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Conserved domains on  [gi|1519576816|gb|AZB28259|]
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acyltransferase [Chryseobacterium balustinum]

Protein Classification

acyltransferase( domain architecture ID 10140306)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to Neisseria meningitidis polysialic acid O-acetyltransferase

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0120225
PubMed:  15500694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 76-185 1.59e-32

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: 112.94  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  76 KIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPYDDIHLPIErQNITTKPVYIGEGCKIYNNVVIMQGTKI 155
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIE-QGVTSAPIVIGDDVWIGANVVILPGVTI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519576816 156 GKHCTIGANSIVSGYFDDYCVIVGAPAKIV 185
Cdd:cd04647    80 GDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
 
Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 76-185 1.59e-32

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: 112.94  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  76 KIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPYDDIHLPIErQNITTKPVYIGEGCKIYNNVVIMQGTKI 155
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIE-QGVTSAPIVIGDDVWIGANVVILPGVTI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519576816 156 GKHCTIGANSIVSGYFDDYCVIVGAPAKIV 185
Cdd:cd04647    80 GDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 75-196 4.32e-31

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 111.89  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  75 PKIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHH-------PYDDIHLPIERQNITTKPVYIGEGCKIYNNV 147
Cdd:PRK09677   64 GKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgsfkhsdDFSSPNLPPDMRTLESSAVVIGQRVWIGENV 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519576816 148 VIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVKKYNSDTKNWE 196
Cdd:PRK09677  144 TILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETKLWE 192
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
48-193 1.58e-29

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 106.11  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  48 IILGDRVSIGNNARIEGvqhyedkkfdPKIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPYDDIHLPIER 127
Cdd:COG0110     9 ARIGDGVVIGPGVRIYG----------GNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519576816 128 qnitTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVKKYNSDTK 193
Cdd:COG0110    79 ----TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 47-182 3.51e-07

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 48.64  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  47 SIILGDRVSIGnnariEGVQhyedkkFDPKIILNDGVTIQQNIHLTCAESIE----IGENTAIAANVTITDihhpyddih 122
Cdd:TIGR03570  93 SAIVSPSASIG-----EGTV------IMAGAVINPDVRIGDNVIINTGAIVEhdcvIGDFVHIAPGVTLSG--------- 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816 123 lpierqnittkPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPA 182
Cdd:TIGR03570 153 -----------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
134-163 1.05e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.09  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1519576816 134 PVYIGEGCKIYNNVVIMQGTKIGKHCTIGA 163
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 76-185 1.59e-32

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: 112.94  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  76 KIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPYDDIHLPIErQNITTKPVYIGEGCKIYNNVVIMQGTKI 155
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIE-QGVTSAPIVIGDDVWIGANVVILPGVTI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519576816 156 GKHCTIGANSIVSGYFDDYCVIVGAPAKIV 185
Cdd:cd04647    80 GDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 75-196 4.32e-31

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 111.89  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  75 PKIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHH-------PYDDIHLPIERQNITTKPVYIGEGCKIYNNV 147
Cdd:PRK09677   64 GKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgsfkhsdDFSSPNLPPDMRTLESSAVVIGQRVWIGENV 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519576816 148 VIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVKKYNSDTKNWE 196
Cdd:PRK09677  144 TILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETKLWE 192
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
48-193 1.58e-29

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 106.11  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  48 IILGDRVSIGNNARIEGvqhyedkkfdPKIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPYDDIHLPIER 127
Cdd:COG0110     9 ARIGDGVVIGPGVRIYG----------GNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519576816 128 qnitTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVKKYNSDTK 193
Cdd:COG0110    79 ----TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 27-185 4.01e-17

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: 74.77  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  27 LFKKIGKYCVIINPLKITpesiiLGDRVSIGNNARIegvqhyedkkfdpkiilNDGVTIqqnihLTCAEsIEIGENTAIA 106
Cdd:cd03357    41 LFGSVGENVYIEPPFHCD-----YGYNIHIGDNFYA-----------------NFNCTI-----LDVAP-VTIGDNVLIG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816 107 ANVTITDIHHPYDdihlPIERQN--ITTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKI 184
Cdd:cd03357    93 PNVQIYTAGHPLD----PEERNRglEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARV 168


                  .
gi 1519576816 185 V 185
Cdd:cd03357   169 I 169
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 50-186 2.68e-13

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: 63.67  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  50 LGDRVSIGNNARIEGvqhyedkkfdpKIILNDGVTIQQNIHLTcaESIEIGENTAIAANVTITDIHHPYDDIHLPIErqn 129
Cdd:cd03358     1 IGDNCIIGTNVFIEN-----------DVKIGDNVKIQSNVSIY--EGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWE--- 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1519576816 130 itTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVK 186
Cdd:cd03358    65 --LKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 48-195 5.31e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 63.89  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  48 IILGDRVSIGNNARIEGvqhyeDkkFDPkIILNDGVTIQQN--IHLTCAESIEIGENTAIAANVTItdihhpyddiHlpi 125
Cdd:COG0663    29 VTIGEDVSVWPGAVLRG-----D--VGP-IRIGEGSNIQDGvvLHVDPGYPLTIGDDVTIGHGAIL----------H--- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519576816 126 erqnittkpvyigeGCKIYNNV------VIMQGTKIGKHCTIGANSIVSG--YFDDYCVIVGAPAKIVKKYNSDTKNW 195
Cdd:COG0663    88 --------------GCTIGDNVligmgaIVLDGAVIGDGSIVGAGALVTEgkVVPPGSLVVGSPAKVVRELTEEEIAF 151
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 46-195 5.76e-12

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 61.94  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  46 ESIILGDRVSIGNNARIEGVQHYEdkkFDPKIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPyddIHLPI 125
Cdd:PRK09527   48 ESLIKEMFATVGENAWVEPPVYFS---YGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHP---VHHEL 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519576816 126 ERQ-NITTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVKKYNSDTKNW 195
Cdd:PRK09527  122 RKNgEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQY 192
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 76-185 2.98e-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: 54.92  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  76 KIILNDGVTIQQNIHLTCAESIEIGENTAIAANVTITDIHHPYDDIHLPIerqniTTKPVYIGEGCKIYNNVVIMQGTKI 155
Cdd:cd05825     3 NLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPL-----ITAPIVIGDGAWVAAEAFVGPGVTI 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519576816 156 GKHCTIGANSIVSGYFDDYCVIVGAPAKIV 185
Cdd:cd05825    78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 48-187 1.03e-09

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: 54.73  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  48 IILGDRVSIGNNARIEGVQHYedkkfdpkIILNDGVTIQQN--IHLTCAESIEIGENTAIAANVTItdihhpyddihlpi 125
Cdd:cd04645    18 VTLGEGSSVWFGAVLRGDVNP--------IRIGERTNIQDGsvLHVDPGYPTIIGDNVTVGHGAVL-------------- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519576816 126 erqnittkpvyigEGCKIYNNV------VIMQGTKIGKHCTIGANSIV-------SGYfddycVIVGAPAKIVKK 187
Cdd:cd04645    76 -------------HGCTIGDNCligmgaIILDGAVIGKGSIVAAGSLVppgkvipPGS-----LVAGSPAKVVRE 132
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 48-195 2.28e-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: 53.91  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  48 IILGDRVSIGNNARIEGvqhyedkKFDPkIILNDGVTIQQN--IHLTCAESIEIGENTAIAANVTITDIHhpyddihlpi 125
Cdd:cd04745    19 VIIGKNCYIGPHASLRG-------DFGR-IVIRDGANVQDNcvIHGFPGQDTVLEENGHIGHGAILHGCT---------- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519576816 126 erqnittkpvyIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV-SGY-FDDYCVIVGAPAKIVKKYNSDTKNW 195
Cdd:cd04745    81 -----------IGRNALVGMNAVVMDGAVIGEESIVGAMAFVkAGTvIPPRSLIAGSPAKVIRELSDEEVAW 141
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 46-167 3.00e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.41  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  46 ESIILGDRVSIGNNARIEgvqhyedkkfdpkiilnDGVtiqqnihltcaesiEIGENTAIAANVTItdihhpYDDihlpi 125
Cdd:COG1044   107 PSAKIGEGVSIGPFAVIG-----------------AGV--------------VIGDGVVIGPGVVI------GDG----- 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1519576816 126 erqnittkpVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV 167
Cdd:COG1044   145 ---------VVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 97-187 4.89e-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: 52.55  E-value: 4.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  97 IEIGENTAIAANVTI-TDIHHPYDDI-HLPIERQN------------ITTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIG 162
Cdd:cd03349    22 LSIGKFCSIAPGVKIgLGGNHPTDWVsTYPFYIFGgeweddakfddwPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIA 101

                          90       100
                  ....*....|....*....|....*
gi 1519576816 163 ANSIVSGYFDDYCVIVGAPAKIVKK 187
Cdd:cd03349   102 AGAVVTKDVPPYAIVGGNPAKVIRY 126
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 97-187 3.29e-08

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 51.35  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  97 IEIGENTAIAANVTITDIHHPYDdihlPIERQNITT--KPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDY 174
Cdd:PRK10092   94 IRIGDNCMLAPGVHIYTATHPLD----PVARNSGAElgKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169

                          90
                  ....*....|...
gi 1519576816 175 CVIVGAPAKIVKK 187
Cdd:PRK10092  170 VVVGGNPARIIKK 182
PRK10502 PRK10502
putative acyl transferase; Provisional
 9-186 4.66e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 50.72  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816   9 LIFTGKWHRLKAvfWYRFLFK----KIGKYCVIINPLKIT-PESIILGDRVSIGNNARIEGVqhyedkkfdpkiilndgv 83
Cdd:PRK10502   30 TLFAWSPQPLYR--WRAFLLRlfgaKIGKGVVIRPSVRITyPWKLTIGDYAWIGDDVWLYNL------------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  84 tiqqnihltcaESIEIGENTAIAANVTITDIHHPYDDIHLpierqNITTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGA 163
Cdd:PRK10502   90 -----------GEITIGAHCVISQKSYLCTGSHDYSDPHF-----DLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGA 153

                         170       180
                  ....*....|....*....|...
gi 1519576816 164 NSIVSGYFDDYCVIVGAPAKIVK 186
Cdd:PRK10502  154 RSSVFKSLPANTICRGNPAVPIR 176
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 98-191 5.52e-08

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: 50.47  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  98 EIGENTAIAANVTITDIHHPYDDIHlPIERQNittkpVYIGEGCKIYNNVvimqgtKIGKHCTIGANSIVSGYFDDYCVI 177
Cdd:COG1045    93 VIGDNVTIYQGVTLGGTGKEKGKRH-PTIGDN-----VVIGAGAKILGPI------TIGDNAKIGANSVVLKDVPPGSTV 160

                          90
                  ....*....|....
gi 1519576816 178 VGAPAKIVKKYNSD 191
Cdd:COG1045   161 VGVPARIVKRKGSK 174
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 94-177 7.83e-08

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: 51.17  E-value: 7.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  94 AESIEIGENTAIAANVTItdihhpyddihlpieRQNittkpVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSgyfdD 173
Cdd:COG1044   106 DPSAKIGEGVSIGPFAVI---------------GAG-----VVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY----E 161


                  ....
gi 1519576816 174 YCVI 177
Cdd:COG1044   162 RCVI 165
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 47-182 3.51e-07

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 48.64  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  47 SIILGDRVSIGnnariEGVQhyedkkFDPKIILNDGVTIQQNIHLTCAESIE----IGENTAIAANVTITDihhpyddih 122
Cdd:TIGR03570  93 SAIVSPSASIG-----EGTV------IMAGAVINPDVRIGDNVIINTGAIVEhdcvIGDFVHIAPGVTLSG--------- 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816 123 lpierqnittkPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPA 182
Cdd:TIGR03570 153 -----------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 98-167 5.87e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 47.79  E-value: 5.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  98 EIGENTAIAANVTItdihhpYDDihlpierqnittkpVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV 167
Cdd:cd03352    21 VIGDGVVIGPGVVI------GDG--------------VVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 38-167 6.93e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.21  E-value: 6.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  38 INPLKITPESIILGDRVSIGNNARIEgvqhyedkkfdpkiilnDGVtiqqnihltcaesiEIGENTAIAANVTItdihhp 117
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIG-----------------AGV--------------VIGDGVVIGAGAVI------ 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519576816 118 YDDihlpierqnittkpVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV 167
Cdd:PRK00892  146 GDG--------------VKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 30-180 1.25e-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: 47.02  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  30 KIGKYCVIINPLKITPESIIlGDRVSIGNNARI--EGVQHYEDKKFDPKIILNDGVTIQQNIhltcaesiEIGENTAI-- 105
Cdd:cd03352    39 VIGDDCVIHPNVTIYEGCII-GDRVIIHSGAVIgsDGFGFAPDGGGWVKIPQLGGVIIGDDV--------EIGANTTIdr 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519576816 106 -AANVTItdihhpyddihlpierqnittkpvyIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGY--FDDYCVIVGA 180
Cdd:cd03352   110 gALGDTV-------------------------IGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSttIGDNVIIGGQ 162
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 30-180 1.47e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.44  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  30 KIGKYCVIINPLKITPESIIlGDRVSIGNNARI---------EGVQHYedkkfdpKIILNDGVTIQQNIhltcaesiEIG 100
Cdd:PRK00892  150 KIGADCRLHANVTIYHAVRI-GNRVIIHSGAVIgsdgfgfanDRGGWV-------KIPQLGRVIIGDDV--------EIG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816 101 ENTAI---AANVTItdihhpyddihlpierqnittkpvyIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSG--YFDDYC 175
Cdd:PRK00892  214 ANTTIdrgALDDTV-------------------------IGEGVKIDNLVQIAHNVVIGRHTAIAAQVGIAGstKIGRYC 268


                  ....*
gi 1519576816 176 VIVGA 180
Cdd:PRK00892  269 MIGGQ 273
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 95-197 2.05e-06

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: 45.64  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  95 ESIEIGENTAIAANVTItdihhpYDDIHLPIE-RQNITTKPVYIGEGCKIYNNV------VIMQGTKIGKHCTIGANSIV 167
Cdd:cd04650    38 DSIYIGKYSNVQENVSI------HTDHGYPTEiGDYVTIGHNAVVHGAKVGNYVivgmgaILLNGAKIGDHVIIGAGAVV 111

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1519576816 168 S--GYFDDYCVIVGAPAKIVKKYNSDTKNWEK 197
Cdd:cd04650   112 TpgKEIPDYSLVLGVPAKVVRKLTEEEIEWIK 143
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 96-167 2.20e-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: 46.25  E-value: 2.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519576816  96 SIEIGENTAIAANVTITdihhpyddihlpierqnittKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV 167
Cdd:cd03352     1 SAKIGENVSIGPNAVIG--------------------EGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI 52
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 98-181 2.45e-06

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 44.35  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  98 EIGENTAIAANVTITDIHHPYDDIHlpierqnittkPVyIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVI 177
Cdd:cd03354    30 VIGDNCTIYQGVTLGGKGKGGGKRH-----------PT-IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTV 97


                  ....
gi 1519576816 178 VGAP 181
Cdd:cd03354    98 VGVP 101
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 105-169 2.66e-06

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: 46.55  E-value: 2.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519576816 105 IAANVTItdihHPYDDIHlpierqnittKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSG 169
Cdd:COG1043    16 LGENVEI----GPFCVIG----------PDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGE 66
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 135-177 9.82e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 9.82e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1519576816 135 VYIGEGCKIYNNVVIMQGTKIGKHCTIGANSI----VSGYFDdyCVI 177
Cdd:PRK00892  125 AVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRlhanVTIYHA--VRI 169
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 37-170 1.40e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 44.24  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  37 IINPLKITPESIILGDRVSIGNNARIE-GVQHYEDKKFDPKIILNDGVTI---------------QQNIHLTCAES-IEI 99
Cdd:PRK12461    1 MIHPTAVIDPSAKLGSGVEIGPFAVIGaNVEIGDGTWIGPHAVILGPTRIgknnkihqgavvgdePQDFTYKGEESrLEI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519576816 100 GENTAIAANVTITDIHHPYDDIHlpIERQNITTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGY 170
Cdd:PRK12461   81 GDRNVIREGVTIHRGTKGGGVTR--IGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGN 149
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
105-169 1.77e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.93  E-value: 1.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519576816 105 IAANVTItdihHPYDDIHlpierqnittKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSG 169
Cdd:PRK05289   17 IGENVEI----GPFCVIG----------PNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGE 67
cysE PRK11132
serine acetyltransferase; Provisional
 84-191 1.94e-05

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 43.92  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  84 TIQQNIHLTCAESIEIGEnTAIAAN-------VTITDIHHPYDDIHlPIERQNittkpVYIGEGCKIYNNVvimqgtKIG 156
Cdd:PRK11132  149 KIGRGIMLDHATGIVIGE-TAVIENdvsilqsVTLGGTGKTSGDRH-PKIREG-----VMIGAGAKILGNI------EVG 215

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1519576816 157 KHCTIGANSIVSGYFDDYCVIVGAPAKIVKKYNSD 191
Cdd:PRK11132  216 RGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPESD 250
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 135-181 2.55e-05

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: 43.24  E-value: 2.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1519576816 135 VYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAP 181
Cdd:cd03360   151 VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 95-167 2.88e-05

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 40.70  E-value: 2.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519576816  95 ESIEIGENTAIAANVTITDIHHPYDDihlpierqnittKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV 167
Cdd:cd00208    17 GPVVIGDNVNIGPGAVIGAATGPNEK------------NPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 105-167 3.04e-05

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: 43.19  E-value: 3.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519576816 105 IAANVTItdihHPYDDIHlpierqnittKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIV 167
Cdd:cd03351    14 IGENVEI----GPFCVIG----------PNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 31-168 5.75e-05

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: 41.80  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  31 IGKYCVIINPLKITPeSIILGDRVSIGNNARIEGVqhyedkkfdpkiILNDGVTIQqniHLT-CAESIeIGENTAIAANV 109
Cdd:cd05636    38 IGKGCEIGPNAYIRG-YTVLGDGCVVGNSVEVKNS------------IIMDGTKVP---HLNyVGDSV-LGENVNLGAGT 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519576816 110 TITDIHHPYDDIHLPIERQNITTK----PVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVS 168
Cdd:cd05636   101 ITANLRFDDKPVKVRLKGERVDTGrrklGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 30-180 8.94e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  30 KIGKYCVIINPLKITPESIIlGDRVSIGNNARI----------EGVQHYedkkfdpKI------ILNDGVtiqqnihltc 93
Cdd:COG1044   146 VIGDDCVLHPNVTIYERCVI-GDRVIIHSGAVIgadgfgfapdEDGGWV-------KIpqlgrvVIGDDV---------- 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  94 aesiEIGENTAI---AANVTItdihhpyddihlpierqnittkpvyIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGY 170
Cdd:COG1044   208 ----EIGANTTIdrgALGDTV-------------------------IGDGTKIDNLVQIAHNVRIGEHTAIAAQVGIAGS 258

                         170
                  ....*....|..
gi 1519576816 171 --FDDYCVIVGA 180
Cdd:COG1044   259 tkIGDNVVIGGQ 270
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
134-163 1.05e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.09  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1519576816 134 PVYIGEGCKIYNNVVIMQGTKIGKHCTIGA 163
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 94-179 7.93e-04

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: 38.62  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  94 AESIEIGENTAIAANVTITdihhPYddihlpierqnittkpVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYfdd 173
Cdd:cd03360    94 SPSAVIGEGCVIMAGAVIN----PD----------------ARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGG--- 150


                  ....*.
gi 1519576816 174 ycVIVG 179
Cdd:cd03360   151 --VTIG 154
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 82-179 8.40e-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: 38.56  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  82 GVTIQQNIHLTCAESIEIGENTAIAANVTITDihhpyddihlpierqnittkPVYIGEGCKIYNNVVImQGTKIGKHCTI 161
Cdd:cd03353     1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEG--------------------KTVIGEDCVIGPNCVI-KDSTIGDGVVI 59

                          90
                  ....*....|....*...
gi 1519576816 162 GANSIVSGYFDDYCVIVG 179
Cdd:cd03353    60 KASSVIEGAVIGNGATVG 77
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 49-188 9.72e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.54  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  49 ILGDRVSIGNNARIE-GVqhyedkkFDPKIIlNDGVTIQQNIHLtcAESIEIGENTAIAANVTITDihhpyddihlpier 127
Cdd:cd03352    94 IIGDDVEIGANTTIDrGA-------LGDTVI-GDGTKIDNLVQI--AHNVRIGENCLIAAQVGIAG-------------- 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519576816 128 qniTTKpvyIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKIVKKY 188
Cdd:cd03352   150 ---STT---IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREW 204
PLN02694 PLN02694
serine O-acetyltransferase
 85-185 1.36e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 38.47  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  85 IQQNIHLTCAESIEIGENTAIAANVTItdIHHpyddIHLPIERQNITTKPVYIGEGCKIYNNVVIMQGTKIGKHCTIGAN 164
Cdd:PLN02694  169 IGKGILFDHATGVVIGETAVIGNNVSI--LHH----VTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAG 242

                          90       100
                  ....*....|....*....|.
gi 1519576816 165 SIVSGYFDDYCVIVGAPAKIV 185
Cdd:PLN02694  243 SVVLIDVPPRTTAVGNPARLV 263
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 31-156 4.18e-03

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: 36.92  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  31 IGKYCVIinplkitpesiilGDRVSIGNNARIEGvqhyedkkfdpkiilndGVTIQQNIhltcaesiEIGENTAIAANVT 110
Cdd:COG1044   117 IGPFAVI-------------GAGVVIGDGVVIGP-----------------GVVIGDGV--------VIGDDCVLHPNVT 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1519576816 111 ItdihhpyddihlpierqnittkpvyiGEGCKIYNNVVIMQGTKIG 156
Cdd:COG1044   159 I--------------------------YERCVIGDRVIIHSGAVIG 178
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 107-169 4.27e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 4.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519576816 107 ANVTITDIHHPYddihlpIERQnittkpVYIGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSG 169
Cdd:PRK14355  253 AGVTLIDPETTY------IDRG------VVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG 303
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 135-185 8.15e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 36.38  E-value: 8.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519576816 135 VYIGEGCKIyNNVVIMQGTKIGKHCTI-----GANSIVsgyfDDYCVIVGAPAKIV 185
Cdd:PRK05293  315 VQVGEGSVV-KDSVIMPGAKIGENVVIeraiiGENAVI----GDGVIIGGGKEVIT 365
PRK10191 PRK10191
putative acyl transferase; Provisional
 137-184 8.44e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 35.25  E-value: 8.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1519576816 137 IGEGCKIYNNVVIMQGTKIGKHCTIGANSIVSGYFDDYCVIVGAPAKI 184
Cdd:PRK10191   95 IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 135-166 8.55e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 36.16  E-value: 8.55e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1519576816 135 VYIGEGCKIYNNVVIMQGTKIGKHCTIGANSI 166
Cdd:COG1207   267 VEIGRDVVIDPNVILEGKTVIGEGVVIGPNCT 298
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 79-180 9.91e-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: 35.05  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519576816  79 LNDGVTIQQNIHL-TCAEsieIGENTAIAANVTITDIHHPyddihlpierqnITTKPVYIGEGCKIYNNVVIMQGTKIGK 157
Cdd:cd03350    34 VDEGTMVDSWATVgSCAQ---IGKNVHLSAGAVIGGVLEP------------LQATPVIIEDDVFIGANCEVVEGVIVGK 98

                          90       100
                  ....*....|....*....|...
gi 1519576816 158 HCTIGANSIVSGYFDDYCVIVGA 180
Cdd:cd03350    99 GAVLAAGVVLTQSTPIYDRETGE 121
 
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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