 54-184 6.66e-30

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: 108.25  E-value: 6.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  54 LMWWRLANEMFisgNKKQRKCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVS 133
Cdd:COG1045   35 LALHRLAHWLW---KRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGK 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446517371 134 DSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:COG1045  112 EKGKRHPTIGDNVVIGAGAKILG-PITIGDNAKIGANSVVLKDVPPGSTVV 161
PLN02357 PLN02357
serine acetyltransferase
 51-184 1.71e-22

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 92.64  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  51 RGFLMWW--RLANEMFISGNKKqrkCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTI 128
Cdd:PLN02357 191 KGFLACQahRIAHKLWTQGRKI---LALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTL 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446517371 129 GEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:PLN02357 268 GGTGKQSGDRHPKIGDGVLIGAGTCILG-NITIGEGAKIGAGSVVLKDVPPRTTAV 322
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 94-184 4.83e-13

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: 64.44  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371   94 ARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGEKVSDSRDNYI----------VIGDNVDIGAHTCIIGlNVKIGS 163
Cdd:TIGR03570 100 ASIGEGTVI--MAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIapgvtlsggvVIGEGVFIGAGATIIQ-GVTIGA 176

                          90       100
                  ....*....|....*....|.
gi 446517371  164 NVKIGAMSFIMDDVPDNCTYV 184
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVV 197
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
140-169 9.96e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 9.96e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 446517371  140 IVIGDNVDIGAHTCIIGlNVKIGSNVKIGA 169
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGG-GVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 86-184 1.09e-40

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: 133.33  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  86 YGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNV 165
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILG-NITIGDNV 79

                         90
                 ....*....|....*....
gi 446517371 166 KIGAMSFIMDDVPDNCTYV 184
Cdd:cd03354   80 KIGANAVVTKDVPANSTVV 98
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 54-184 6.66e-30

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: 108.25  E-value: 6.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  54 LMWWRLANEMFisgNKKQRKCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVS 133
Cdd:COG1045   35 LALHRLAHWLW---KRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGK 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446517371 134 DSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:COG1045  112 EKGKRHPTIGDNVVIGAGAKILG-PITIGDNAKIGANSVVLKDVPPGSTVV 161
PLN02357 PLN02357
serine acetyltransferase
 51-184 1.71e-22

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 92.64  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  51 RGFLMWW--RLANEMFISGNKKqrkCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTI 128
Cdd:PLN02357 191 KGFLACQahRIAHKLWTQGRKI---LALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTL 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446517371 129 GEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:PLN02357 268 GGTGKQSGDRHPKIGDGVLIGAGTCILG-NITIGEGAKIGAGSVVLKDVPPRTTAV 322
PLN02694 PLN02694
serine O-acetyltransferase
 51-184 1.86e-18

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 80.84  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  51 RGFLMWW--RLANEMFisgNKKQRKCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTI 128
Cdd:PLN02694 125 KGFLACQahRVAHKLW---TQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTL 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446517371 129 GEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:PLN02694 202 GGTGKACGDRHPKIGDGVLIGAGATILG-NVKIGEGAKIGAGSVVLIDVPPRTTAV 256
PLN02739 PLN02739
serine acetyltransferase
 54-178 7.59e-16

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 74.30  E-value: 7.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  54 LMWWRLANEMFISGNKKqrkCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVS 133
Cdd:PLN02739 175 LQAYRVAHKLWKQGRKL---LALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGK 251

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446517371 134 DSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVP 178
Cdd:PLN02739 252 ETGDRHPKIGDGALLGACVTILG-NISIGAGAMVAAGSLVLKDVP 295
PRK10191 PRK10191
putative acyl transferase; Provisional
 86-191 2.11e-14

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 67.22  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  86 YGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTIGEKVSDSRdNYIVIGDNVDIGAHTCIIGlNVKIGSNV 165
Cdd:PRK10191  40 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNM-ACPHIGNGVELGANVIILG-DITIGNNV 117

                         90       100
                 ....*....|....*....|....*.
gi 446517371 166 KIGAMSFIMDDVPDNcTYVTRKESRV 191
Cdd:PRK10191 118 TVGAGSVVLDSVPDN-ALVVGEKARV 142
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 90-184 3.75e-14

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: 67.51  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  90 IGLGARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGEkvsDSR--DN-----------YIVIGDNVDIGAHTCIIG 156
Cdd:cd03360   93 VSPSAVIGEGCVI--MAGAVINPDARIGDNVIINTGAVIGH---DCVigDFvhiapgvvlsgGVTIGEGAFIGAGATIIQ 167

                         90       100
                 ....*....|....*....|....*...
gi 446517371 157 lNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:cd03360  168 -GVTIGAGAIIGAGAVVTKDVPDGSVVV 194
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 87-173 1.03e-13

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: 68.12  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  87 GCDIGLGARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGEK----VSDSRDNYI--------VIGDNVDIGAHTCI 154
Cdd:COG1044  138 GVVIGDGVVIGDDCVL--HPNVTIYERCVIGDRVIIHSGAVIGADgfgfAPDEDGGWVkipqlgrvVIGDDVEIGANTTI 215

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446517371 155 ---------IGLNVK------IGSNVKIGAMSFI 173
Cdd:COG1044  216 drgalgdtvIGDGTKidnlvqIAHNVRIGEHTAI 249
cysE PRK11132
serine acetyltransferase; Provisional
 51-182 1.05e-13

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 67.41  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  51 RGF--LMWWRLANEMFisgNKKQRKCAIKIKNALMERYGCDIGLGARIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTI 128
Cdd:PRK11132 106 KGFhaLQAYRIGHWLW---NQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTL 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446517371 129 GEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCT 182
Cdd:PRK11132 183 GGTGKTSGDRHPKIREGVMIGAGAKILG-NIEVGRGAKIGAGSVVLQPVPPHTT 235
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
81-184 2.05e-13

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 64.12  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  81 ALMERYGCDIGLGARIGKGLVLpHHAGIVIHGNVDIGENVIL--RQNTTIGEKVS------------DSRDNY------- 139
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIddPGGITIGDNVLigpgvtiltgnhPIDDPAtfplrtg 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446517371 140 -IVIGDNVDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:COG0110   81 pVTIGDDVWIGAG-ATILPGVTIGDGAVVGAGSVVTKDVPPYAIVA 125
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 87-169 2.38e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 67.09  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  87 GCDIGLGARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGekvSD------SRDNYI--------VIGDNVDIGAHT 152
Cdd:PRK00892 142 GAVIGDGVKIGADCRL--HANVTIYHAVRIGNRVIIHSGAVIG---SDgfgfanDRGGWVkipqlgrvIIGDDVEIGANT 216

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446517371 153 CI---------IGLNVK------IGSNVKIGA 169
Cdd:PRK00892 217 TIdrgalddtvIGEGVKidnlvqIAHNVVIGR 248
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 87-173 3.37e-13

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: 65.12  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  87 GCDIGLGARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGekvSD------SRDNYI--------VIGDNVDIGAHT 152
Cdd:cd03352   31 GVVIGDGVVIGDDCVI--HPNVTIYEGCIIGDRVIIHSGAVIG---SDgfgfapDGGGWVkipqlggvIIGDDVEIGANT 105

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446517371 153 CI---------IGLNVK------IGSNVKIGAMSFI 173
Cdd:cd03352  106 TIdrgalgdtvIGDGTKidnlvqIAHNVRIGENCLI 141
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 94-184 4.83e-13

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: 64.44  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371   94 ARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGEKVSDSRDNYI----------VIGDNVDIGAHTCIIGlNVKIGS 163
Cdd:TIGR03570 100 ASIGEGTVI--MAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIapgvtlsggvVIGEGVFIGAGATIIQ-GVTIGA 176

                          90       100
                  ....*....|....*....|.
gi 446517371  164 NVKIGAMSFIMDDVPDNCTYV 184
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVV 197
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 90-184 3.55e-12

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: 60.16  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  90 IGLGARIGKGLVLPHHAGIVIHGNVDIGENVIL-----RQNTTIGEKVSDSRDNYIVIGDNVDIGAHtCIIGLNVKIGSN 164
Cdd:cd04647    4 IGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIydhnhDIDDPERPIEQGVTSAPIVIGDDVWIGAN-VVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|
gi 446517371 165 VKIGAMSFIMDDVPDNCTYV 184
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVA 102
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 105-177 1.48e-10

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: 58.88  E-value: 1.48e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446517371 105 HAGIVIHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDV 177
Cdd:COG1044  100 HPSAVIDPSAKIGEGVSIGPFAVIGAGV--------VIGDGVVIGPG-VVIGDGVVIGDDCVLHPNVTIYERC 163
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 87-173 3.31e-10

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, 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. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 58.07  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371   87 GCDIGLGARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGEK-----VSDSRDNY-------IVIGDNVDIGAHTCI 154
Cdd:TIGR01853 133 GVVIGDDVVIGDGSRI--HPNVVIYERVQLGKNVIIHSGAVIGSDgfgyaHTANGGHVkipqigrVIIEDDVEIGANTTI 210

                          90       100       110
                  ....*....|....*....|....*....|....
gi 446517371  155 ---------IGLNVKI------GSNVKIGAMSFI 173
Cdd:TIGR01853 211 drgafddtiIGEGTKIdnlvqiAHNCRIGENCII 244
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 94-174 3.49e-10

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: 54.18  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  94 ARIGKGLVLPHHAgiVIHGNVDIGENVILRQNTTIGEKVSDSRDNYIVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFI 173
Cdd:cd00208    1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHG-GVKIGDNAVIGAGAVV 77


                 .
gi 446517371 174 M 174
Cdd:cd00208   78 T 78
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 86-184 5.57e-08

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: 50.11  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  86 YGCDIglgaRIGKGLVLPHHAGIVIHGNVDIGENVIlrqnttIGEKVS----------DSRDNY------IVIGDNVDIG 149
Cdd:cd03357   59 YGYNI----HIGDNFYANFNCTILDVAPVTIGDNVL------IGPNVQiytaghpldpEERNRGleyakpITIGDNVWIG 128

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446517371 150 AHTCIIGlNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:cd03357  129 GGVIILP-GVTIGDNSVIGAGSVVTKDIPANVVAA 162
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 94-172 8.95e-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: 50.10  E-value: 8.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  94 ARIGKGLVLphHAGIVIHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHT-----CIIGLNVKIGSNVKIG 168
Cdd:cd03352    2 AKIGENVSI--GPNAVIGEGVVIGDGVVIGPGVVIGDGV--------VIGDDCVIHPNVtiyegCIIGDRVIIHSGAVIG 71


                 ....
gi 446517371 169 AMSF 172
Cdd:cd03352   72 SDGF 75
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 90-169 1.15e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.52  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  90 IGLGARIGKGLVLPHHAgiVIHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGA-----HTCIIGLNVKIGSN 164
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNA--VIGAGVVIGDGVVIGAGAVIGDGV--------KIGADCRLHAnvtiyHAVRIGNRVIIHSG 178


                 ....*
gi 446517371 165 VKIGA 169
Cdd:PRK00892 179 AVIGS 183
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 86-192 2.73e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 49.54  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  86 YGCDIGLGARIGkglvlPH-HagivIHGNVDIGE-----NVILRQNTTIGEKVSDSRDNYI---VIGDNVDIGA------ 150
Cdd:PRK14360 312 SDSQIGDGVKIG-----PYaH----LRPEAQIGSncrigNFVEIKKSQLGEGSKVNHLSYIgdaTLGEQVNIGAgtitan 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371 151 ------HTCIIGLNVKIGSN------------VKIGAMSFIMDDVPDNCTYVTRKESRVI 192
Cdd:PRK14360 383 ydgvkkHRTVIGDRSKTGANsvlvapitlgedVTVAAGSTITKDVPDNSLAIARSRQVIK 442
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 88-168 3.87e-07

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: 48.19  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  88 CDIGLGARIGKGLVLPHhaGIVIHGNVDIGENVILRQNTTIGekvsDSrdnyiVIGDNVDIGAHT----CIIGLNVKIG- 162
Cdd:cd03353   10 TYIDGDVEIGVDVVIDP--GVILEGKTVIGEDCVIGPNCVIK----DS-----TIGDGVVIKASSviegAVIGNGATVGp 78

                         90
                 ....*....|....*..
gi 446517371 163 -----------SNVKIG 168
Cdd:cd03353   79 fahlrpgtvlgEGVHIG 95
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 105-177 5.35e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.60  E-value: 5.35e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446517371 105 HAGIVIHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHT-----CIIGLNVKIGSNVKIGAMSFIMDDV 177
Cdd:PRK00892 104 HPSAVIDPSAKIGEGVSIGPNAVIGAGV--------VIGDGVVIGAGAvigdgVKIGADCRLHANVTIYHAVRIGNRV 173
PRK10502 PRK10502
putative acyl transferase; Provisional
 93-192 6.23e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 47.64  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  93 GARIGKGLVLPHHAGI------VIHGNVDIGENVILRQ--NTTIGEKVSDSRDNY-------------------IVIGDN 145
Cdd:PRK10502  51 GAKIGKGVVIRPSVRItypwklTIGDYAWIGDDVWLYNlgEITIGAHCVISQKSYlctgshdysdphfdlntapIVIGEG 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446517371 146 VDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDVPDNCTYV----TRKESRVI 192
Cdd:PRK10502 131 CWLAAD-VFVAPGVTIGSGAVVGARSSVFKSLPANTICRgnpaVPIRPRVE 180
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 94-186 8.40e-07

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: 47.41  E-value: 8.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  94 ARIGKGLVLPHHAGIvihGNVDIGENVilrqN---TTI-----GEKVSDSrdnyiVIGDNVDIGAHTCIIGlNVKIGSNV 165
Cdd:cd03353  103 STIGEGSKANHLSYL---GDAEIGEGV----NigaGTItcnydGVNKHRT-----VIGDNVFIGSNSQLVA-PVTIGDGA 169

                         90       100
                 ....*....|....*....|.
gi 446517371 166 KIGAMSFIMDDVPDNCTYVTR 186
Cdd:cd03353  170 TIAAGSTITKDVPPGALAIAR 190
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 89-192 1.18e-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: 47.71  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  89 DIGLGARIGKGLVLphHAGIVIHGNVDIGENVI---------------------------------------LRQNTTIG 129
Cdd:COG1207  262 YIDGDVEIGRDVVI--DPNVILEGKTVIGEGVVigpnctlkdstigdgvvikysviedavvgagatvgpfarLRPGTVLG 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371 130 EKV--------------SDSRDN---YI---VIGDNVDIGA------------HTCIIGLNVKIGSN------VKIGAMS 171
Cdd:COG1207  340 EGVkignfvevknstigEGSKVNhlsYIgdaEIGEGVNIGAgtitcnydgvnkHRTVIGDGAFIGSNtnlvapVTIGDGA 419

                        170       180
                 ....*....|....*....|....*..
gi 446517371 172 F------IMDDVPDNCTYVTRKESRVI 192
Cdd:COG1207  420 TigagstITKDVPAGALAIARARQRNI 446
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 79-180 1.73e-06

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 46.54  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  79 KNALME-----RYGCDIglgaRIGKGLVLPHHAGIVIHGNVDIGENVILRQNTTI---GEKVSDS-RDN------YIVIG 143
Cdd:PRK09527  60 ENAWVEppvyfSYGSNI----HIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLsvtGHPVHHElRKNgemysfPITIG 135

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446517371 144 DNVDIGAHTcIIGLNVKIGSNVKIGAMSFIMDDVPDN 180
Cdd:PRK09527 136 NNVWIGSHV-VINPGVTIGDNSVIGAGSVVTKDIPPN 171
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 113-177 4.51e-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: 45.48  E-value: 4.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446517371 113 NVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDV 177
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGV--------VIGDGVVIGPG-VVIGDGVVIGDDCVIHPNVTIYEGC 56
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 141-182 1.12e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 1.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446517371 141 VIGDNVDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDVP--DNCT 182
Cdd:PRK00892 114 KIGEGVSIGPN-AVIGAGVVIGDGVVIGAGAVIGDGVKigADCR 156
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 110-173 1.35e-05

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: 43.95  E-value: 1.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446517371 110 IHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHTCIIglNVKIGSNVKIGAMSFI 173
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKT--------VIGEDCVIGPNCVIK--DSTIGDGVVIKASSVI 65
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-180 1.76e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.47  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  87 GCDIGLGARIGkglvlPH---HAGIVIHGNVDIGeNVILRQNTTIGEKVSDSRDNYI---VIGDNVDIGA---------- 150
Cdd:PRK14353 303 GAHVGEGAEVG-----PYarlRPGAELGEGAKVG-NFVEVKNAKLGEGAKVNHLTYIgdaTIGAGANIGAgtitcnydgf 376

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446517371 151 --HTCIIGLNVKIGSN------VKIG--AM----SFIMDDVPDN 180
Cdd:PRK14353 377 nkHRTEIGAGAFIGSNsalvapVTIGdgAYiasgSVITEDVPDD 420
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 87-184 1.90e-05

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: 42.10  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  87 GCDIGLGARIGKGLVLPHHAGIviHGNVDIGENVILRQNTTIGEKVSDSRDNY-------------IVIGDNVDIGAHtC 153
Cdd:cd03358    4 NCIIGTNVFIENDVKIGDNVKI--QSNVSIYEGVTIEDDVFIGPNVVFTNDLYprskiyrkwelkgTTVKRGASIGAN-A 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446517371 154 IIGLNVKIGSNVKIGAMSFIMDDVPDNCTYV 184
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVV 111
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 92-179 2.45e-05

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: 43.97  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371   92 LGARIGKGLVLpHHAGIVIHGNVDIGENVILRQNTTIGEKVSDS---RDNYIVIGDNVDIGAHTcIIGLNVKIGSNVKIG 168
Cdd:TIGR02353 111 LGAKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERgrlHTGPVTLGRDAFIGTRS-TLDIDTSIGDGAQLG 188

                          90
                  ....*....|...
gi 446517371  169 AMSFIMDD--VPD 179
Cdd:TIGR02353 189 HGSALQGGqsIPD 201
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 90-168 3.31e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 43.32  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  90 IGLGARIGKGLVLphhAGIVIHGNVdigENVILRQNTTIGE--KVSDSR-DNYIVIGDNVDIgaHTCIIGLNVKIGSNVK 166
Cdd:PRK05293 285 IAENAKVKNSLVV---EGCVVYGTV---EHSVLFQGVQVGEgsVVKDSViMPGAKIGENVVI--ERAIIGENAVIGDGVI 356


                 ..
gi 446517371 167 IG 168
Cdd:PRK05293 357 IG 358
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 141-196 6.16e-05

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: 42.01  E-value: 6.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446517371 141 VIGDNVDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDVP--DNCTYvtrkESRVIICEQ 196
Cdd:cd03352    3 KIGENVSIGPN-AVIGEGVVIGDGVVIGPGVVIGDGVVigDDCVI----HPNVTIYEG 55
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 142-177 6.73e-05

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: 40.56  E-value: 6.73e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446517371 142 IGDNVDIGAHT-----CIIGLNVKIGSNVKIGAMSFIMDDV 177
Cdd:cd03358    1 IGDNCIIGTNVfiendVKIGDNVKIQSNVSIYEGVTIEDDV 41
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-180 7.54e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.51  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  87 GCDIGLGAR-----IGKGLVLPHHAGI--VIHGNVDIGENVILRQNTTIGEKV----------SDSRDN-------YI-- 140
Cdd:PRK14354 289 DCVIGPGSRivdstIGDGVTITNSVIEesKVGDNVTVGPFAHLRPGSVIGEEVkignfveikkSTIGEGtkvshltYIgd 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446517371 141 -VIGDNVDIGA------------HTCIIGLNVKIGSN------VKIG------AMSFIMDDVPDN 180
Cdd:PRK14354 369 aEVGENVNIGCgtitvnydgknkFKTIIGDNAFIGCNsnlvapVTVGdnayiaAGSTITKDVPED 433
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 107-195 7.80e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.44  E-value: 7.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371 107 GIVIHGNVDIGeNVILRQNTTIGEKVSDSRDNYI---VIGDNVDIGAHT--C----------------IIGLN------V 159
Cdd:PRK14357 324 GTVLKKSVKIG-NFVEIKKSTIGENTKAQHLTYLgdaTVGKNVNIGAGTitCnydgkkknptfiedgaFIGSNsslvapV 402

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446517371 160 KIGSNVKIGAMSFIMDDVPDNCTYVTRkeSRVIICE 195
Cdd:PRK14357 403 RIGKGALIGAGSVITEDVPPYSLALGR--ARQIVKE 436
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-192 8.54e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.32  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  94 ARIGKGLVLPHHAGIvihGNVDIGENVilrqntTIGEKVSDSrdNY-------IVIGDNVDIGAHTCIIGlNVKIGSNVK 166
Cdd:PRK09451 353 ARLGKGSKAGHLTYL---GDAEIGDNV------NIGAGTITC--NYdgankfkTIIGDDVFVGSDTQLVA-PVTVGKGAT 420

                         90       100
                 ....*....|....*....|....*.
gi 446517371 167 IGAMSFIMDDVPDNCTYVTRKESRVI 192
Cdd:PRK09451 421 IGAGTTVTRDVAENELVISRVPQRHI 446
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 106-177 1.53e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 40.65  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446517371 106 AGIVIHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHT-----CIIGLNVKIGSNVKIGAmSFIMDDV 177
Cdd:cd05636   10 EGVTIKGPVWIGEGAIVRSGAYIEGPV--------IIGKGCEIGPNAyirgyTVLGDGCVVGNSVEVKN-SIIMDGT 77
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 118-168 1.98e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 38.98  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446517371 118 ENVILRQNTTIGE--KVSDSrdnyiVIGDNVDIGAHT----CIIGLNVKIGSNVKIG 168
Cdd:cd04651   27 ENSVLFRGVRVGSgsVVEDS-----VIMPNVGIGRNAvirrAIIDKNVVIPDGVVIG 78
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 109-168 3.73e-04

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: 40.00  E-value: 3.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371 109 VIHGNVDIGENVILRQNTTIGEKVsdsrdnyiVIGDNVDIGAHTCIIGlNVKIGSNVKIG 168
Cdd:COG1043    9 IVDPGAKLGENVEIGPFCVIGPDV--------EIGDGTVIGSHVVIEG-PTTIGKNNRIF 59
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-186 4.82e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.09  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  88 CDIGLGARIGKGlvlphhagiVIHGNVDiGENvilRQNTTIGEKVsdsrdnyiVIGDNVDIGAhtciiglNVKIGSNVKI 167
Cdd:PRK14356 374 AEIGAGANIGAG---------TITCNYD-GVN---KHRTVIGEGA--------FIGSNTALVA-------PVTIGDGALV 425

                         90
                 ....*....|....*....
gi 446517371 168 GAMSFIMDDVPDNCTYVTR 186
Cdd:PRK14356 426 GAGSVITKDVPDGSLAIAR 444
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 140-175 5.69e-04

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: 37.82  E-value: 5.69e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446517371 140 IVIGDNVDIGAHTCIIGLN-VKIGSNVKIGAMSFIMD 175
Cdd:cd04647    2 ISIGDNVYIGPGCVISAGGgITIGDNVLIGPNVTIYD 38
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 114-183 6.55e-04

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: 37.59  E-value: 6.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446517371 114 VDIGENVILRQNTTIGEKVSDSRDNY-------IVIGDNVDIGAHtCIIGLNVKIGSNVKIGAMSFIMDDVPDNCTY 183
Cdd:cd05825   24 VTIGSDACISQGAYLCTGSHDYRSPAfplitapIVIGDGAWVAAE-AFVGPGVTIGEGAVVGARSVVVRDLPAWTVY 99
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 141-169 7.32e-04

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: 39.23  E-value: 7.32e-04
                         10        20
                 ....*....|....*....|....*....
gi 446517371 141 VIGDNVDIGAHtCIIGLNVKIGSNVKIGA 169
Cdd:COG1043   15 KLGENVEIGPF-CVIGPDVEIGDGTVIGS 42
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-192 1.02e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 39.15  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  94 ARIGKGLVLPHHAGIvihGNVDIGENvilrqnTTIG--------EKVSDSRdnyIVIGDNVDIGAHTCIIGlNVKIGSNV 165
Cdd:PRK14352 358 ATIGRGTKVPHLTYV---GDADIGEH------SNIGassvfvnyDGVNKHR---TTIGSHVRTGSDTMFVA-PVTVGDGA 424

                         90       100
                 ....*....|....*....|....*..
gi 446517371 166 KIGAMSFIMDDVPDNCTYVTRKESRVI 192
Cdd:PRK14352 425 YTGAGTVIREDVPPGALAVSEGPQRNI 451
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
141-169 1.60e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.16  E-value: 1.60e-03
                         10        20
                 ....*....|....*....|....*....
gi 446517371 141 VIGDNVDIGAHtCIIGLNVKIGSNVKIGA 169
Cdd:PRK05289  16 KIGENVEIGPF-CVIGPNVVIGDGTVIGS 43
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 93-181 1.68e-03

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: 37.58  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  93 GARIGKGLVLPHHAGIVIHGNVDIGENVILR---QNTTIGE---------------KVSDSRDNY-IVIGDNVDIGAHTC 153
Cdd:cd03359    7 GNKVSRKSVICGSQNIVLNGKTIIQSDVIIRgdlATVSIGRycilsegcvirppfkKFSKGVAFFpLHIGDYVFIGENCV 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446517371 154 I----IGLNVKIGSNVKIGAMSFImddvPDNC 181
Cdd:cd03359   87 VnaaqIGSYVHIGKNCVIGRRCII----KDCV 114
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 141-169 1.72e-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: 38.18  E-value: 1.72e-03
                         10        20
                 ....*....|....*....|....*....
gi 446517371 141 VIGDNVDIGAHtCIIGLNVKIGSNVKIGA 169
Cdd:cd03351   13 KIGENVEIGPF-CVIGPNVEIGDGTVIGS 40
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
109-169 1.89e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.77  E-value: 1.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446517371 109 VIHGNVDIGENVilrqntTIGEkvsdsrdnYIVIGDNVDIGAHTcIIGLNVKIGSNVKIGA 169
Cdd:PRK05289  10 IVEPGAKIGENV------EIGP--------FCVIGPNVVIGDGT-VIGSHVVIDGHTTIGK 55
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 140-192 2.90e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 37.10  E-value: 2.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446517371 140 IVIGDNVDIGAHTcIIGLNVKIGSNVKIGAMSFIMDDVPDNCTyVTRKESRVI 192
Cdd:PRK10092 130 VTIGNNVWIGGRA-VINPGVTIGDNVVVASGAVVTKDVPDNVV-VGGNPARII 180
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 88-168 3.04e-03

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: 37.31  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  88 CDIGLGARIGKGLVLPHHAgiVIHGNVDIGENVILRQNTTIGEKVSDSR----DNYIVIGDNVDIG-------------- 149
Cdd:COG1043   26 CVIGPDVEIGDGTVIGSHV--VIEGPTTIGKNNRIFPFASIGEEPQDLKykgePTRLEIGDNNTIRefvtihrgtvqggg 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446517371 150 ----------------AHTCIIGLNVKIGSNVKIG 168
Cdd:COG1043  104 vtrigddnllmayvhvAHDCVVGNNVILANNATLA 138
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 109-169 3.10e-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: 37.41  E-value: 3.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446517371 109 VIHGNVDIGENVilrqntTIGEkvsdsrdnYIVIGDNVDIGAHtCIIGLNVKIGSNVKIGA 169
Cdd:cd03351    7 IVDPGAKIGENV------EIGP--------FCVIGPNVEIGDG-TVIGSHVVIDGPTTIGK 52
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 90-173 3.17e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 35.25  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  90 IGLGARIGKGLVLPHHagiVIHGNVDIGENVILRqNTTIGEKVsdsrdnyiVIGDNVDIgaHTCIIGLNVKIGSNVKIGA 169
Cdd:cd05787    2 IGRGTSIGEGTTIKNS---VIGRNCKIGKNVVID-NSYIWDDV--------TIEDGCTI--HHSIVADGAVIGKGCTIPP 67


                 ....
gi 446517371 170 MSFI 173
Cdd:cd05787   68 GSLI 71
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 90-173 3.33e-03

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: 36.20  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  90 IGLGARIGKGLVLPHHAgiVIHGNVDIGENVILRQNTTIGEKVSDSRDNYIVIGDNVDIGAHtCIIGLNVKIGSNVKIGA 169
Cdd:cd03350   28 VNIGAYVDEGTMVDSWA--TVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGAN-CEVVEGVIVGKGAVLAA 104


                 ....
gi 446517371 170 MSFI 173
Cdd:cd03350  105 GVVL 108
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 88-168 3.73e-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: 37.03  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  88 CDIGLGARIGKGLVLPHHAgiVIHGNVDIGENVILRQNTTIGEKVSDSR----DNYIVIGDNVDIG-------------- 149
Cdd:cd03351   24 CVIGPNVEIGDGTVIGSHV--VIDGPTTIGKNNRIFPFASIGEAPQDLKykgePTRLEIGDNNTIRefvtihrgtaqggg 101

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446517371 150 ----------------AHTCIIGLNVKIGSNVKIG 168
Cdd:cd03351  102 vtrignnnllmayvhvAHDCVIGNNVILANNATLA 136
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 103-164 3.94e-03

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: 36.42  E-value: 3.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446517371 103 PHHAGIVIHGNVDIGENVILrQNTTIGekvsdsrdNYIVIGDNVDIGaHTCIIGLNVKIGSN 164
Cdd:cd03359   68 VAFFPLHIGDYVFIGENCVV-NAAQIG--------SYVHIGKNCVIG-RRCIIKDCVKILDG 119
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 113-178 4.70e-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: 4.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446517371 113 NVDIGENVILRQNTTIGekvsdsrdNYIVIGDNVDIGAHTCIIGLnVKIGSNVKIGAMSFIMDDVP 178
Cdd:cd03351  120 DCVIGNNVILANNATLA--------GHVEIGDYAIIGGLSAVHQF-CRIGRHAMVGGGSGVVQDVP 176
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 109-177 6.80e-03

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: 34.14  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371 109 VIHGNVDIGE-----NVILRQNTTIGEKV--SDSrdnyiVIGDNVDIGAHT----CIIGLNVKIGSNVKIGAMSFIMDDV 177
Cdd:cd03356    1 LIGESTVIGEnaiikNSVIGDNVRIGDGVtiTNS-----ILMDNVTIGANSvivdSIIGDNAVIGENVRVVNLCIIGDDV 75
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 105-173 6.88e-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: 36.26  E-value: 6.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446517371 105 HAGIVIHGNVDIGENVIlrqnttIGEKVsdsrdnyiVIGDNVDIGAHTCIIGlNVKIGSNVKIGAMSFI 173
Cdd:cd03351    9 DPGAKIGENVEIGPFCV------IGPNV--------EIGDGTVIGSHVVIDG-PTTIGKNNRIFPFASI 62
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 110-167 7.58e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 36.35  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371 110 IHGNVDIGE------NVILRQNTTIGE--------KVSDSR--DNYIV---------IGDNVDIG--AH---TCIIGLNV 159
Cdd:PRK14354 262 IDADVEIGSdtviepGVVIKGNTVIGEdcvigpgsRIVDSTigDGVTItnsvieeskVGDNVTVGpfAHlrpGSVIGEEV 341


                 ....*...
gi 446517371 160 KIGSNVKI 167
Cdd:PRK14354 342 KIGNFVEI 349
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 141-182 8.16e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.09  E-value: 8.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446517371 141 VIGDNVDIGAHT----CIIGLNVKIGSNVKIGAmSFIMDDV--PDNCT 182
Cdd:cd05787    1 VIGRGTSIGEGTtiknSVIGRNCKIGKNVVIDN-SYIWDDVtiEDGCT 47
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 72-167 9.88e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 35.99  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446517371  72 RKCaiKIKNALmerygcdIGLGARIGKGLVLphhAGIVIHGNvDIGEnvilrqntTIGEKVSDSRDNYIVIGdnvdIGAH 151
Cdd:PLN02241 325 REC--KIEHSV-------VGLRSRIGEGVEI---EDTVMMGA-DYYE--------TEEEIASLLAEGKVPIG----IGEN 379

                         90       100
                 ....*....|....*....|
gi 446517371 152 T----CIIGLNVKIGSNVKI 167
Cdd:PLN02241 380 TkirnAIIDKNARIGKNVVI 399
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
140-169 9.96e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 9.96e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 446517371  140 IVIGDNVDIGAHTCIIGlNVKIGSNVKIGA 169
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGG-GVIIGDNVIIGA 30
 
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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