NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30688366|ref|NP_194683|]
View 

bacterial transferase hexapeptide repeat-containing protein [Arabidopsis thaliana]

Protein Classification

UDP-N-acetylglucosamine O-acyltransferase( domain architecture ID 10129645)

UDP-N-acetylglucosamine O-acyltransferase catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc, the first step of lipid A biosynthetic pathway

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 41-323 2.33e-127

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: 364.45  E-value: 2.33e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPssHVfgntelgescVLMtgavvgdelpGYTFIGCNNIIGHH 120
Cdd:cd03351   2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGS--HV----------VID----------GPTTIGKNNRIFPF 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 121 AVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGH 199
Cdd:cd03351  60 ASIGEAPQDLKYK-GEPTRLEIGDNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGH 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 200 VVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFM 279
Cdd:cd03351 139 VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYR 218

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 30688366 280 StetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGI 323
Cdd:cd03351 219 S----GLTLEEALEELEEEAPDSPEVEELVDFIR----SSKRGI 254
 
Name Accession Description Interval E-value
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 41-323 2.33e-127

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: 364.45  E-value: 2.33e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPssHVfgntelgescVLMtgavvgdelpGYTFIGCNNIIGHH 120
Cdd:cd03351   2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGS--HV----------VID----------GPTTIGKNNRIFPF 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 121 AVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGH 199
Cdd:cd03351  60 ASIGEAPQDLKYK-GEPTRLEIGDNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGH 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 200 VVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFM 279
Cdd:cd03351 139 VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYR 218

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 30688366 280 StetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGI 323
Cdd:cd03351 219 S----GLTLEEALEELEEEAPDSPEVEELVDFIR----SSKRGI 254
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 38-325 1.29e-123

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: 355.09  E-value: 1.29e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  38 EVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLypSSHVfgntelgescVLMtgavvgdelpGYTFIGCNNII 117
Cdd:COG1043   1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVI--GSHV----------VIE----------GPTTIGKNNRI 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 118 GHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLL 196
Cdd:COG1043  59 FPFASIGEEPQDLKYK-GEPTRLEIGDNNTIREFVTIHRgTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATL 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 197 AGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRK 276
Cdd:COG1043 138 AGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRL 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 30688366 277 IFMStetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGICK 325
Cdd:COG1043 218 LYRS----GLTLEEALEELEAELPDSPEVRELLDFIR----ASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
37-327 5.05e-123

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 353.63  E-value: 5.05e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   37 SEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYpsSHVfgntelgescVLMtgavvgdelpGYTFIGCNNI 116
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIG--SHV----------VID----------GHTTIGKNNR 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  117 IGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTL 195
Cdd:PRK05289  59 IFPFASIGEDPQDLKYK-GEPTRLVIGDNNTIREFVTINRgTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNAT 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  196 LAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYR 275
Cdd:PRK05289 138 LAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYK 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30688366  276 KIFMStetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGICKFR 327
Cdd:PRK05289 218 LLYRS----GLTLEEALEELAEEYPDSPEVKEILDFIE----SSKRGIIRPR 261
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 41-324 3.86e-99

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 293.01  E-value: 3.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366    41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDElPgytfigcnniighh 120
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGV-P-------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   121 avvgvkcQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGH 199
Cdd:TIGR01852  66 -------QDLKYK-GEKTRLIIGDNNTIREFVTINRGTASGGgVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGH 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   200 VVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFM 279
Cdd:TIGR01852 138 VEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 30688366   280 STetvsLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGIC 324
Cdd:TIGR01852 218 SG----LPLREAAQQVAEEYEDNPEVKEILDFIR----ESKRGIC 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 235-324 2.47e-30

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 110.24  E-value: 2.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   235 DVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFMStetvSLSFEERLTELDQELYSVPAVSAMLQSIRd 314
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRS----GLTLEEALEELEEEVPDSPEVQEILDFIR- 75

                          90
                  ....*....|
gi 30688366   315 sftESRRGIC 324
Cdd:pfam13720  76 ---SSKRGII 82
 
Name Accession Description Interval E-value
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 41-323 2.33e-127

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: 364.45  E-value: 2.33e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPssHVfgntelgescVLMtgavvgdelpGYTFIGCNNIIGHH 120
Cdd:cd03351   2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGS--HV----------VID----------GPTTIGKNNRIFPF 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 121 AVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGH 199
Cdd:cd03351  60 ASIGEAPQDLKYK-GEPTRLEIGDNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGH 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 200 VVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFM 279
Cdd:cd03351 139 VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYR 218

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 30688366 280 StetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGI 323
Cdd:cd03351 219 S----GLTLEEALEELEEEAPDSPEVEELVDFIR----SSKRGI 254
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 38-325 1.29e-123

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: 355.09  E-value: 1.29e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  38 EVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLypSSHVfgntelgescVLMtgavvgdelpGYTFIGCNNII 117
Cdd:COG1043   1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVI--GSHV----------VIE----------GPTTIGKNNRI 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 118 GHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLL 196
Cdd:COG1043  59 FPFASIGEEPQDLKYK-GEPTRLEIGDNNTIREFVTIHRgTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATL 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 197 AGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRK 276
Cdd:COG1043 138 AGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRL 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 30688366 277 IFMStetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGICK 325
Cdd:COG1043 218 LYRS----GLTLEEALEELEAELPDSPEVRELLDFIR----ASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
37-327 5.05e-123

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 353.63  E-value: 5.05e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   37 SEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYpsSHVfgntelgescVLMtgavvgdelpGYTFIGCNNI 116
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIG--SHV----------VID----------GHTTIGKNNR 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  117 IGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTL 195
Cdd:PRK05289  59 IFPFASIGEDPQDLKYK-GEPTRLVIGDNNTIREFVTINRgTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNAT 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  196 LAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYR 275
Cdd:PRK05289 138 LAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYK 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30688366  276 KIFMStetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGICKFR 327
Cdd:PRK05289 218 LLYRS----GLTLEEALEELAEEYPDSPEVKEILDFIE----SSKRGIIRPR 261
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 41-324 3.86e-99

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 293.01  E-value: 3.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366    41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDElPgytfigcnniighh 120
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGV-P-------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   121 avvgvkcQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGH 199
Cdd:TIGR01852  66 -------QDLKYK-GEKTRLIIGDNNTIREFVTINRGTASGGgVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGH 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   200 VVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFM 279
Cdd:TIGR01852 138 VEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 30688366   280 STetvsLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGIC 324
Cdd:TIGR01852 218 SG----LPLREAAQQVAEEYEDNPEVKEILDFIR----ESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 40-325 1.81e-89

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 268.43  E-value: 1.81e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   40 LIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDElPgytfigcnniigh 119
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE-P------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  120 havvgvkcQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGH 199
Cdd:PRK12461  67 --------QDFTYK-GEESRLEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  200 VVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFM 279
Cdd:PRK12461 138 VTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYR 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 30688366  280 StetvSLSFEERLTELDQELYSVPAVSAMLQSIRdsftESRRGICK 325
Cdd:PRK12461 218 S----GLSVQQAVAELELQQFESPEVEELIDFIK----ASKRGIVR 255
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 41-244 4.20e-37

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: 135.53  E-value: 4.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDElpgyTFIGCNNIIGHH 120
Cdd:COG1044  99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYER----CVIGDRVIIHSG 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 121 AVVGvkcQD-------LKYKH-----------GDECFlcIGNNneirefCSIHRSSkpSDKTVIGDN----NLImgscHI 178
Cdd:COG1044 175 AVIG---ADgfgfapdEDGGWvkipqlgrvviGDDVE--IGAN------TTIDRGA--LGDTVIGDGtkidNLV----QI 237

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30688366 179 AHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVV--HqfCHIGSFAFIGGGSVVSQDVPKYMMVAG 244
Cdd:COG1044 238 AHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIagH--LTIGDGVIIGAQSGVTKSIPEGGVYSG 303
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 39-244 5.98e-36

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: 129.07  E-value: 5.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  39 VLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDELPGYTFIGCNNIIG 118
Cdd:cd03352   8 VSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPDGGGWVKI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 119 HHaVVGVKcqdlkykhgdecflcIGNNNEIREFCSIHRSSKpsDKTVIGDN----NLimgsCHIAHDCKIGDRNIFANNT 194
Cdd:cd03352  88 PQ-LGGVI---------------IGDDVEIGANTTIDRGAL--GDTVIGDGtkidNL----VQIAHNVRIGENCLIAAQV 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 30688366 195 LLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAG 244
Cdd:cd03352 146 GIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 41-238 5.32e-31

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 119.47  E-value: 5.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDElpgyTFIGCNNIIGHH 120
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA----VRIGNRVIIHSG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  121 AVVGvkcQD-----------LKYKH-GdecFLCIGNNNEIREFCSIHRSSkpSDKTVIGDN----NLimgsCHIAHDCKI 184
Cdd:PRK00892 179 AVIG---SDgfgfandrggwVKIPQlG---RVIIGDDVEIGANTTIDRGA--LDDTVIGEGvkidNL----VQIAHNVVI 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30688366  185 GDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPK 238
Cdd:PRK00892 247 GRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPE 300
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 235-324 2.47e-30

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 110.24  E-value: 2.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   235 DVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFMStetvSLSFEERLTELDQELYSVPAVSAMLQSIRd 314
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRS----GLTLEEALEELEEEVPDSPEVQEILDFIR- 75

                          90
                  ....*....|
gi 30688366   315 sftESRRGIC 324
Cdd:pfam13720  76 ---SSKRGII 82
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 99-244 4.33e-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: 80.99  E-value: 4.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  99 AVVGDELPGYTFIGCNNIIGHHAVVgvkcqDLKYKHGDECFLCIGNNN---EIREFCS---------IHRSSKPSD---- 162
Cdd:cd03360  25 GFLDDDPELKGTEGLGLPVGLDELL-----LLYPPPDDEFVVAIGDNKlrrKLAEKLLaagyrfatlIHPSAVVSPsavi 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 163 --------------KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGG 228
Cdd:cd03360 100 gegcvimagavinpDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGA 179

                       170
                ....*....|....*.
gi 30688366 229 GSVVSQDVPKYMMVAG 244
Cdd:cd03360 180 GAVVTKDVPDGSVVVG 195
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 106-244 9.40e-17

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: 77.53  E-value: 9.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   106 PGYTFIgcnNIIGHHAVVGVKCQdlkykhgdecflcIGNNNEIREFCSIHRSSKpsdktvIGDNNLIMGSCHIAHDCKIG 185
Cdd:TIGR03570  82 KGYRFA---TLIHPSAIVSPSAS-------------IGEGTVIMAGAVINPDVR------IGDNVIINTGAIVEHDCVIG 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   186 DRNIFANNTLLAGHVVVEDNTHT-AGASVVHQfCHIGSFAFIGGGSVVSQDVPKYMMVAG 244
Cdd:TIGR03570 140 DFVHIAPGVTLSGGVVIGEGVFIgAGATIIQG-VTIGAGAIVGAGAVVTKDIPDGGVVVG 198
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
142-244 2.69e-12

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 63.35  E-value: 2.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 142 IGNNNEIREFCSIHRSskpsdKTVIGDNNLIMGSCHI--AHDCKIGDRNIFANNTLL----------------AGHVVVE 203
Cdd:COG0110  11 IGDGVVIGPGVRIYGG-----NITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIG 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30688366 204 DNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAG 244
Cdd:COG0110  86 DDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAG 126
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 53-251 1.25e-09

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: 55.20  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  53 IGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCvlmtgavvgdelpgytFIGcnniigHHAVvgvkcqdlky 132
Cdd:cd03358   1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDV----------------FIG------PNVV---------- 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 133 khgdecflcIGNNNEIRefCSIHRSSKpSDKTVIGDNnlimgschiahdCKIGdrnifANNTLLAGHvvvednthtagas 212
Cdd:cd03358  49 ---------FTNDLYPR--SKIYRKWE-LKGTTVKRG------------ASIG-----ANATILPGV------------- 86

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 30688366 213 vvhqfcHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRG 251
Cdd:cd03358  87 ------TIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 39-237 1.44e-09

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: 56.66  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  39 VLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVkLGNGCKLYPSSHVfgntelgESCVLMTGAVVGdelPgYTFIGCNNIIG 118
Cdd:cd03353  22 VVIDPGVILEGKTVIGEDCVIGPNCVIKDST-IGDGVVIKASSVI-------EGAVIGNGATVG---P-FAHLRPGTVLG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 119 HHAvvgvkcqdlkykHgdecflcIGNNNEIREfCSIHRSSKPSDKTVIGDnnlimgsCHIAHDCKIGDRNIFAN------ 192
Cdd:cd03353  90 EGV------------H-------IGNFVEIKK-STIGEGSKANHLSYLGD-------AEIGEGVNIGAGTITCNydgvnk 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 30688366 193 -NTllaghvVVEDNTHTAGASV----VhqfcHIGSFAFIGGGSVVSQDVP 237
Cdd:cd03353 143 hRT------VIGDNVFIGSNSQlvapV----TIGDGATIAAGSTITKDVP 182
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 142-244 2.80e-09

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: 54.00  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 142 IGNNNEIREFCSIHrsskPSDKTVIGDNNLIMGSCHI-AHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHI 220
Cdd:cd04647   4 IGDNVYIGPGCVIS----AGGGITIGDNVLIGPNVTIyDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTI 79

                        90       100
                ....*....|....*....|....
gi 30688366 221 GSFAFIGGGSVVSQDVPKYMMVAG 244
Cdd:cd04647  80 GDGAVVGAGSVVTKDVPPNSIVAG 103
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 41-211 3.04e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 55.42  E-value: 3.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAV------IGKGVSVGPYCTI---GSSVKLGNGCklypsshvfgNteLGESCVLMTgavvgdeLPGY-TF 110
Cdd:COG0663  13 IHPSAFVAPTAVvigdvtIGEDVSVWPGAVLrgdVGPIRIGEGS----------N--IQDGVVLHV-------DPGYpLT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 111 IGCNNIIGHHAVVgvkcqdlkykHGdeCflcignnneirefcsihrsskpsdktVIGDNNLI-MGSChIAHDCKIGDRNI 189
Cdd:COG0663  74 IGDDVTIGHGAIL----------HG--C--------------------------TIGDNVLIgMGAI-VLDGAVIGDGSI 114

                       170       180
                ....*....|....*....|..
gi 30688366 190 FANNTLLAGHVVVEDNTHTAGA 211
Cdd:COG0663 115 VGAGALVTEGKVVPPGSLVVGS 136
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
39-123 8.34e-09

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 53.34  E-value: 8.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  39 VLIHPSAVVHP-NAVIGKGVSVGPYC--------TIGSSVKLGNGCKLYPSSH----------VFGNTELGESCVLMTGA 99
Cdd:COG0110  15 VVIGPGVRIYGgNITIGDNVYIGPGVtiddpggiTIGDNVLIGPGVTILTGNHpiddpatfplRTGPVTIGDDVWIGAGA 94

                        90       100
                ....*....|....*....|....
gi 30688366 100 VVgdeLPGYTfIGCNNIIGHHAVV 123
Cdd:COG0110  95 TI---LPGVT-IGDGAVVGAGSVV 114
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 36-256 3.30e-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: 54.65  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  36 DSEVLIHPSAVVHPNA------VIGKGVSVGPYCTIgSSVKLGNGCKLYpSSHVfgntelgescvlmTGAVVGDelpgyt 109
Cdd:COG1207 264 DGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTL-KDSTIGDGVVIK-YSVI-------------EDAVVGA------ 322

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 110 fiGCNniIG---H---HAVVGVKCqdlkykHgdecflcIGNnneireFCSIhrssKpsdKTVIGDnnlimGScHIAH--- 180
Cdd:COG1207 323 --GAT--VGpfaRlrpGTVLGEGV------K-------IGN------FVEV----K---NSTIGE-----GS-KVNHlsy 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 181 --DCKIGDR-N-----IFAN----N---TllaghvVVEDNTHTaG------ASVvhqfcHIGSFAFIGGGSVVSQDVPKY 239
Cdd:COG1207 367 igDAEIGEGvNigagtITCNydgvNkhrT------VIGDGAFI-GsntnlvAPV-----TIGDGATIGAGSTITKDVPAG 434

                       250
                ....*....|....*..
gi 30688366 240 MMVAGeRAELRglNLEG 256
Cdd:COG1207 435 ALAIA-RARQR--NIEG 448
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 41-172 8.16e-08

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 51.09  E-value: 8.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAV------IGKGVSVGPYCTI--------------------------GSSVKLGNGCKLYPSSHVFGNTE 88
Cdd:cd00710   5 IDPSAYVHPTAVvigdviIGDNVFVGPGASIradegtpiiiganvniqdgvvihaleGYSVWIGKNVSIAHGAIVHGPAY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  89 LGESCVLMTGAVVGDelpgyTFIGCNNIIGHHAVV-GVKCQDLKY-KHGdecfLCIGNNNEIREFCSIHRSSKPSDKTVI 166
Cdd:cd00710  85 IGDNCFIGFRSVVFN-----AKVGDNCVIGHNAVVdGVEIPPGRYvPAG----AVITSQTQADALPDVTDSAREFNEKVI 155


                ....*.
gi 30688366 167 GDNNLI 172
Cdd:cd00710 156 TVNNEL 161
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-237 2.50e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 52.05  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   36 DSEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLgNGCKlypsshvfgnteLGESCVLMTGAVVGDelpgytfigcnN 115
Cdd:PRK14355 266 DRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-KGCR------------IGDDVTVKAGSVLED-----------S 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  116 IIGHHAVVGVKCQdlkYKHGDEC--FLCIGNNNEIREFcSIHRSSKPSDKTVIGDnnlimgsCHIAHDCKIGDRNIFANN 193
Cdd:PRK14355 322 VVGDDVAIGPMAH---LRPGTELsaHVKIGNFVETKKI-VMGEGSKASHLTYLGD-------ATIGRNVNIGCGTITCNY 390

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30688366  194 TLLAGH-VVVEDNTHTaGASVvhQF---CHIGSFAFIGGGSVVSQDVP 237
Cdd:PRK14355 391 DGVKKHrTVIEDDVFV-GSDV--QFvapVTVGRNSLIAAGTTVTKDVP 435
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 56-256 3.98e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 51.37  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   56 GVS-VGPYCT-IGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDelpgyTFIGCNNII----GHHAVVGVKCQd 129
Cdd:PRK14354 251 GVTiIDPESTyIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVD-----STIGDGVTItnsvIEESKVGDNVT- 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  130 lkykhgdecflcIGNNNEIREFCSIHRSSKPSD-----KTVIGDNNLI-----MGSCHIAHDCKIGDRNIFAN------- 192
Cdd:PRK14354 325 ------------VGPFAHLRPGSVIGEEVKIGNfveikKSTIGEGTKVshltyIGDAEVGENVNIGCGTITVNydgknkf 392

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30688366  193 NTLLAGHVVVEDNThTAGASVvhqfcHIGSFAFIGGGSVVSQDVPKYMMvAGERAelRGLNLEG 256
Cdd:PRK14354 393 KTIIGDNAFIGCNS-NLVAPV-----TVGDNAYIAAGSTITKDVPEDAL-AIARA--RQVNKEG 447
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 36-206 4.64e-07

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: 48.56  E-value: 4.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  36 DSEVLIHPSAVVHPNAVIGKGVSVGPYCTI---GSSVKLGNgcklypsshvfgNTELGESCVLMTGavvgdelPGY-TFI 111
Cdd:cd04645   3 DPSAFIAPNATVIGDVTLGEGSSVWFGAVLrgdVNPIRIGE------------RTNIQDGSVLHVD-------PGYpTII 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 112 GCNNIIGHHAVVgvkcqdlkykHGdecflcignnneirefCSIHrsskpsDKTVIGdnnliMGSChIAHDCKIGDRNIFA 191
Cdd:cd04645  64 GDNVTVGHGAVL----------HG----------------CTIG------DNCLIG-----MGAI-ILDGAVIGKGSIVA 105

                       170
                ....*....|....*
gi 30688366 192 NNTLLAGHVVVEDNT 206
Cdd:cd04645 106 AGSLVPPGKVIPPGS 120
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 50-124 1.14e-06

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: 46.68  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  50 NAVIGKGVSVGPYC--------TIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVV-GDelpgYTFIGCNNI---- 116
Cdd:cd04647   1 NISIGDNVYIGPGCvisagggiTIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIViGD----DVWIGANVVilpg 76

                        90
                ....*....|
gi 30688366 117 --IGHHAVVG 124
Cdd:cd04647  77 vtIGDGAVVG 86
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 39-112 1.42e-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: 45.89  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  39 VLIHPSAVV-HPNAVIGKGVSVGPYCTIGS--------SVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDELP-GY 108
Cdd:cd03354  16 FIDHGTGIViGETAVIGDNCTIYQGVTLGGkgkgggkrHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPaNS 95


                ....
gi 30688366 109 TFIG 112
Cdd:cd03354  96 TVVG 99
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 164-244 2.07e-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: 45.51  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 164 TVIGDNNLIMGSCHIAHDCKIGDRNIFANNtllaGHVVVEDNTHT-AGASVVHQfCHIGSFAFIGGGSVVSQDVPKYMMV 242
Cdd:cd03354  23 IVIGETAVIGDNCTIYQGVTLGGKGKGGGK----RHPTIGDNVVIgAGAKILGN-ITIGDNVKIGANAVVTKDVPANSTV 97


                ..
gi 30688366 243 AG 244
Cdd:cd03354  98 VG 99
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-124 4.48e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.90  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   13 SPLVSSTIRRLSSSLSYSREDSR-DSEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVkLGNGCKlypSSHV--FGNTEL 89
Cdd:PRK14354 296 SRIVDSTIGDGVTITNSVIEESKvGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKST-IGEGTK---VSHLtyIGDAEV 371

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30688366   90 GESCVLMTGAV-------------VGDelpgYTFIGCN-NII-----GHHAVVG 124
Cdd:PRK14354 372 GENVNIGCGTItvnydgknkfktiIGD----NAFIGCNsNLVapvtvGDNAYIA 421
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 39-124 6.20e-06

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 43.78  E-value: 6.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  39 VLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNgcklYPSSHVFGNTELGESCVLMTGAVVGdelpGYTFIGCNNIIG 118
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGA----ATGPNEKNPTIIGDNVEIGANAVIH----GGVKIGDNAVIG 72


                ....*.
gi 30688366 119 HHAVVG 124
Cdd:cd00208  73 AGAVVT 78
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 34-136 7.75e-06

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: 45.27  E-value: 7.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  34 SRDSEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVV-------GDELP 106
Cdd:cd05636   1 KDEIEGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVknsiimdGTKVP 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 30688366 107 GYTFIGcNNIIGHHAVV--GVKCQDLKYKHGD 136
Cdd:cd05636  81 HLNYVG-DSVLGENVNLgaGTITANLRFDDKP 111
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 55-261 8.65e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 47.07  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   55 KGVS-VGPYCT-IGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDelpgyTFIGCNNIIGHHAVVGVKCQD--- 129
Cdd:PRK14357 240 NGVTiLDPNTTyIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVD-----CEIGNNVKIIRSECEKSVIEDdvs 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  130 ----LKYKHGDEcfLC----IGNNNEIREfCSIHRSSKPSDKTVIGDnnlimgsCHIAHDCKIGDRNIFANNTLLAGH-V 200
Cdd:PRK14357 315 vgpfSRLREGTV--LKksvkIGNFVEIKK-STIGENTKAQHLTYLGD-------ATVGKNVNIGAGTITCNYDGKKKNpT 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30688366  201 VVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGeRAelRGLNLEG--LRRNG 261
Cdd:PRK14357 385 FIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALG-RA--RQIVKEGwvLKKRK 444
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 41-176 1.33e-05

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: 44.67  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAVIGKGVSVGPYCTIGSSVKL-GNgcklypsshvFGNTELGESCVLMTGAVVgDELPGY-TFIGCNNIIG 118
Cdd:cd04745   3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLrGD----------FGRIVIRDGANVQDNCVI-HGFPGQdTVLEENGHIG 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30688366 119 HHAVVgvkcqdlkykHGdecflCIgnnneIREFCSIHRSSKPSDKTVIGDNNlIMGSC 176
Cdd:cd04745  72 HGAIL----------HG-----CT-----IGRNALVGMNAVVMDGAVIGEES-IVGAM 108
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 163-251 2.51e-05

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: 43.92  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 163 KTVIGDNnlimgsCHIAHDCKIGDRNIFANNtllaGHVVVEDNTHT-AGASV---VHqfchIGSFAFIGGGSVVSQDVPK 238
Cdd:COG1045  91 TAVIGDN------VTIYQGVTLGGTGKEKGK----RHPTIGDNVVIgAGAKIlgpIT----IGDNAKIGANSVVLKDVPP 156

                        90
                ....*....|...
gi 30688366 239 YMMVAGERAELRG 251
Cdd:COG1045 157 GSTVVGVPARIVK 169
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
163-192 2.73e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.40  E-value: 2.73e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 30688366   163 KTVIGDNNLIMGSCHIAHDCKIGDRNIFAN 192
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 40-128 3.16e-05

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 41.79  E-value: 3.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  40 LIHPSAVVHPNAVIGKGVsVGPYCTIGSSVKLGNgcklypsshvfgntelgesCVLMTGAVVGDelpGYTFIGCnnIIGH 119
Cdd:cd04652   1 LVGENTQVGEKTSIKRSV-IGANCKIGKRVKITN-------------------CVIMDNVTIED---GCTLENC--IIGN 55


                ....*....
gi 30688366 120 HAVVGVKCQ 128
Cdd:cd04652  56 GAVIGEKCK 64
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 164-236 7.65e-05

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: 40.64  E-value: 7.65e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30688366 164 TVIGDNNLIMGSChIAHDCKIGDrNIFANNTLLAGHVVVEDNTHTAGaSVVHQFCHIGSFAFIGGGSVVSQDV 236
Cdd:cd05787   6 TSIGEGTTIKNSV-IGRNCKIGK-NVVIDNSYIWDDVTIEDGCTIHH-SIVADGAVIGKGCTIPPGSLISFGV 75
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 63-260 7.69e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.15  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   63 CTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDelpgyTFIGCNNIIGH----HAVVGVKCQDLKYKH---- 134
Cdd:PRK14360 257 CTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIEN-----SQIGENVTVLYsvvsDSQIGDGVKIGPYAHlrpe 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  135 ---GDECFlcIGNNNEIRefcsihrsskpsdKTVIGDNNLI-----MGSCHIAHDCKIGDRNIFANNTLLAGH-VVVEDN 205
Cdd:PRK14360 332 aqiGSNCR--IGNFVEIK-------------KSQLGEGSKVnhlsyIGDATLGEQVNIGAGTITANYDGVKKHrTVIGDR 396

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30688366  206 THTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGeRAelRGLNLEGLRRN 260
Cdd:PRK14360 397 SKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA-RS--RQVIKENWKKK 448
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-251 9.56e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.94  E-value: 9.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   36 DSEVLIHP--SAVVHPNAVIGKGVSV-GPyCTIGSSVKLGNGCKLYpsSHVF-GNTELGESCVL-----MTGAVVGDelp 106
Cdd:PRK14356 253 ESGVLIHApeSVRIGPRATIEPGAEIyGP-CEIYGASRIARGAVIH--SHCWlRDAVVSSGATIhsfshLEGAEVGD--- 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  107 gytfiGCnnIIGHHAvvgvkcqdlKYKHGdeCFL----CIGNNNEIREfCSIHRSSKPSDKTVIGDNNLIMGS------- 175
Cdd:PRK14356 327 -----GC--SVGPYA---------RLRPG--AVLeegaRVGNFVEMKK-AVLGKGAKANHLTYLGDAEIGAGAnigagti 387

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  176 -CHI----AHDCKIGDRNIFANNTLLAGHVvvednthtagasvvhqfcHIGSFAFIGGGSVVSQDVPkymmvAGERAELR 250
Cdd:PRK14356 388 tCNYdgvnKHRTVIGEGAFIGSNTALVAPV------------------TIGDGALVGAGSVITKDVP-----DGSLAIAR 444


                 .
gi 30688366  251 G 251
Cdd:PRK14356 445 G 445
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-128 1.20e-04

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: 39.92  E-value: 1.20e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30688366  51 AVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVfgntelgescvlmtGAVVGDELPGYTFIGCNNIIGHHAVVGVKCQ 128
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVI--------------GAATGPNEKNPTIIGDNVEIGANAVIHGGVK 64
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 40-118 2.38e-04

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 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: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 39.06  E-value: 2.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  40 LIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLgngcklypsshvfgntelgESCVLMTGAVVGDE-LPGYTFIGCNNIIG 118
Cdd:cd05824   1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRL-------------------QRCVILSNSTVRDHsWVKSSIVGWNSTVG 61
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 162-244 2.83e-04

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 39.51  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 162 DKTVIGDNNLI--MGSCHIAHDCKI--------GDRNI----FAnntLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIG 227
Cdd:cd05825   8 DNSWIGEGVWIynLAPVTIGSDACIsqgaylctGSHDYrspaFP---LITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVG 84

                        90
                ....*....|....*..
gi 30688366 228 GGSVVSQDVPKYMMVAG 244
Cdd:cd05825  85 ARSVVVRDLPAWTVYAG 101
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 162-232 3.52e-04

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: 38.77  E-value: 3.52e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30688366 162 DKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNT--LLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVV 232
Cdd:cd00208   5 EGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATgpNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
50-79 5.23e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 5.23e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 30688366    50 NAVIGKGVSVGPYCTIGSSVKLGNGCKLYP 79
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 161-250 5.87e-04

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: 39.67  E-value: 5.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 161 SDKTVIGDNNLImGSC-HIAHDCKIGdrnifaNNTLLAG--------HVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSV 231
Cdd:cd03350  35 DEGTMVDSWATV-GSCaQIGKNVHLS------AGAVIGGvleplqatPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVV 107

                        90
                ....*....|....*....
gi 30688366 232 VSQDVPKYMMVAGERAELR 250
Cdd:cd03350 108 LTQSTPIYDRETGEIYYGR 126
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 166-244 1.07e-03

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: 39.33  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 166 IGDNnlimgsCHIAHDC--------KIGDRNIFANNTLL--AGH----------------VVVEDNTHTAGASVVHQFCH 219
Cdd:cd03357  65 IGDN------FYANFNCtildvapvTIGDNVLIGPNVQIytAGHpldpeernrgleyakpITIGDNVWIGGGVIILPGVT 138

                        90       100
                ....*....|....*....|....*
gi 30688366 220 IGSFAFIGGGSVVSQDVPKYMMVAG 244
Cdd:cd03357 139 IGDNSVIGAGSVVTKDIPANVVAAG 163
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 41-167 1.21e-03

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 38.85  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  41 IHPSAVVHPNAVIGKGVSVGPyctigssvklgnGCKLYPSSHVF---GNTELGESCVLMTGAVVGDELPGYTFIGCNNII 117
Cdd:cd04646   2 IAPGAVVCQESEIRGDVTIGP------------GTVVHPRATIIaeaGPIIIGENNIIEEQVTIVNKKPKDPAEPKPMII 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 30688366 118 GHHAV--VGVKCQDLKykhgdecflcIGNNNEIREFCSIHRSSKPSDKTVIG 167
Cdd:cd04646  70 GSNNVfeVGCKCEALK----------IGNNNVFESKSFVGKNVIITDGCIIG 111
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 89-179 1.55e-03

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: 36.84  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  89 LGESCVLMTGAVVGDELpgytFIGCNNIIGHHAVVGVKCQDLKYKHgdecfLCIGNNNEIREFCSIHrsskpsDKTVIGD 168
Cdd:cd00208   3 IGEGVKIHPKAVIRGPV----VIGDNVNIGPGAVIGAATGPNEKNP-----TIIGDNVEIGANAVIH------GGVKIGD 67

                        90
                ....*....|.
gi 30688366 169 NNLIMGSCHIA 179
Cdd:cd00208  68 NAVIGAGAVVT 78
PLN02694 PLN02694
serine O-acetyltransferase
 34-109 1.65e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 39.63  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366   34 SRDSEVL---IHPSA--------------VVHPNAVIGKGVSVGPYCTIGSS--------VKLGNGCKLYPSSHVFGNTE 88
Cdd:PLN02694 153 SRISDVFavdIHPAAkigkgilfdhatgvVIGETAVIGNNVSILHHVTLGGTgkacgdrhPKIGDGVLIGAGATILGNVK 232

                         90       100
                 ....*....|....*....|.
gi 30688366   89 LGESCVLMTGAVVGDELPGYT 109
Cdd:PLN02694 233 IGEGAKIGAGSVVLIDVPPRT 253
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
39-67 2.26e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 2.26e-03
                          10        20
                  ....*....|....*....|....*....
gi 30688366    39 VLIHPSAVVHPNAVIGKGVSVGPYCTIGS 67
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 81-214 3.61e-03

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: 37.69  E-value: 3.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  81 SHVFGNTELGESCVLMTGAVVGDElPGYTFIGCNNIIGHHAVVGVKCQDLKYKHGDecfLCIGNNNEIREFCSIHRSSkp 160
Cdd:cd04646  12 SEIRGDVTIGPGTVVHPRATIIAE-AGPIIIGENNIIEEQVTIVNKKPKDPAEPKP---MIIGSNNVFEVGCKCEALK-- 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30688366 161 sdktvIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVV 214
Cdd:cd04646  86 -----IGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCL 134
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 89-186 4.21e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 35.68  E-value: 4.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  89 LGESCVLMTGAVVGDelpgyTFIGCNNIIGHHAVVgvkcqdlkykhgDECFlcIGNNNEIREFCSIhRSSKPSDKTVIGD 168
Cdd:cd03356   2 IGESTVIGENAIIKN-----SVIGDNVRIGDGVTI------------TNSI--LMDNVTIGANSVI-VDSIIGDNAVIGE 61

                        90
                ....*....|....*...
gi 30688366 169 NNLIMGSCHIAHDCKIGD 186
Cdd:cd03356  62 NVRVVNLCIIGDDVVVED 79
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 142-232 5.48e-03

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 35.25  E-value: 5.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366 142 IGNNNEIREFCSIHRSskpsdktVIGDNnlimgschiahdCKIGDRNIFANNTLLaGHVVVEDNthtagasVVHQFCHIG 221
Cdd:cd04652   2 VGENTQVGEKTSIKRS-------VIGAN------------CKIGKRVKITNCVIM-DNVTIEDG-------CTLENCIIG 54

                        90
                ....*....|.
gi 30688366 222 SFAFIGGGSVV 232
Cdd:cd04652  55 NGAVIGEKCKL 65
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 38-172 6.65e-03

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: 36.92  E-value: 6.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688366  38 EVLIHPSAVVHPNAVI---GKGVSVGPYCTIGSSVKLGNgcKLYPSSHVFGNTELGESCVLMTGAVVgdelpGYTFIGCN 114
Cdd:cd04646  17 DVTIGPGTVVHPRATIiaeAGPIIIGENNIIEEQVTIVN--KKPKDPAEPKPMIIGSNNVFEVGCKC-----EALKIGNN 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30688366 115 NIIGHHAVVGVKCQdlkykhgdecflcIGNNNEIREFCSIHRSSKPSDKTVI-GDNNLI 172
Cdd:cd04646  90 NVFESKSFVGKNVI-------------ITDGCIIGAGCKLPSSEILPENTVIyGADCLR 135
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 36-104 6.87e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.91  E-value: 6.87e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30688366  36 DSEVLIHPSAVVHpNAVIGKGVSVGPYCTIGSS-----VKLGNGCKLYpSSHVFGNTELGESCVLMTGAVVGDE 104
Cdd:cd03356   3 GESTVIGENAIIK-NSVIGDNVRIGDGVTITNSilmdnVTIGANSVIV-DSIIGDNAVIGENVRVVNLCIIGDD 74
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 165-235 9.11e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.00  E-value: 9.11e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30688366 165 VIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQD 235
Cdd:cd03352   3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSD 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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