NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2323452076|ref|WP_264319707|]
View 

acetyltransferase [Zarconia navalis]

Protein Classification

acetyltransferase( domain architecture ID 11497165)

acetyltransferase similar to Caulobacter vibrioides GDP-perosamine N-acetyltransferase that catalyzes the transfer of an acetyl residue from acetyl-CoA onto GDP-perosamine to form GDP-N-acetyl-perosamine; belongs to the transferase hexapeptide repeat family

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-207 2.07e-80

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: 238.55  E-value: 2.07e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   5 IIVLGGGGHGKVLIDALHRQGHQVLGITERNVREDSPSVLGIPILGGDDIVLQYPPDRIKLVNALGSvssLSKRQQLFEK 84
Cdd:TIGR03570   2 LVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGD---NKLRRRLVEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  85 FKRSGYHFLSVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQ 164
Cdd:TIGR03570  79 LKAKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2323452076 165 GSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPA 207
Cdd:TIGR03570 159 GVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-207 2.07e-80

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: 238.55  E-value: 2.07e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   5 IIVLGGGGHGKVLIDALHRQGHQVLGITERNVREDSPSVLGIPILGGDDIVLQYPPDRIKLVNALGSvssLSKRQQLFEK 84
Cdd:TIGR03570   2 LVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGD---NKLRRRLVEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  85 FKRSGYHFLSVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQ 164
Cdd:TIGR03570  79 LKAKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2323452076 165 GSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPA 207
Cdd:TIGR03570 159 GVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 7-206 1.35e-70

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: 213.50  E-value: 1.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   7 VLGGGGHGKVLIDALHRQ-GHQVLGITERNVREDSPSVLGIPIlGGDDIVLQYPPDRIKLVNALGSVSslsKRQQLFEKF 85
Cdd:cd03360     1 IIGAGGHARVVADILEADsGYEVVGFLDDDPELKGTEGLGLPV-GLDELLLLYPPPDDEFVVAIGDNK---LRRKLAEKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  86 KRSGYHFLSVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQG 165
Cdd:cd03360    77 LAAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2323452076 166 SHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIP 206
Cdd:cd03360   157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
105-212 1.06e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 86.46  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 105 DAQLSEGVQIMAGAVIQ-AGASIGENTIVNTRAVVD--HDCEIAAHVHLAPGVVL----------------SGSVKIGQG 165
Cdd:COG0110     8 GARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2323452076 166 SHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVKR 212
Cdd:COG0110    88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-175 9.57e-17

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 77.10  E-value: 9.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGAtVI 175
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGA-VI 181
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 5-85 2.01e-06

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 44.09  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   5 IIVLGGGGHGKVLIDALHRQG-HQVLGITERNVREdspSVLGIPILGGDDIVL-QYPPDRIKLVNALGSVsslSKRQQLF 82
Cdd:pfam17836   2 LIIIGAGGHGKVVADIIEAMGeYEIIGFLDDNKKT---EVNGYPVLGGDIDLLaSLSPDEYDVVIAIGNN---KVRKKIA 75


                  ...
gi 2323452076  83 EKF 85
Cdd:pfam17836  76 EKL 78
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-207 2.07e-80

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: 238.55  E-value: 2.07e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   5 IIVLGGGGHGKVLIDALHRQGHQVLGITERNVREDSPSVLGIPILGGDDIVLQYPPDRIKLVNALGSvssLSKRQQLFEK 84
Cdd:TIGR03570   2 LVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGD---NKLRRRLVEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  85 FKRSGYHFLSVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQ 164
Cdd:TIGR03570  79 LKAKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2323452076 165 GSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPA 207
Cdd:TIGR03570 159 GVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 7-206 1.35e-70

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: 213.50  E-value: 1.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   7 VLGGGGHGKVLIDALHRQ-GHQVLGITERNVREDSPSVLGIPIlGGDDIVLQYPPDRIKLVNALGSVSslsKRQQLFEKF 85
Cdd:cd03360     1 IIGAGGHARVVADILEADsGYEVVGFLDDDPELKGTEGLGLPV-GLDELLLLYPPPDDEFVVAIGDNK---LRRKLAEKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  86 KRSGYHFLSVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQG 165
Cdd:cd03360    77 LAAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2323452076 166 SHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIP 206
Cdd:cd03360   157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
105-212 1.06e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 86.46  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 105 DAQLSEGVQIMAGAVIQ-AGASIGENTIVNTRAVVD--HDCEIAAHVHLAPGVVL----------------SGSVKIGQG 165
Cdd:COG0110     8 GARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2323452076 166 SHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVKR 212
Cdd:COG0110    88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 110-211 2.80e-18

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: 76.77  E-value: 2.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 110 EGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLS---------------GSVKIGQGSHIGTGATV 174
Cdd:cd03358     3 DNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTndlyprskiyrkwelKGTTVKRGASIGANATI 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2323452076 175 IQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVK 211
Cdd:cd03358    83 LPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-175 9.57e-17

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 77.10  E-value: 9.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGAtVI 175
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGA-VI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 96-192 3.62e-16

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: 75.44  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIvntravvdhdceIAAHVHLAPGVVlsgsvkIGQGSHIGTGATVI 175
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVV------------IGPGVVIGDGVV------IGDDCVLHPNVTIY 160

                          90
                  ....*....|....*..
gi 2323452076 176 QEIQIGMNSLVGAGAVV 192
Cdd:COG1044   161 ERCVIGDRVIIHSGAVI 177
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 96-211 7.99e-15

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 69.29  E-value: 7.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGAS---IGENTIVNTRAVV----DHDCEIAAHVHLAPGVVLSGSvKIGQGSHI 168
Cdd:COG0663    19 VAPTAVVIGDVTIGEDVSVWPGAVLRGDVGpirIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHGC-TIGDNVLI 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2323452076 169 GTGATVIQEIQIGMNSLVGAGAVVV--RDIPPDTKVLGIPAREVK 211
Cdd:COG0663    98 GMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVR 142
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 96-208 2.34e-14

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: 69.66  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVD------------------------------------ 139
Cdd:COG1043     4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEgpttigknnrifpfasigeepqdlkykgeptrleig 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 140 -------------------------------------HDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGM 182
Cdd:COG1043    84 dnntirefvtihrgtvqgggvtrigddnllmayvhvaHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGA 163

                         170       180
                  ....*....|....*....|....*.
gi 2323452076 183 NSLVGAGAVVVRDIPPDTKVLGIPAR 208
Cdd:COG1043   164 HAMVGGGSGVVKDVPPYVLAAGNPAR 189
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 123-212 2.42e-14

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: 67.80  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 123 GASIGEntivntRAVVDH--------DCEIAAHVHLAPGVVLSGS--------VKIGQGSHIGTGATVIQEIQIGMNSLV 186
Cdd:COG1045    71 GATIGR------GFFIDHgtgvvigeTAVIGDNVTIYQGVTLGGTgkekgkrhPTIGDNVVIGAGAKILGPITIGDNAKI 144

                          90       100
                  ....*....|....*....|....*.
gi 2323452076 187 GAGAVVVRDIPPDTKVLGIPAREVKR 212
Cdd:COG1045   145 GANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 94-212 4.30e-14

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: 67.82  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIV---------------------------------------NT 134
Cdd:cd03352    26 VVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIhsgavigsdgfgfapdgggwvkipqlggviigddveigaNT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 135 ---RAVVD-----------------HDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVR 194
Cdd:cd03352   106 tidRGALGdtvigdgtkidnlvqiaHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTS 185

                         170
                  ....*....|....*...
gi 2323452076 195 DIPPDTKVLGIPAREVKR 212
Cdd:cd03352   186 IVPPGEYVSGTPAQPHRE 203
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 96-208 7.89e-14

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: 67.84  E-value: 7.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVD------------------------------------ 139
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDgpttigknnrifpfasigeapqdlkykgeptrleig 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 140 -------------------------------------HDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGM 182
Cdd:cd03351    82 dnntirefvtihrgtaqgggvtrignnnllmayvhvaHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                         170       180
                  ....*....|....*....|....*.
gi 2323452076 183 NSLVGAGAVVVRDIPPDTKVLGIPAR 208
Cdd:cd03351   162 HAMVGGGSGVVQDVPPYVIAAGNRAR 187
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
94-208 3.52e-13

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 66.28  E-value: 3.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVD---------------------------------- 139
Cdd:PRK05289    3 AKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDghttigknnrifpfasigedpqdlkykgeptrlv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 140 ---------------------------------------HDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQI 180
Cdd:PRK05289   83 igdnntirefvtinrgtvqgggvtrigdnnllmayvhvaHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRI 162

                         170       180
                  ....*....|....*....|....*...
gi 2323452076 181 GMNSLVGAGAVVVRDIPPDTKVLGIPAR 208
Cdd:PRK05289  163 GAHAMVGGMSGVSQDVPPYVLAEGNPAR 190
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 96-211 5.27e-13

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: 63.97  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGAS---IGENTIVNTRAVV----DHDCEIAAHVHLAPGVVLSGSvKIGQGSHI 168
Cdd:cd04645     8 IAPNATVIGDVTLGEGSSVWFGAVLRGDVNpirIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGC-TIGDNCLI 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2323452076 169 GTGATVIQEIQIGMNSLVGAGAVVV--RDIPPDTKVLGIPAREVK 211
Cdd:cd04645    87 GMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVR 131
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 94-211 7.09e-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: 66.19  E-value: 7.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIV----------------------------------------N 133
Cdd:COG1044   133 VVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIhsgavigadgfgfapdedggwvkipqlgrvvigddveigaN 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 134 T---RAVVD-----------------HDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVV 193
Cdd:COG1044   213 TtidRGALGdtvigdgtkidnlvqiaHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVT 292

                         170
                  ....*....|....*...
gi 2323452076 194 RDIPPDTKVLGIPAREVK 211
Cdd:COG1044   293 KSIPEGGVYSGSPAQPHR 310
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 110-210 8.46e-13

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: 62.09  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 110 EGVQIMAGAVIQAGA--SIGENTIVNTRA-VVDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLV 186
Cdd:cd04647     6 DNVYIGPGCVISAGGgiTIGDNVLIGPNVtIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVV 85

                          90       100
                  ....*....|....*....|....
gi 2323452076 187 GAGAVVVRDIPPDTKVLGIPAREV 210
Cdd:cd04647    86 GAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 125-208 4.98e-12

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: 61.67  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 125 SIGENTIVNTRAVVDHDCE--IAAHVHLAPGVVL------------------SGSVKIGQGSHIGTGATVIQEIQIGMNS 184
Cdd:cd03357    64 HIGDNFYANFNCTILDVAPvtIGDNVLIGPNVQIytaghpldpeernrgleyAKPITIGDNVWIGGGVIILPGVTIGDNS 143

                          90       100
                  ....*....|....*....|....
gi 2323452076 185 LVGAGAVVVRDIPPDTKVLGIPAR 208
Cdd:cd03357   144 VIGAGSVVTKDIPANVVAAGNPAR 167
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 117-206 5.27e-12

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: 59.76  E-value: 5.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 117 GAVIQAGASIGEN-TIVNTRAVVDH-DCEIAAHVHLAPGVVLSGSVKIGQGSH--------IGTGATVIQEIQIGMNSLV 186
Cdd:cd03354     2 GIDIHPGAKIGPGlFIDHGTGIVIGeTAVIGDNCTIYQGVTLGGKGKGGGKRHptigdnvvIGAGAKILGNITIGDNVKI 81

                          90       100
                  ....*....|....*....|
gi 2323452076 187 GAGAVVVRDIPPDTKVLGIP 206
Cdd:cd03354    82 GANAVVTKDVPANSTVVGVP 101
PLN02694 PLN02694
serine O-acetyltransferase
 123-210 4.48e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 60.81  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 123 GASIGENtivntrAVVDHDCEIAAHVHLAPGVVLSGS--VKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDT 200
Cdd:PLN02694  180 GVVIGET------AVIGNNVSILHHVTLGGTGKACGDrhPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRT 253

                          90
                  ....*....|
gi 2323452076 201 KVLGIPAREV 210
Cdd:PLN02694  254 TAVGNPARLV 263
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-200 6.67e-11

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 60.91  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPGAIVAADAQLSEGVQIMAGAVIQaGASIGENTIVNTRAVVDhDCEIAAHV------HLAPGVVLSGSVKIG---- 163
Cdd:PRK14355  275 TTIYPGVCISGDTRIGEGCTIEQGVVIK-GCRIGDDVTVKAGSVLE-DSVVGDDVaigpmaHLRPGTELSAHVKIGnfve 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 164 ----------QGSH--------------IGTGA------------TVIQE-------------IQIGMNSLVGAGAVVVR 194
Cdd:PRK14355  353 tkkivmgegsKASHltylgdatigrnvnIGCGTitcnydgvkkhrTVIEDdvfvgsdvqfvapVTVGRNSLIAAGTTVTK 432


                  ....*.
gi 2323452076 195 DIPPDT 200
Cdd:PRK14355  433 DVPPDS 438
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 96-197 1.14e-10

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: 57.39  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGS--------VKIGQGSH 167
Cdd:cd03350     4 VPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVleplqatpVIIEDDVF 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 2323452076 168 IGTGATVIQEIQIGMNSLVGAGAVVVRDIP 197
Cdd:cd03350    84 IGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
cysE PRK11132
serine acetyltransferase; Provisional
 96-212 1.57e-10

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 58.94  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVaadaqlseGVQIMAGAViqAGASIGENtivntrAVVDHDceiaahVHLAPGVVLSGS--------VKIGQGSH 167
Cdd:PRK11132  144 IHPAAKI--------GRGIMLDHA--TGIVIGET------AVIEND------VSILQSVTLGGTgktsgdrhPKIREGVM 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2323452076 168 IGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVKR 212
Cdd:PRK11132  202 IGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
PRK10502 PRK10502
putative acyl transferase; Provisional
 126-211 1.75e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 57.65  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 126 IGENTIVNTRAVVdhdcEIAAHVHLAPGVVL---------------SGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGA 190
Cdd:PRK10502   80 IGDDVWLYNLGEI----TIGAHCVISQKSYLctgshdysdphfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARS 155

                          90       100
                  ....*....|....*....|.
gi 2323452076 191 VVVRDIPPDTKVLGIPAREVK 211
Cdd:PRK10502  156 SVFKSLPANTICRGNPAVPIR 176
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-193 2.46e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.00  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  95 VIHPGAIVAadaqlsEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVL------------------ 156
Cdd:PRK00892  126 VIGAGVVIG------DGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgfandrggwvkip 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2323452076 157 -SGSVKIGQGSHIGT---------GATVIQE-------IQIGMNSLVGAGAVVV 193
Cdd:PRK00892  200 qLGRVIIGDDVEIGAnttidrgalDDTVIGEgvkidnlVQIAHNVVIGRHTAIA 253
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 105-174 4.32e-10

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: 57.03  E-value: 4.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 105 DAQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATV 174
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 126-212 7.52e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 56.17  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 126 IGENTIVNTRAVV--DHDCEIAAHVHLAPGVVLSGS------------------VKIGQGSHIGTGATVIQEIQIGMNSL 185
Cdd:PRK09527   78 IGRNFYANFNLTIvdDYTVTIGDNVLIAPNVTLSVTghpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTIGDNSV 157

                          90       100
                  ....*....|....*....|....*..
gi 2323452076 186 VGAGAVVVRDIPPDTKVLGIPAREVKR 212
Cdd:PRK09527  158 IGAGSVVTKDIPPNVVAAGVPCRVIRE 184
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 120-210 9.11e-10

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: 54.15  E-value: 9.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 120 IQAGASIGENTIVNTRA--VVDHDCEIAAHVHLAPGV---------VLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVGA 188
Cdd:cd05825     6 IGDNSWIGEGVWIYNLApvTIGSDACISQGAYLCTGShdyrspafpLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGA 85

                          90       100
                  ....*....|....*....|..
gi 2323452076 189 GAVVVRDIPPDTKVLGIPAREV 210
Cdd:cd05825    86 RSVVVRDLPAWTVYAGNPAVPV 107
PLN02357 PLN02357
serine acetyltransferase
 120-208 2.47e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 56.04  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 120 IQAGASIGENTIVN--TRAVVDHDCEIAAHVHLAPGVVLSGS--------VKIGQGSHIGTGATVIQEIQIGMNSLVGAG 189
Cdd:PLN02357  229 IHPGAKIGQGILLDhaTGVVIGETAVVGNNVSILHNVTLGGTgkqsgdrhPKIGDGVLIGAGTCILGNITIGEGAKIGAG 308

                          90
                  ....*....|....*....
gi 2323452076 190 AVVVRDIPPDTKVLGIPAR 208
Cdd:PLN02357  309 SVVLKDVPPRTTAVGNPAR 327
PLN02739 PLN02739
serine acetyltransferase
 96-208 6.86e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 54.66  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAivaadaQLSEGVQIMAGAviqaGASIGENTIVNTRAVVDHdceiaahvhlapGVVLSGSVK--------IGQGSH 167
Cdd:PLN02739  208 IHPAA------RIGKGILLDHGT----GVVIGETAVIGDRVSILH------------GVTLGGTGKetgdrhpkIGDGAL 265

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2323452076 168 IGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAR 208
Cdd:PLN02739  266 LGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAK 306
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 94-212 8.33e-09

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: 52.76  E-value: 8.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPGAIVAADAQLSEGVQIMAGA---------VIQAGASIGENTIVNTRAvvDHDCEIAAHVHLAPGVVLSGSvKIGQ 164
Cdd:cd04745     7 SFVHPTAVLIGDVIIGKNCYIGPHAslrgdfgriVIRDGANVQDNCVIHGFP--GQDTVLEENGHIGHGAILHGC-TIGR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2323452076 165 GSHIGTGATVIQEIQIGMNSLVGAGAVVVR--DIPPDTKVLGIPAREVKR 212
Cdd:cd04745    84 NALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRE 133
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 96-198 9.04e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 53.87  E-value: 9.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTIVNTRAV-------------------------------------- 137
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVilgptrigknnkihqgavvgdepqdftykgeesrleig 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 138 ----------------------------------VDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMN 183
Cdd:PRK12461   82 drnviregvtihrgtkgggvtrigndnllmayshVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGAL 161

                         170
                  ....*....|....*
gi 2323452076 184 SLVGAGAVVVRDIPP 198
Cdd:PRK12461  162 AMMAGGSRISKDVPP 176
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 157-211 9.24e-09

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 52.16  E-value: 9.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2323452076 157 SGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVK 211
Cdd:cd03349    71 KGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 126-212 1.29e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 49.81  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 126 IGENTIVNTRAVVDHDCE--IAAHVHLAPGVVL-------------SGS-----VKIGQGSHIGTGATVIQEIQIGMNSL 185
Cdd:PRK10092   76 LGNNFYANFDCVMLDVCPirIGDNCMLAPGVHIytathpldpvarnSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVV 155

                          90       100
                  ....*....|....*....|....*..
gi 2323452076 186 VGAGAVVVRDIPPDTKVLGIPAREVKR 212
Cdd:PRK10092  156 VASGAVVTKDVPDNVVVGGNPARIIKK 182
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 95-204 1.29e-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: 49.73  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  95 VIHPGAIVAADAQLSEGVQIMAGAVIQaGASIGENTIVN-----TRAVVDHDCEIAAHVHLAPGVVLSGSVKIG-----Q 164
Cdd:cd03353    23 VIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKassviEGAVIGNGATVGPFAHLRPGTVLGEGVHIGnfveiK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 165 GSHIGTGA-----------------------------------TVIQE-------------IQIGMNSLVGAGAVVVRDI 196
Cdd:cd03353   102 KSTIGEGSkanhlsylgdaeigegvnigagtitcnydgvnkhrTVIGDnvfigsnsqlvapVTIGDGATIAAGSTITKDV 181


                  ....*...
gi 2323452076 197 PPDTKVLG 204
Cdd:cd03353   182 PPGALAIA 189
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-209 1.19e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 48.18  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHP-----GAIVAADAQLSEGVQIMAGAVIQAGASIG-----ENTIVNTRAVVDH-----DCEIAAHVHLAPGVV--- 155
Cdd:PRK14356  311 ATIHSfshleGAEVGDGCSVGPYARLRPGAVLEEGARVGnfvemKKAVLGKGAKANHltylgDAEIGAGANIGAGTItcn 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2323452076 156 LSGSVK----IGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTkvLGIpARE 209
Cdd:PRK14356  391 YDGVNKhrtvIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGS--LAI-ARG 445
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 105-211 1.55e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 46.79  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 105 DAQLSEGVQIMAGAVIQagasIGENTIVNTRA-VVDHDCEIAAHV------HLAPGV--VLSGSVKIGQGSHIGTGATVI 175
Cdd:PRK09677   71 NVQVNDYVHIACIESIT----IGRDTLIASKVfITDHNHGSFKHSddfsspNLPPDMrtLESSAVVIGQRVWIGENVTIL 146

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2323452076 176 QEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVK 211
Cdd:PRK09677  147 PGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 96-202 1.69e-06

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: 46.46  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  96 IHPGAIVAADAQLSEGVQIMAGAVIQA----GASIGENTIVNTRAVV----DHDCEIAAHVHLAPGVVLSGSVKIGQGSH 167
Cdd:cd00710    11 VHPTAVVIGDVIIGDNVFVGPGASIRAdegtPIIIGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIVHGPAYIGDNCF 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2323452076 168 IGTGATVIQEiQIGMNSLVGAGAVVV-RDIPPDTKV 202
Cdd:cd00710    91 IGFRSVVFNA-KVGDNCVIGHNAVVDgVEIPPGRYV 125
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 5-85 2.01e-06

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 44.09  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   5 IIVLGGGGHGKVLIDALHRQG-HQVLGITERNVREdspSVLGIPILGGDDIVL-QYPPDRIKLVNALGSVsslSKRQQLF 82
Cdd:pfam17836   2 LIIIGAGGHGKVVADIIEAMGeYEIIGFLDDNKKT---EVNGYPVLGGDIDLLaSLSPDEYDVVIAIGNN---KVRKKIA 75


                  ...
gi 2323452076  83 EKF 85
Cdd:pfam17836  76 EKL 78
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 95-199 4.94e-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: 46.17  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  95 VIHPGAIVAADAQLSEGVQIMAGAVIQaGASIGENTIVN----TRAVVDHDCEIAAHVHLAPGVVLSGSVKIG-----QG 165
Cdd:COG1207   274 VIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKysviEDAVVGAGATVGPFARLRPGTVLGEGVKIGnfvevKN 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 166 SHIGTGA-----------------------------------TVIQE-------------IQIGMNSLVGAGAVVVRDIP 197
Cdd:COG1207   353 STIGEGSkvnhlsyigdaeigegvnigagtitcnydgvnkhrTVIGDgafigsntnlvapVTIGDGATIGAGSTITKDVP 432


                  ..
gi 2323452076 198 PD 199
Cdd:COG1207   433 AG 434
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 112-192 8.01e-06

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 42.62  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 112 VQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAhvhlAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAV 191
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGA----ATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76


                  .
gi 2323452076 192 V 192
Cdd:cd00208    77 V 77
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 99-194 1.10e-05

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: 45.40  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  99 GAIVAADAQLSEGV----QIM-AGAVIQ---------AGAsigenTIVN-TRAVVDHDCEIAAHVHLAPGVVLSGSVKIG 163
Cdd:COG1207   214 AAVQPEDPWEVLGVndrvQLAeAERILQrriaerlmrAGV-----TIIDpATTYIDGDVEIGRDVVIDPNVILEGKTVIG 288

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2323452076 164 QGSHIGTGATVIqeiqigmNSLVGAGAVVVR 194
Cdd:COG1207   289 EGVVIGPNCTLK-------DSTIGDGVVIKY 312
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 95-211 2.35e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.08  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  95 VIHP-----GAIVAADAQLSEGVQIMAGAVIQAGASIG-----ENTIVNTRAVVDH-----DCEIAAHVHLAPGVVL--- 156
Cdd:PRK14353  294 VIHAfshleGAHVGEGAEVGPYARLRPGAELGEGAKVGnfvevKNAKLGEGAKVNHltyigDATIGAGANIGAGTITcny 373

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2323452076 157 SGSVK----IGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVK 211
Cdd:PRK14353  374 DGFNKhrteIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 95-204 8.05e-05

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: 41.54  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  95 VIHPGAIVAADAQLSEGVQIMAGAVIQAGASI---------GENTIVNTRAVVDHDCE----------IAAHVHLAPGVV 155
Cdd:cd04646     1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIiaeagpiiiGENNIIEEQVTIVNKKPkdpaepkpmiIGSNNVFEVGCK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2323452076 156 LSgSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRD--IPPDTKVLG 204
Cdd:cd04646    81 CE-ALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSeiLPENTVIYG 130
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 92-211 9.18e-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: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  92 FLSVIHPGAIVAADAQLSEGVQIMAGAVIQAGASIGENTI-VNTRAvvDH-----DCEIAAHVHLAPGVV---LSGSVK- 161
Cdd:PRK14357  305 EKSVIEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIgENTKA--QHltylgDATVGKNVNIGAGTItcnYDGKKKn 382

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2323452076 162 ---IGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLGIPAREVK 211
Cdd:PRK14357  383 ptfIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
PRK10191 PRK10191
putative acyl transferase; Provisional
 117-208 2.11e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 40.26  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 117 GAVIQAGASIGEN--------TIVNTRAVVDHDCEIAAHVHLAP-GVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVG 187
Cdd:PRK10191   41 GYEIQAAATIGRRftihhgyaVVINKNVVAGDDFTIRHGVTIGNrGADNMACPHIGNGVELGANVIILGDITIGNNVTVG 120

                          90       100
                  ....*....|....*....|.
gi 2323452076 188 AGAVVVRDIPPDTKVLGIPAR 208
Cdd:PRK10191  121 AGSVVLDSVPDNALVVGEKAR 141
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 104-193 4.92e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 104 ADAQLSEGVQIMAGAVIQAGASIGENTIV--NTR-------------------AVVDHDCEIAAHVHLAPGVVLSGSVKI 162
Cdd:PRK14354  264 ADVEIGSDTVIEPGVVIKGNTVIGEDCVIgpGSRivdstigdgvtitnsvieeSKVGDNVTVGPFAHLRPGSVIGEEVKI 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2323452076 163 G-----QGSHIGTGA-----TVIQEIQIGMNSLVGAGAVVV 193
Cdd:PRK14354  344 GnfveiKKSTIGEGTkvshlTYIGDAEVGENVNIGCGTITV 384
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 131-208 5.39e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.01  E-value: 5.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2323452076 131 IVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAvVVRDIPPDTKVLGIPAR 208
Cdd:PRK12461    1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGA-VVGDEPQDFTYKGEESR 77
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 130-192 7.38e-04

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: 38.94  E-value: 7.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2323452076 130 TIVNTRAV-VDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIqeiqigmNSLVGAGAVV 192
Cdd:cd03353     3 TLIDPETTyIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-------DSTIGDGVVI 59
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 106-191 8.12e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.73  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 106 AQLSEGVQIMAGAVIQAGASIGENTIVNTRAVVDHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGAtVIQEIQIGMNSL 185
Cdd:PRK14355  233 AQLAEAARVLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGV-VIKGCRIGDDVT 311


                  ....*.
gi 2323452076 186 VGAGAV 191
Cdd:PRK14355  312 VKAGSV 317
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-209 8.45e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.43  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPgAIVAADAQLSEGVQIMAGAVIQAGASIG-----ENTIVNTRAVVDH-----DCEIAAHVHLAPGVVLS---GSV 160
Cdd:PRK14354  312 SVIEE-SKVGDNVTVGPFAHLRPGSVIGEEVKIGnfveiKKSTIGEGTKVSHltyigDAEVGENVNIGCGTITVnydGKN 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2323452076 161 K----IGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTkvLGIpARE 209
Cdd:PRK14354  391 KfktiIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDA--LAI-ARA 440
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 94-192 9.02e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.47  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  94 SVIHPGAIVAADAQ---LSEGVQIMAGA-----VIQAGASIGENTIVNtRAVVdhdceiaahvhlAPGVVlsgsvkIGQG 165
Cdd:PRK05293  294 SLVVEGCVVYGTVEhsvLFQGVQVGEGSvvkdsVIMPGAKIGENVVIE-RAII------------GENAV------IGDG 354

                          90       100
                  ....*....|....*....|....*..
gi 2323452076 166 SHIGTGATVIQeiQIGMNSLVGAGAVV 192
Cdd:PRK05293  355 VIIGGGKEVIT--VIGENEVIGVGTVI 379
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 141-195 1.51e-03

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: 38.16  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2323452076 141 DCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRD 195
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEG 55
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 99-194 3.38e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.61  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  99 GAIVAADAQLSEG----VQIM-AGAV----IQAGASIGENTIVNTRAV-VDHDCEIAAHVHLAPGVVLSGSVKIGQGSHI 168
Cdd:PRK14352  219 GAHHADDSAEVAGvndrVQLAaLGAElnrrIVEAWMRAGVTIVDPATTwIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVV 298

                          90       100
                  ....*....|....*....|....*.
gi 2323452076 169 GTGATVIqeiqigmNSLVGAGAVVVR 194
Cdd:PRK14352  299 GPDTTLT-------DVTVGEGASVVR 317
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 126-212 4.39e-03

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: 36.39  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 126 IGENTIVNTRAVVdHDCEIAAHVHLAPGVVLSGSVKIGQGSHIGTGATVIQEiqigmnslvgagavvvRDIPPDTKVLGI 205
Cdd:cd04650    64 IGDYVTIGHNAVV-HGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPG----------------KEIPDYSLVLGV 126


                  ....*..
gi 2323452076 206 PAREVKR 212
Cdd:cd04650   127 PAKVVRK 133
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 143-192 4.40e-03

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: 36.24  E-value: 4.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2323452076 143 EIAAHVHLAPGVVLSGSVKIGQGSHIGTGATV---IQEIQIGMNSLVGAGAVV 192
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVL 53
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
 5-95 4.81e-03

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 35.67  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076   5 IIVLGGGGHGKVLIDALHRQ---GHQVLGITERNVREDSPSVLGIPILGGDD----IVLQYPPDRIkLVnALGSVSSlSK 77
Cdd:COG1086    24 VLIVGAGEAGRQLARALRRNpdlGYRVVGFVDDDPDKRGRRIEGVPVLGTLDdlpeLVRRLGVDEV-II-ALPSASR-ER 100

                          90
                  ....*....|....*...
gi 2323452076  78 RQQLFEKFKRSGYHFLSV 95
Cdd:COG1086   101 LRELLEQLEDLGVKVKIV 118
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 95-192 5.50e-03

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 37.27  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076  95 VIHPGAIVAADAQLSEGVQIMAGAVIqAGASIGENTIVNTRAV-----VDHDCEIAAHVHLAPGVVLSGSVKIG-----Q 164
Cdd:PRK14358  278 TIEPGVLLRGQTRVADGVTIGAYSVV-TDSVLHEGAVIKPHSVlegaeVGAGSDVGPFARLRPGTVLGEGVHIGnfvetK 356

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2323452076 165 GSHIGTGATV-----IQEIQIGMNSLVGAGAVV 192
Cdd:PRK14358  357 NARLDAGVKAghlayLGDVTIGAETNVGAGTIV 389
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 114-211 8.45e-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: 35.65  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 114 IMAGAVIQ---AGASIGENTIVNTRAVVDHDCEIAAhvhlapGVVLSGSVKIGQGSHIGTGaTVIQEIQIGMNSLVGAGA 190
Cdd:cd03359    30 IQSDVIIRgdlATVSIGRYCILSEGCVIRPPFKKFS------KGVAFFPLHIGDYVFIGEN-CVVNAAQIGSYVHIGKNC 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2323452076 191 V-----VVRD---------IPPDTKVL------GIPAREVK 211
Cdd:cd03359   103 VigrrcIIKDcvkildgtvVPPDTVIPpysvvsGRPARFIG 143
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-204 9.09e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.44  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323452076 102 VAADAQLSEGVQI------MAGAVIQAGASIG-----ENTIVNTRAVVDH-----DCEIAAHVHLAPGVVLSG------- 158
Cdd:PRK14360  310 VVSDSQIGDGVKIgpyahlRPEAQIGSNCRIGnfveiKKSQLGEGSKVNHlsyigDATLGEQVNIGAGTITANydgvkkh 389

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2323452076 159 SVKIGQGSHIGTGATVIQEIQIGMNSLVGAGAVVVRDIPPDTKVLG 204
Cdd:PRK14360  390 RTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA 435
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH