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Conserved domains on  [gi|496040759|ref|WP_008765266|]
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MULTISPECIES: DapH/DapD/GlmU-related protein [Bacteroides]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
75-195 1.95e-38

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 129.22  E-value: 1.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  75 GNFDIIGSTVVVLPdAKLILGSG-YINFHSKLHCFNHIEIGENVIISENVIIRDSdNHQITGGNSM---FAPVIIKDNAW 150
Cdd:COG0110   12 GDGVVIGPGVRIYG-GNITIGDNvYIGPGVTIDDPGGITIGDNVLIGPGVTILTG-NHPIDDPATFplrTGPVTIGDDVW 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496040759 151 IGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:COG0110   90 IGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
75-195 1.95e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 129.22  E-value: 1.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  75 GNFDIIGSTVVVLPdAKLILGSG-YINFHSKLHCFNHIEIGENVIISENVIIRDSdNHQITGGNSM---FAPVIIKDNAW 150
Cdd:COG0110   12 GDGVVIGPGVRIYG-GNITIGDNvYIGPGVTIDDPGGITIGDNVLIGPGVTILTG-NHPIDDPATFplrTGPVTIGDDVW 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496040759 151 IGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:COG0110   90 IGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 91-193 5.75e-36

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: 121.79  E-value: 5.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  91 KLILGSG-YINFHSKLHCFNHIEIGENVIISENVIIRDS-----DNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVG 164
Cdd:cd04647    1 NISIGDNvYIGPGCVISAGGGITIGDNVLIGPNVTIYDHnhdidDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 496040759 165 EGAIVAAGSVVTKDVPPHTIVAGVPARVI 193
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 56-195 2.91e-23

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 91.99  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  56 PSQEKGRlilhansELIVKGNFDIIGSTVVVLPDAKLILGSG-------YINFHSKLHCFNHIEIGENVIISENVIIRDS 128
Cdd:PRK09527  41 PSEVEKR-------ESLIKEMFATVGENAWVEPPVYFSYGSNihigrnfYANFNLTIVDDYTVTIGDNVLIAPNVTLSVT 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496040759 129 DN---HQITGGNSMFA-PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:PRK09527 114 GHpvhHELRKNGEMYSfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 79-190 1.96e-19

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 81.77  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759   79 IIGSTVVVLPDAklILGSG-YINFHSKLHCFnhIEIGENVIISENVIIrdsDNHQITGGNSMFAP-------VIIKDNAW 150
Cdd:TIGR03570  89 LIHPSAIVSPSA--SIGEGtVIMAGAVINPD--VRIGDNVIINTGAIV---EHDCVIGDFVHIAPgvtlsggVVIGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496040759  151 IGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPA 190
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
143-177 2.47e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.34  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 496040759  143 VIIKDNAWIGMSAIIlkGVTVGEGAIVAAGSVVTK 177
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
75-195 1.95e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 129.22  E-value: 1.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  75 GNFDIIGSTVVVLPdAKLILGSG-YINFHSKLHCFNHIEIGENVIISENVIIRDSdNHQITGGNSM---FAPVIIKDNAW 150
Cdd:COG0110   12 GDGVVIGPGVRIYG-GNITIGDNvYIGPGVTIDDPGGITIGDNVLIGPGVTILTG-NHPIDDPATFplrTGPVTIGDDVW 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496040759 151 IGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:COG0110   90 IGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 91-193 5.75e-36

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: 121.79  E-value: 5.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  91 KLILGSG-YINFHSKLHCFNHIEIGENVIISENVIIRDS-----DNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVG 164
Cdd:cd04647    1 NISIGDNvYIGPGCVISAGGGITIGDNVLIGPNVTIYDHnhdidDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 496040759 165 EGAIVAAGSVVTKDVPPHTIVAGVPARVI 193
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 98-195 1.05e-28

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: 104.55  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  98 YINFHSKLHCFNHIEIGENVIISENVIIRDSDNHQITGGNSMF--------------------APVIIKDNAWIGMSAII 157
Cdd:cd03349    9 YGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGNHPTDWVSTYPfyifggeweddakfddwpskGDVIIGNDVWIGHGATI 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496040759 158 LKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:cd03349   89 LPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 110-193 4.39e-28

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: 103.66  E-value: 4.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 110 HIEIGENVIISENVIIrdSDNHQIT-GGNSMFAP-------------------------VIIKDNAWIGMSAIILKGVTV 163
Cdd:cd03357   62 NIHIGDNFYANFNCTI--LDVAPVTiGDNVLIGPnvqiytaghpldpeernrgleyakpITIGDNVWIGGGVIILPGVTI 139

                         90       100       110
                 ....*....|....*....|....*....|
gi 496040759 164 GEGAIVAAGSVVTKDVPPHTIVAGVPARVI 193
Cdd:cd03357  140 GDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 79-194 3.10e-24

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 92.18  E-value: 3.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  79 IIGSTVVVLPDAKLilGSgYINFHSKLHCFNHIEIGENVIISENVIIRDsDNH--QITGGNSMFAPVIIKDNAWIGMSAI 156
Cdd:cd03358    6 IIGTNVFIENDVKI--GD-NVKIQSNVSIYEGVTIEDDVFIGPNVVFTN-DLYprSKIYRKWELKGTTVKRGASIGANAT 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496040759 157 ILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIK 194
Cdd:cd03358   82 ILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 56-195 2.91e-23

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 91.99  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  56 PSQEKGRlilhansELIVKGNFDIIGSTVVVLPDAKLILGSG-------YINFHSKLHCFNHIEIGENVIISENVIIRDS 128
Cdd:PRK09527  41 PSEVEKR-------ESLIKEMFATVGENAWVEPPVYFSYGSNihigrnfYANFNLTIVDDYTVTIGDNVLIAPNVTLSVT 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496040759 129 DN---HQITGGNSMFA-PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:PRK09527 114 GHpvhHELRKNGEMYSfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 94-195 1.19e-20

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 84.48  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  94 LGSG-YINFHSKLHCFNHIEIGENVIISENVIIRDS----DNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAI 168
Cdd:PRK10092  76 LGNNfYANFDCVMLDVCPIRIGDNCMLAPGVHIYTAthplDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVV 155

                         90       100
                 ....*....|....*....|....*..
gi 496040759 169 VAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:PRK10092 156 VASGAVVTKDVPDNVVVGGNPARIIKK 182
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 113-196 2.05e-20

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 83.59  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIrdsdNHQIT-GGNSMFA----PVIiKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAG 187
Cdd:COG1045   88 IGETAVIGDNVTI----YQGVTlGGTGKEKgkrhPTI-GDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVG 162


                 ....*....
gi 496040759 188 VPARVIKKD 196
Cdd:COG1045  163 VPARIVKRK 171
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 91-193 2.90e-20

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: 81.50  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  91 KLILGSG-YINFHSKLHCFNHIEIGENVIISENVII------RDSDNHQITGgnsmfAPVIIKDNAWIGMSAIILKGVTV 163
Cdd:cd05825    3 NLTIGDNsWIGEGVWIYNLAPVTIGSDACISQGAYLctgshdYRSPAFPLIT-----APIVIGDGAWVAAEAFVGPGVTI 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 496040759 164 GEGAIVAAGSVVTKDVPPHTIVAGVPARVI 193
Cdd:cd05825   78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 80-195 5.24e-20

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: 82.07  E-value: 5.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  80 IGSTVVVLPDAKLI----LGSG-YINFHSKLHC-FNHIEIGENVIISENVIIRDSDNHQIT-------GGNSMFAPVIIK 146
Cdd:cd04645    2 IDPSAFIAPNATVIgdvtLGEGsSVWFGAVLRGdVNPIRIGERTNIQDGSVLHVDPGYPTIigdnvtvGHGAVLHGCTIG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496040759 147 DNAWIGMSAIILKGVTVGEGAIVAAGSVVT--KDVPPHTIVAGVPARVIKK 195
Cdd:cd04645   82 DNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 79-190 1.96e-19

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 81.77  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759   79 IIGSTVVVLPDAklILGSG-YINFHSKLHCFnhIEIGENVIISENVIIrdsDNHQITGGNSMFAP-------VIIKDNAW 150
Cdd:TIGR03570  89 LIHPSAIVSPSA--SIGEGtVIMAGAVINPD--VRIGDNVIINTGAIV---EHDCVIGDFVHIAPgvtlsggVVIGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496040759  151 IGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPA 190
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 108-194 7.38e-19

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 79.69  E-value: 7.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 108 FNHIEIGENVIISENVIIRDSDNHQIT-------GGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVT--KD 178
Cdd:COG0663   47 VGPIRIGEGSNIQDGVVLHVDPGYPLTigddvtiGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKV 126

                         90
                 ....*....|....*.
gi 496040759 179 VPPHTIVAGVPARVIK 194
Cdd:COG0663  127 VPPGSLVVGSPAKVVR 142
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 99-195 9.45e-19

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.92  E-value: 9.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  99 INFHSKLHCFNHIEIGENVIISENVIIRDSDNHQITGGNSMFA-------------PVIIKDNAWIGMSAIILKGVTVGE 165
Cdd:PRK09677  74 VNDYVHIACIESITIGRDTLIASKVFITDHNHGSFKHSDDFSSpnlppdmrtlessAVVIGQRVWIGENVTILPGVSIGN 153

                         90       100       110
                 ....*....|....*....|....*....|
gi 496040759 166 GAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:PRK09677 154 GCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 79-189 5.42e-18

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: 77.91  E-value: 5.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  79 IIGSTVVVLPDAklILGSG-YINFHSKLHCFnhIEIGENVIISENVIIrdsDNHQITGGNSMFAP-------VIIKDNAW 150
Cdd:cd03360   86 LIHPSAVVSPSA--VIGEGcVIMAGAVINPD--ARIGDNVIINTGAVI---GHDCVIGDFVHIAPgvvlsggVTIGEGAF 158

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496040759 151 IGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVP 189
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PRK10502 PRK10502
putative acyl transferase; Provisional
 80-194 4.29e-17

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 75.37  E-value: 4.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  80 IGSTVVVLPDAKlilgsgyINFHSKLHCFNHIEIGENV--------IISENVIIRD-------SDNHQITGGNSMFAPVI 144
Cdd:PRK10502  54 IGKGVVIRPSVR-------ITYPWKLTIGDYAWIGDDVwlynlgeiTIGAHCVISQksylctgSHDYSDPHFDLNTAPIV 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 496040759 145 IKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIK 194
Cdd:PRK10502 127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 111-189 3.59e-16

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: 70.55  E-value: 3.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 111 IEIGENVIISENVIIRdsdnHQITGGNSMFAPV----IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVA 186
Cdd:cd03354   23 IVIGETAVIGDNCTIY----QGVTLGGKGKGGGkrhpTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVV 98


                 ...
gi 496040759 187 GVP 189
Cdd:cd03354   99 GVP 101
cysE PRK11132
serine acetyltransferase; Provisional
 108-196 3.13e-13

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 66.26  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 108 FNH---IEIGENVIISENVIIRDSDNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTI 184
Cdd:PRK11132 156 LDHatgIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTT 235

                         90
                 ....*....|..
gi 496040759 185 VAGVPARVIKKD 196
Cdd:PRK11132 236 AAGVPARIVGKP 247
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 111-191 3.70e-13

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 64.24  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  111 IEIGENVIISENVIIRdsdnHQIT-GGNSMFA----PVIiKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIV 185
Cdd:TIGR01172  82 VVIGETAVIGDDVTIY----HGVTlGGTGKEKgkrhPTI-GEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATV 156


                  ....*.
gi 496040759  186 AGVPAR 191
Cdd:TIGR01172 157 VGVPAR 162
PLN02694 PLN02694
serine O-acetyltransferase
 108-193 1.10e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 62.35  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 108 FNH---IEIGENVIISENVIIRdsdnHQITGGNSMFA-----PVIiKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDV 179
Cdd:PLN02694 175 FDHatgVVIGETAVIGNNVSIL----HHVTLGGTGKAcgdrhPKI-GDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDV 249

                         90
                 ....*....|....
gi 496040759 180 PPHTIVAGVPARVI 193
Cdd:PLN02694 250 PPRTTAVGNPARLV 263
PLN02739 PLN02739
serine acetyltransferase
 113-194 1.21e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 62.36  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIRDSDNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARV 192
Cdd:PLN02739 228 IGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKL 307


                 ..
gi 496040759 193 IK 194
Cdd:PLN02739 308 IG 309
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 111-195 3.37e-11

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: 58.74  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 111 IEIGENVIISENVIIRDSDNHQI-------TGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVT--KDVPP 181
Cdd:cd04650   40 IYIGKYSNVQENVSIHTDHGYPTeigdyvtIGHNAVVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPD 119

                         90
                 ....*....|....
gi 496040759 182 HTIVAGVPARVIKK 195
Cdd:cd04650  120 YSLVLGVPAKVVRK 133
PLN02357 PLN02357
serine acetyltransferase
 111-193 1.17e-10

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 59.51  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 111 IEIGENVIISENVIIRDSDNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPA 190
Cdd:PLN02357 247 VVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPA 326


                 ...
gi 496040759 191 RVI 193
Cdd:PLN02357 327 RLI 329
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 79-194 1.18e-10

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: 57.38  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  79 IIGSTVVVLPDAKLI----LGSG-YINFHSKLHC-FNHIEIGENVIISENVIIR---------DSDNHqiTGGNSMFAPV 143
Cdd:cd04745    2 VVDPSSFVHPTAVLIgdviIGKNcYIGPHASLRGdFGRIVIRDGANVQDNCVIHgfpgqdtvlEENGH--IGHGAILHGC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496040759 144 IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTK--DVPPHTIVAGVPARVIK 194
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIR 132
PLN02296 PLN02296
carbonate dehydratase
 113-195 1.27e-10

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 58.98  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIrdsdnHQITggnsmfapviIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKD--VPPHTIVAGVPA 190
Cdd:PLN02296 122 IGDNVTIGHSAVL-----HGCT----------VEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPA 186


                 ....*
gi 496040759 191 RVIKK 195
Cdd:PLN02296 187 KFLRK 191
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 113-192 7.44e-10

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 56.57  E-value: 7.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIrdsdnhqitGGNsmfapVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARV 192
Cdd:COG1043  125 VGNNVILANNATL---------AGH-----VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 109-191 1.84e-09

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: 55.11  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 109 NHIEIGENVIISENVIIrdsdnhqitGGNSMFA-PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAG 187
Cdd:cd03352  125 NLVQIAHNVRIGENCLI---------AAQVGIAgSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195


                 ....
gi 496040759 188 VPAR 191
Cdd:cd03352  196 TPAQ 199
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 113-192 5.20e-09

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: 54.36  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIrdsdnhqitGGNsmfapVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARV 192
Cdd:cd03351  123 IGNNVILANNATL---------AGH-----VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 144-196 1.65e-08

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: 53.49  E-value: 1.65e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496040759 144 IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKKD 196
Cdd:COG1207  396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIEG 448
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-196 2.59e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.84  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIRDSDNHQITggnsmfaPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARV 192
Cdd:PRK14357 361 VGKNVNIGAGTITCNYDGKKKN-------PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQI 433


                 ....
gi 496040759 193 IKKD 196
Cdd:PRK14357 434 VKEG 437
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 145-196 6.15e-08

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.79  E-value: 6.15e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496040759 145 IKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKKD 196
Cdd:PRK14353 383 IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKPG 434
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 112-190 6.48e-08

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: 49.69  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 112 EIGENVIISENVIIrdsdnhqitGG--NSMFA-PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTK----------- 177
Cdd:cd03350   51 QIGKNVHLSAGAVI---------GGvlEPLQAtPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretge 121

                         90
                 ....*....|....*...
gi 496040759 178 ----DVPPH-TIVAGVPA 190
Cdd:cd03350  122 iyygRVPPGsVVVAGSLP 139
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
110-192 9.73e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 50.48  E-value: 9.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 110 HI----EIGENVIISENVIIrdsdnhqitGGNsmfapVIIKDNAWI-GMSAIIlKGVTVGEGAIVAAGSVVTKDVPPHTI 184
Cdd:PRK05289 119 HVahdcVVGNHVILANNATL---------AGH-----VEVGDYAIIgGLTAVH-QFVRIGAHAMVGGMSGVSQDVPPYVL 183


                 ....*...
gi 496040759 185 VAGVPARV 192
Cdd:PRK05289 184 AEGNPARL 191
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 144-185 2.05e-07

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 48.96  E-value: 2.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 496040759 144 IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIV 185
Cdd:cd03353  146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 143-190 3.25e-07

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 49.75  E-value: 3.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 496040759  143 VIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTK--DVPPHTIVAGVPA 190
Cdd:TIGR02353 646 VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 94-196 4.19e-07

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 49.36  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759   94 LGSGYINFHSKLHCFNHIEIGENVIISENVIIRdsdNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGS 173
Cdd:TIGR02353 115 IGKGVDIGSLPPVCTDLLTIGAGTIVRKEVMLL---GYRAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|....*
gi 496040759  174 VVTKD--VPPHTIVAGVPARVIKKD 196
Cdd:TIGR02353 192 ALQGGqsIPDGERWHGSPAQKTGAD 216
PRK10191 PRK10191
putative acyl transferase; Provisional
 111-192 7.53e-07

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 46.81  E-value: 7.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 111 IEIGENVIISENVIIRD--SDNHQIT----GGNSMFAPVIiKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTI 184
Cdd:PRK10191  56 IHHGYAVVINKNVVAGDdfTIRHGVTignrGADNMACPHI-GNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNAL 134


                 ....*...
gi 496040759 185 VAGVPARV 192
Cdd:PRK10191 135 VVGEKARV 142
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 110-176 7.79e-07

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: 45.32  E-value: 7.79e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496040759 110 HIEIGENVIISENVIIRDsdnhqiTGGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVT 176
Cdd:cd00208   18 PVVIGDNVNIGPGAVIGA------ATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 144-184 1.01e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 48.29  E-value: 1.01e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 496040759 144 IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTI 184
Cdd:PRK14354 395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 113-191 2.01e-06

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 46.72  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIrdsdnhqitGG--NSMFA-PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTK-----DVPPHTI 184
Cdd:PRK11830 153 IGKNVHLSGGVGI---------GGvlEPLQAnPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiyDRETGEV 223


                 ....*...
gi 496040759 185 VAG-VPAR 191
Cdd:PRK11830 224 HYGrVPAG 231
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 75-194 2.12e-06

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: 45.67  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  75 GNFDIIGSTVVVLPDAKLilgsgyinfHSKLHCFNHIEIGENVIISENVIIrdsdNHQITGGNsmfapVIIKDNAWIGMS 154
Cdd:cd03359   46 GRYCILSEGCVIRPPFKK---------FSKGVAFFPLHIGDYVFIGENCVV----NAAQIGSY-----VHIGKNCVIGRR 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496040759 155 AIILKGVTVGEGAIVAAGSVvtkdVPPHTIVAGVPARVIK 194
Cdd:cd03359  108 CIIKDCVKILDGTVVPPDTV----IPPYSVVSGRPARFIG 143
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 109-191 3.16e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 46.55  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 109 NHIEIGENVIISENVIIrdsdnhqitGGNSMFA-PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAG 187
Cdd:COG1044  233 NLVQIAHNVRIGEHTAI---------AAQVGIAgSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSG 303


                 ....
gi 496040759 188 VPAR 191
Cdd:COG1044  304 SPAQ 307
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 144-180 3.46e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 46.64  E-value: 3.46e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496040759 144 IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVP 180
Cdd:PRK14356 400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVP 436
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 79-194 4.18e-06

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 45.57  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  79 IIGSTVVVLPDA-------KLILGSGyinfhSKLH--CFNHIEIGENVIISENVIIrdsdnhqitGGNSMFAPVIIKDNA 149
Cdd:PRK13627  30 IVGAGVYIGPLAslrgdygRLIVQAG-----ANLQdgCIMHGYCDTDTIVGENGHI---------GHGAILHGCVIGRDA 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 496040759 150 WIGMSAIILKGVTVGEGAIVAAGSVVTKDV--PPHTIVAGVPARVIK 194
Cdd:PRK13627  96 LVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVR 142
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 113-177 7.69e-06

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 45.11  E-value: 7.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 113 IGENVIISENVIIrdsdnhqitGG-----NSmfAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTK 177
Cdd:COG2171  147 IGKNVHLSGGAGI---------GGvleplQA--APVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTA 205
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 112-194 8.15e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.40  E-value: 8.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 112 EIGENVIISENVIIRDSDnhqitGGNSMfaPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAG-VPA 190
Cdd:PRK09451 371 EIGDNVNIGAGTITCNYD-----GANKF--KTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISrVPQ 443


                 ....
gi 496040759 191 RVIK 194
Cdd:PRK09451 444 RHIQ 447
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-193 1.27e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 44.93  E-value: 1.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496040759 131 HQITGGNSMF-APViikdnawigmsaiilkgvTVGEGAIVAAGSVVTKDVPPHTI-VAGVPARVI 193
Cdd:PRK14352 405 HVRTGSDTMFvAPV------------------TVGDGAYTGAGTVIREDVPPGALaVSEGPQRNI 451
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 142-195 4.38e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 43.38  E-value: 4.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496040759 142 PVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPPHTIVAGVPARVIKK 195
Cdd:PRK14360 390 RTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 70-187 8.06e-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: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759  70 ELIVKGNFdIIGSTVVVLPDAKLILGSGyinfhsklhcfnHIEIGENVIISENVIIRDSDNHQITGGNSMF--------- 140
Cdd:cd04646   11 ESEIRGDV-TIGPGTVVHPRATIIAEAG------------PIIIGENNIIEEQVTIVNKKPKDPAEPKPMIigsnnvfev 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496040759 141 ----APVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKD--VPPHTIVAG 187
Cdd:cd04646   78 gckcEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSeiLPENTVIYG 130
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 110-192 8.28e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.93  E-value: 8.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 110 HIEIGENVIISENVII----RDSDNHQITGGNSMFAPVIIKDNAWIGMSAIILKGVT----------------------- 162
Cdd:PRK12461  77 RLEIGDRNVIREGVTIhrgtKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALlaghvtvgdraiisgnclvhqfc 156

                         90       100       110
                 ....*....|....*....|....*....|.
gi 496040759 163 -VGEGAIVAAGSVVTKDVPPHTIVAGVPARV 192
Cdd:PRK12461 157 rIGALAMMAGGSRISKDVPPYCMMAGHPTNV 187
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 109-194 1.18e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496040759 109 NHIEIGENV----------IISENVIIrdsDNH-QI-----TGGNSMFA-------PVIIKDNAWIGMSAIILKGVTVGE 165
Cdd:PRK00892 208 DDVEIGANTtidrgalddtVIGEGVKI---DNLvQIahnvvIGRHTAIAaqvgiagSTKIGRYCMIGGQVGIAGHLEIGD 284

                         90       100       110
                 ....*....|....*....|....*....|
gi 496040759 166 GAIVAAGSVVTKDVP-PHTIVAGVPARVIK 194
Cdd:PRK00892 285 GVTITAMSGVTKSIPePGEYSSGIPAQPNK 314
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 144-181 2.80e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.88  E-value: 2.80e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 496040759 144 IIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVTKDVPP 181
Cdd:PRK14355 399 VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPP 436
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
143-177 2.47e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.34  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 496040759  143 VIIKDNAWIGMSAIIlkGVTVGEGAIVAAGSVVTK 177
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 113-179 2.57e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 35.63  E-value: 2.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496040759 113 IGENVIISENVIIRDSdnhqitggnSMFAPVIIKDNAWIGMSaIILKGVTVGEGAIVAAGSVVTKDV 179
Cdd:cd05787   19 IGRNCKIGKNVVIDNS---------YIWDDVTIEDGCTIHHS-IVADGAVIGKGCTIPPGSLISFGV 75
PLN02472 PLN02472
uncharacterized protein
 135-195 3.85e-03

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 37.25  E-value: 3.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496040759 135 GGNSMFAPVIIKDNAWIGMSAIILKGVTVGEGAIVAAGSVVT--KDVPPHTIVAGVPARVIKK 195
Cdd:PLN02472 136 GAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRT 198
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
142-171 6.83e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 6.83e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 496040759  142 PVIIKDNAWIGMSAIILKGVTVGEGAIVAA 171
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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