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Conserved domains on  [gi|1340274856|gb|AUZ84076|]
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acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase [Methylophaga nitratireducenticrescens]

Protein Classification

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase( domain architecture ID 11437198)

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell

CATH:  1.20.1180.10|2.160.10.10
EC:  2.3.1.129
Gene Ontology:  GO:0008780|GO:0009245
SCOP:  4002830

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 1-256 5.52e-151

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: 420.96  E-value: 5.52e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:COG1043     3 MIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:COG1043    83 GDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:COG1043   163 AHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSPEV 242

                         250
                  ....*....|....*.
gi 1340274856 241 TIFIEFLDKQQGGIIR 256
Cdd:COG1043   243 RELLDFIRASKRGIIR 258
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 1-256 5.52e-151

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: 420.96  E-value: 5.52e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:COG1043     3 MIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:COG1043    83 GDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:COG1043   163 AHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSPEV 242

                         250
                  ....*....|....*.
gi 1340274856 241 TIFIEFLDKQQGGIIR 256
Cdd:COG1043   243 RELLDFIRASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-256 1.41e-144

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 404.87  E-value: 1.41e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:PRK05289    4 KIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTRLVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:PRK05289   84 GDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:PRK05289  164 AHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDSPEV 243

                         250
                  ....*....|....*.
gi 1340274856 241 TIFIEFLDKQQGGIIR 256
Cdd:PRK05289  244 KEILDFIESSKRGIIR 259
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 1-254 1.02e-143

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: 402.58  E-value: 1.02e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:cd03351     1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:cd03351    81 GDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:cd03351   161 RHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEV 240

                         250
                  ....*....|....
gi 1340274856 241 TIFIEFLDKQQGGI 254
Cdd:cd03351   241 EELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 2-255 1.85e-114

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: 328.45  E-value: 1.85e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEIG 81
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  82 DNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLGS 161
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 162 HCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEELT 241
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|....
gi 1340274856 242 IFIEFLDKQQGGII 255
Cdd:TIGR01852 241 EILDFIRESKRGIC 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 175-255 6.97e-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: 107.16  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 175 VPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEELTIFIEFLDKQQGGI 254
Cdd:pfam13720   2 VPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKRGI 81


                  .
gi 1340274856 255 I 255
Cdd:pfam13720  82 I 82
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 1-256 5.52e-151

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: 420.96  E-value: 5.52e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:COG1043     3 MIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:COG1043    83 GDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:COG1043   163 AHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSPEV 242

                         250
                  ....*....|....*.
gi 1340274856 241 TIFIEFLDKQQGGIIR 256
Cdd:COG1043   243 RELLDFIRASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-256 1.41e-144

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 404.87  E-value: 1.41e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:PRK05289    4 KIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTRLVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:PRK05289   84 GDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:PRK05289  164 AHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDSPEV 243

                         250
                  ....*....|....*.
gi 1340274856 241 TIFIEFLDKQQGGIIR 256
Cdd:PRK05289  244 KEILDFIESSKRGIIR 259
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 1-254 1.02e-143

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: 402.58  E-value: 1.02e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:cd03351     1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:cd03351    81 GDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:cd03351   161 RHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEV 240

                         250
                  ....*....|....
gi 1340274856 241 TIFIEFLDKQQGGI 254
Cdd:cd03351   241 EELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 2-255 1.85e-114

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: 328.45  E-value: 1.85e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEIG 81
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  82 DNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLGS 161
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 162 HCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEELT 241
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|....
gi 1340274856 242 IFIEFLDKQQGGII 255
Cdd:TIGR01852 241 EILDFIRESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 1-256 3.25e-114

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 328.13  E-value: 3.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   1 MIHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEI 80
Cdd:PRK12461    1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGEESRLEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  81 GDNNLIRESVTINRGTeQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLG 160
Cdd:PRK12461   81 GDRNVIREGVTIHRGT-KGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 161 SHCFSAMGSVISRNVPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEEL 240
Cdd:PRK12461  160 ALAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYRSGLSVQQAVAELELQQFESPEV 239

                         250
                  ....*....|....*.
gi 1340274856 241 TIFIEFLDKQQGGIIR 256
Cdd:PRK12461  240 EELIDFIKASKRGIVR 255
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 175-255 6.97e-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: 107.16  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 175 VPPYVLVSGHMAEPVGINVEGLRRRAFTDTQIRNIRQAYKLVYRSGLRMEEARERLHSIQQEAEELTIFIEFLDKQQGGI 254
Cdd:pfam13720   2 VPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKRGI 81


                  .
gi 1340274856 255 I 255
Cdd:pfam13720  82 I 82
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 2-188 2.23e-26

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: 101.72  E-value: 2.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEE-----PQDKKYHG-EQ 75
Cdd:cd03352    10 IGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDgfgfaPDGGGWVKiPQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  76 TL-LEIGDNNLIRESVTINRGTeqgGGMTKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVS 154
Cdd:cd03352    90 LGgVIIGDDVEIGANTTIDRGA---LGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIA 166

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1340274856 155 QFNHLGSHCFSAMGSVISRNVPPYVLVSGHMAEP 188
Cdd:cd03352   167 GHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQP 200
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-188 5.08e-22

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 92.89  E-value: 5.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIgeepqdkkYHGeqtlLEIG 81
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI--------YHA----VRIG 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  82 DNNLIRESV-------------------------------------TINRGT------EQGggmTKVgsDNwimaYVHIA 118
Cdd:PRK00892  171 NRVIIHSGAvigsdgfgfandrggwvkipqlgrviigddveigantTIDRGAlddtviGEG---VKI--DN----LVQIA 241

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340274856 119 HDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSqfNHL--GSHCFSAMGSVISRNVPPY-VLVSGHMAEP 188
Cdd:PRK00892  242 HNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIA--GHLeiGDGVTITAMSGVTKSIPEPgEYSSGIPAQP 312
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-188 1.58e-20

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: 88.92  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADD------------------VVIGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIG 63
Cdd:COG1044    99 IHPSAVIDPSAKIGEGvsigpfavigagvvigdgVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  64 -------EEPQDKKYHGEQT---LL----EIGDNnliresVTINRGTeqgGGMTKVGS----DNwimaYVHIAHDCIIGD 125
Cdd:COG1044   179 adgfgfaPDEDGGWVKIPQLgrvVIgddvEIGAN------TTIDRGA---LGDTVIGDgtkiDN----LVQIAHNVRIGE 245

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340274856 126 NNIFANNASLAGHVIVDQQVILGGFTLVSqfNHL--GSHCFSAMGSVISRNVPPYVLVSGHMAEP 188
Cdd:COG1044   246 HTAIAAQVGIAGSTKIGDNVVIGGQVGIA--GHLtiGDGVIIGAQSGVTKSIPEGGVYSGSPAQP 308
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 79-184 2.74e-13

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: 66.35  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  79 EIGDNNLIRESVTINRGTeqgggmtKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNH 158
Cdd:cd03360    98 VIGEGCVIMAGAVINPDA-------RIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVT 170

                          90       100
                  ....*....|....*....|....*.
gi 1340274856 159 LGSHCFSAMGSVISRNVPPYVLVSGH 184
Cdd:cd03360   171 IGAGAIIGAGAVVTKDVPDGSVVVGN 196
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 79-186 9.58e-13

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 65.21  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  79 EIGDNNLIRESVTINRGTeqgggmtKVGSDNWIMAYVHIAHDCIIGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNH 158
Cdd:TIGR03570 101 SIGEGTVIMAGAVINPDV-------RIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQGVT 173

                          90       100
                  ....*....|....*....|....*...
gi 1340274856 159 LGSHCFSAMGSVISRNVPPYVLVSGHMA 186
Cdd:TIGR03570 174 IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
79-190 5.49e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 50.64  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  79 EIGDNNLIRESVTInrgteqGGGMTKVGSDNWIMAYVHI--AHDCIIGDNNIFANNASL--AGHVIVDQQ---------- 144
Cdd:COG0110    10 RIGDGVVIGPGVRI------YGGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTIltGNHPIDDPAtfplrtgpvt 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340274856 145 -----------VILGGFTLvsqfnhlGSHCFSAMGSVISRNVPPYVLVSGHMAEPVG 190
Cdd:COG0110    84 igddvwigagaTILPGVTI-------GDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 80-190 1.99e-07

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: 48.65  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  80 IGDNNLIRESVTINRGTEQGGGmTKVGSDNWIMAYVHIAHDCIIGDNNIFAN----------NASLAGHVIVDQQVILGG 149
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDN-VKIQSNVSIYEGVTIEDDVFIGPNVVFTNdlyprskiyrKWELKGTTVKRGASIGAN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1340274856 150 FTLVSQfNHLGSHCFSAMGSVISRNVPPYVLVSGHMAEPVG 190
Cdd:cd03358    80 ATILPG-VTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
103-131 3.42e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 3.42e-05
                          10        20
                  ....*....|....*....|....*....
gi 1340274856 103 TKVGSDNWIMAYVHIAHDCIIGDNNIFAN 131
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 32-173 6.64e-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: 42.31  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  32 IASGTEIASHVVIKGPTRIGRNNRIFQFSSIgeepqdkkyHGEQTLLEIGDNNLIRESVTINRGTEQGGGMTKV---GSD 108
Cdd:cd04646     2 IAPGAVVCQESEIRGDVTIGPGTVVHPRATI---------IAEAGPIIIGENNIIEEQVTIVNKKPKDPAEPKPmiiGSN 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1340274856 109 NWIMayVHIAHDCI-IGDNNIFANNASLAGHVIVDQQVILGGFTLVSQFNHLGSHCFSAMGSVISR 173
Cdd:cd04646    73 NVFE--VGCKCEALkIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRR 136
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-199 9.39e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.04  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   6 ALIDPSAKIADDVVIGAYSIIGANVeIASGTEIASHVVIKGpTRIGRNNRIFQFSSIgeEPqdkkyhgeqtlleigdNNL 85
Cdd:PRK14358  283 VLLRGQTRVADGVTIGAYSVVTDSV-LHEGAVIKPHSVLEG-AEVGAGSDVGPFARL--RP----------------GTV 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  86 IRESVTINRGTEQGGGMTKVGSDNWIMAY---VHIAHDCIIGDNNIFANNASLAGH-VIVDQQVILGGFTLVSQFNHLGS 161
Cdd:PRK14358  343 LGEGVHIGNFVETKNARLDAGVKAGHLAYlgdVTIGAETNVGAGTIVANFDGVNKHqSKVGAGVFIGSNTTLIAPRVVGD 422

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1340274856 162 HCFSAMGSVISRNVPpyvlvSGHMAEPVGI--NVEGLRRR 199
Cdd:PRK14358  423 AAFIAAGSAVHDDVP-----EGAMAVARGKqrNLEGWSRR 457
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 5-62 1.85e-04

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 41.25  E-value: 1.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1340274856   5 TALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKgPTRIGRNNRIFQFSSI 62
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKASSVI 65
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 2-221 2.28e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.78  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVEIasgteiashvvikgptRiGRNNRIfqfssigeepqdkkyhgeqtllEIG 81
Cdd:COG0663    13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVL----------------R-GDVGPI----------------------RIG 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  82 DNNLIRESVTInRGTEqgGGMTKVGSDnwimayVHIAHD-----CIIGDNNIFANNAslaghVIVDQQVIlggftlvsqf 156
Cdd:COG0663    54 EGSNIQDGVVL-HVDP--GYPLTIGDD------VTIGHGailhgCTIGDNVLIGMGA-----IVLDGAVI---------- 109

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340274856 157 nhlGSHCFSAMGSVISRN--VPPYVLVSGhmaepvginVEGLRRRAFTDTQIRNIR------QAYKLVYRSGL 221
Cdd:COG0663   110 ---GDGSIVGAGALVTEGkvVPPGSLVVG---------SPAKVVRELTEEEIAFLResaenyVELARRYLAEL 170
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-180 3.09e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   5 TALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGpTRIGRNNRIfQFSSIgeepQDKKYHGEQTlleIGDNN 84
Cdd:PRK14354  259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVD-STIGDGVTI-TNSVI----EESKVGDNVT---VGPFA 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  85 LIRESVTINRGTEQG----------GGMTKVGSdnwiMAYV---HIAHDCIIGDNNIFANNASLAGH--VIVDQQVILGG 149
Cdd:PRK14354  330 HLRPGSVIGEEVKIGnfveikkstiGEGTKVSH----LTYIgdaEVGENVNIGCGTITVNYDGKNKFktIIGDNAFIGCN 405

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1340274856 150 FTLVSQFNhLGSHCFSAMGSVISRNVPPYVL 180
Cdd:PRK14354  406 SNLVAPVT-VGDNAYIAAGSTITKDVPEDAL 435
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 30-190 3.53e-04

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: 39.89  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  30 VEIASGTEIASHVVIKGPTRIGRNNR-IFQfssigeepQDKKYHGEQTLLEIGD------NNLIRESVTINRGTEQGGGM 102
Cdd:cd03359     2 IETASGNKVSRKSVICGSQNIVLNGKtIIQ--------SDVIIRGDLATVSIGRycilseGCVIRPPFKKFSKGVAFFPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856 103 TkvgsdnwIMAYVHIAHDCIIgdnnifaNNASLAGHVIVDQQVILGGFTLVSQFnhlgshCFSAMGSVISRN--VPPYVL 180
Cdd:cd03359    74 H-------IGDYVFIGENCVV-------NAAQIGSYVHIGKNCVIGRRCIIKDC------VKILDGTVVPPDtvIPPYSV 133

                         170
                  ....*....|
gi 1340274856 181 VSGHMAEPVG 190
Cdd:cd03359   134 VSGRPARFIG 143
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 2-189 3.69e-04

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: 39.70  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVeiasgteiashvVIKG---PTRIGRNnrifqfSSIgeepQDKKY-H-GEQT 76
Cdd:cd04645     2 IDPSAFIAPNATVIGDVTLGEGSSVWFGA------------VLRGdvnPIRIGER------TNI----QDGSVlHvDPGY 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  77 LLEIGDNnliresVTINRGTeqgggmtkvgsdnwimayvhIAHDCIIGDNnifannaSLAGH--VIVDQQVIlggftlvs 154
Cdd:cd04645    60 PTIIGDN------VTVGHGA--------------------VLHGCTIGDN-------CLIGMgaIILDGAVI-------- 98

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1340274856 155 qfnhlGSHCFSAMGSVISRN--VPPYVLVSGHMAEPV 189
Cdd:cd04645    99 -----GKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVV 130
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 7-48 3.97e-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: 38.29  E-value: 3.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1340274856   7 LIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGPT 48
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNST 42
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 30-118 4.37e-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: 38.00  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  30 VEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEPQDKKYHGeqtlLEIGDNNLIRESVTINRGteqgggmTKVGSDN 109
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNP----TIIGDNVEIGANAVIHGG-------VKIGDNA 69


                  ....*....
gi 1340274856 110 WIMAYVHIA 118
Cdd:cd00208    70 VIGAGAVVT 78
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-56 6.92e-04

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 39.78  E-value: 6.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGANVEIASGT------------------EIASHVVIKGPTRIGRNNRI 56
Cdd:cd03360    87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNViintgavighdcvigdfvHIAPGVVLSGGVTIGEGAFI 159
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-126 9.42e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   7 LIDPSAkiaddvvigAYsiIGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIgeepQDKKyhgeqtlleIGDNNLI 86
Cdd:PRK14354  254 IIDPES---------TY--IDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI----VDST---------IGDGVTI 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1340274856  87 RESVTINrgteqgggmTKVGSDNWIMAYVHIAHDCIIGDN 126
Cdd:PRK14354  310 TNSVIEE---------SKVGDNVTVGPFAHLRPGSVIGEE 340
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-62 1.67e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 39.24  E-value: 1.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1340274856   8 IDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGpTRIGRNNRIfQFSSI 62
Cdd:COG1207   263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD-STIGDGVVI-KYSVI 315
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 49-136 2.30e-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: 36.07  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  49 RIGRNNRIFQFSSIGEEpqdkkyhgeqtlLEIGDNNLIRESVTI-NRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNN 127
Cdd:cd00208     2 FIGEGVKIHPKAVIRGP------------VVIGDNVNIGPGAVIgAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNA 69


                  ....*....
gi 1340274856 128 IFANNASLA 136
Cdd:cd00208    70 VIGAGAVVT 78
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 49-183 2.30e-03

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: 36.67  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  49 RIGRNNRIFQFSSIGEEpqdkkyhgeqTLLEIGDNNLIRESVTINRGTEQGGGMTKVGSDNWIMAYVHIAHDCIIGDNNI 128
Cdd:cd04647     3 SIGDNVYIGPGCVISAG----------GGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1340274856 129 fannaslaghvivdqqvILGGFTLvsqfnhlGSHCFSAMGSVISRNVPPYVLVSG 183
Cdd:cd04647    73 -----------------ILPGVTI-------GDGAVVGAGSVVTKDVPPNSIVAG 103
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 26-126 2.36e-03

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: 37.78  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  26 IGANVEIASGTEIASHVVIKGPTRIGRNNRIFQFSSIGEEpqdkkyhgeqtllEIGDNNLIRESVTINrgTEQGGGMTKV 105
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDS-------------TIGDGVVIKASSVIE--GAVIGNGATV 76

                          90       100
                  ....*....|....*....|.
gi 1340274856 106 GsdnwimAYVHIAHDCIIGDN 126
Cdd:cd03353    77 G------PFAHLRPGTVLGEG 91
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 8-56 3.00e-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: 35.69  E-value: 3.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340274856   8 IDPSAKIADDVVIGAYSIIGANVEIASGT--------------EIASHVVIKGPTRIGRNNRI 56
Cdd:cd00208     9 IHPKAVIRGPVVIGDNVNIGPGAVIGAATgpneknptiigdnvEIGANAVIHGGVKIGDNAVI 71
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-199 4.98e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.82  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   5 TALIDPSAKIADDVVIGAYSIIGANVEIASGTEIASHVVIKGpTRIGRNNRIFQFSSIGEEPQDKKYHGEQTLLEIGdnN 84
Cdd:PRK14357  249 TTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVD-CEIGNNVKIIRSECEKSVIEDDVSVGPFSRLREG--T 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856  85 LIRESVTINRGTEQGGGMTKVGSDNWIMAYV---HIAHDCIIGDNNIFANNASLAGH--VIVDQQVILGGFTLVSQFNhL 159
Cdd:PRK14357  326 VLKKSVKIGNFVEIKKSTIGENTKAQHLTYLgdaTVGKNVNIGAGTITCNYDGKKKNptFIEDGAFIGSNSSLVAPVR-I 404

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1340274856 160 GSHCFSAMGSVISRNVPPYVLVSGHMAEpvgINVEG--LRRR 199
Cdd:PRK14357  405 GKGALIGAGSVITEDVPPYSLALGRARQ---IVKEGwvLKKR 443
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 2-53 6.43e-03

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: 36.45  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340274856   2 IHQTALIDPSAKIADDVVIGAYSIIGAN--------------------------------VEIASGTEIASHVVIKGPTR 49
Cdd:cd00710     5 IDPSAYVHPTAVVIGDVIIGDNVFVGPGasiradegtpiiiganvniqdgvvihalegysVWIGKNVSIAHGAIVHGPAY 84


                  ....
gi 1340274856  50 IGRN 53
Cdd:cd00710    85 IGDN 88
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 20-56 6.66e-03

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: 36.41  E-value: 6.66e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1340274856  20 IGAYSIIGANVEIASGTEIASHVVIKGPTRIGRNNRI 56
Cdd:cd05636     8 VEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEI 44
 
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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