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Conserved domains on  [gi|500019826|ref|WP_011700544|]
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acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase [Syntrophobacter fumaroxidans]

Protein Classification

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

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

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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 ...
 1-258 7.97e-138

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: 387.84  E-value: 7.97e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   1 MQIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVL 80
Cdd:COG1043    2 AMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  81 IGDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRI 160
Cdd:COG1043   82 IGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 161 GTYSFIGGGSGISMDVPPYMLVVGSrPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCA 240
Cdd:COG1043  162 GAHAMVGGGSGVVKDVPPYVLAAGN-PARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 500019826 241 EVELLLEFVGSSKRGVIR 258
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 1-258 7.97e-138

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: 387.84  E-value: 7.97e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   1 MQIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVL 80
Cdd:COG1043    2 AMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  81 IGDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRI 160
Cdd:COG1043   82 IGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 161 GTYSFIGGGSGISMDVPPYMLVVGSrPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCA 240
Cdd:COG1043  162 GAHAMVGGGSGVVKDVPPYVLAAGN-PARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 500019826 241 EVELLLEFVGSSKRGVIR 258
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 2-256 1.18e-133

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: 377.16  E-value: 1.18e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   2 QIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVLI 81
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  82 GDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIG 161
Cdd:cd03351   81 GDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 162 TYSFIGGGSGISMDVPPYMLVVGSrPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAE 241
Cdd:cd03351  161 RHAMVGGGSGVVQDVPPYVIAAGN-RARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPE 239

                        250
                 ....*....|....*
gi 500019826 242 VELLLEFVGSSKRGV 256
Cdd:cd03351  240 VEELVDFIRSSKRGI 254
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-258 5.39e-131

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 370.58  E-value: 5.39e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   1 MQIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVL 80
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTRLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  81 IGDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRI 160
Cdd:PRK05289  83 IGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 161 GTYSFIGGGSGISMDVPPYMLVVGsRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCA 240
Cdd:PRK05289 163 GAHAMVGGMSGVSQDVPPYVLAEG-NPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDSP 241

                        250
                 ....*....|....*...
gi 500019826 241 EVELLLEFVGSSKRGVIR 258
Cdd:PRK05289 242 EVKEILDFIESSKRGIIR 259
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 3-257 2.70e-104

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: 303.03  E-value: 2.70e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826    3 IHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVLIG 82
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   83 DDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIGT 162
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  163 YSFIGGGSGISMDVPPYMLvVGSRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAEV 242
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCL-AEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEV 239

                         250
                  ....*....|....*
gi 500019826  243 ELLLEFVGSSKRGVI 257
Cdd:TIGR01852 240 KEILDFIRESKRGIC 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 175-257 1.79e-33

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: 116.41  E-value: 1.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  175 DVPPYMLVVGsRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAEVELLLEFVGSSKR 254
Cdd:pfam13720   1 DVPPYVLAAG-NPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKR 79


                  ...
gi 500019826  255 GVI 257
Cdd:pfam13720  80 GII 82
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 1-258 7.97e-138

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: 387.84  E-value: 7.97e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   1 MQIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVL 80
Cdd:COG1043    2 AMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  81 IGDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRI 160
Cdd:COG1043   82 IGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 161 GTYSFIGGGSGISMDVPPYMLVVGSrPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCA 240
Cdd:COG1043  162 GAHAMVGGGSGVVKDVPPYVLAAGN-PARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 500019826 241 EVELLLEFVGSSKRGVIR 258
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 2-256 1.18e-133

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: 377.16  E-value: 1.18e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   2 QIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVLI 81
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  82 GDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIG 161
Cdd:cd03351   81 GDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 162 TYSFIGGGSGISMDVPPYMLVVGSrPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAE 241
Cdd:cd03351  161 RHAMVGGGSGVVQDVPPYVIAAGN-RARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPE 239

                        250
                 ....*....|....*
gi 500019826 242 VELLLEFVGSSKRGV 256
Cdd:cd03351  240 VEELVDFIRSSKRGI 254
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-258 5.39e-131

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 370.58  E-value: 5.39e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   1 MQIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVL 80
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTRLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  81 IGDDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRI 160
Cdd:PRK05289  83 IGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 161 GTYSFIGGGSGISMDVPPYMLVVGsRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCA 240
Cdd:PRK05289 163 GAHAMVGGMSGVSQDVPPYVLAEG-NPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDSP 241

                        250
                 ....*....|....*...
gi 500019826 241 EVELLLEFVGSSKRGVIR 258
Cdd:PRK05289 242 EVKEILDFIESSKRGIIR 259
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 3-257 2.70e-104

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: 303.03  E-value: 2.70e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826    3 IHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVLIG 82
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   83 DDNVFREHVSIHRGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIGT 162
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  163 YSFIGGGSGISMDVPPYMLvVGSRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAEV 242
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCL-AEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEV 239

                         250
                  ....*....|....*
gi 500019826  243 ELLLEFVGSSKRGVI 257
Cdd:TIGR01852 240 KEILDFIRESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 3-258 5.03e-100

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 291.93  E-value: 5.03e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   3 IHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHPPQDFSYRDEETRVLIG 82
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGEESRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  83 DDNVFREHVSIHrGTRRGRGTTRVGSRNYIMSAAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIGT 162
Cdd:PRK12461  82 DRNVIREGVTIH-RGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 163 YSFIGGGSGISMDVPPYmLVVGSRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAEV 242
Cdd:PRK12461 161 LAMMAGGSRISKDVPPY-CMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYRSGLSVQQAVAELELQQFESPEV 239

                        250
                 ....*....|....*.
gi 500019826 243 ELLLEFVGSSKRGVIR 258
Cdd:PRK12461 240 EELIDFIKASKRGIVR 255
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 175-257 1.79e-33

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: 116.41  E-value: 1.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  175 DVPPYMLVVGsRPAKLYGLNTTGLKRHDFSANVLSALKKSYRILFRSGLNVRDAVDKIRVEVETCAEVELLLEFVGSSKR 254
Cdd:pfam13720   1 DVPPYVLAAG-NPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKR 79


                  ...
gi 500019826  255 GVI 257
Cdd:pfam13720  80 GII 82
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 3-189 1.30e-23

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: 94.40  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   3 IHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGhppQD-FSYRDEET---- 77
Cdd:cd03352   10 IGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIG---SDgFGFAPDGGgwvk 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  78 -----RVLIGDDnvfrehVSIhrgtrrgrgttrvGSRNYIMSAA----------------HIAHDCQIGDNVVMANVAVL 136
Cdd:cd03352   87 ipqlgGVIIGDD------VEI-------------GANTTIDRGAlgdtvigdgtkidnlvQIAHNVRIGENCLIAAQVGI 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 500019826 137 GGHVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSrPAK 189
Cdd:cd03352  148 AGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGT-PAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 3-200 7.77e-22

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: 92.39  E-value: 7.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   3 IHPTAIVDSKAELADDVVIKAY------------SIIGPNVKIGPGTSVG------PHAVIDGWTTIGARNQVCSFVAIG 64
Cdd:COG1044   99 IHPSAVIDPSAKIGEGVSIGPFavigagvvigdgVVIGPGVVIGDGVVIGddcvlhPNVTIYERCVIGDRVIIHSGAVIG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  65 hppQD-FSYRDEET----------RVLIGDDnvfrehVSIhrgtrrgrgttrvGSRNYIMSAA----------------H 117
Cdd:COG1044  179 ---ADgFGFAPDEDggwvkipqlgRVVIGDD------VEI-------------GANTTIDRGAlgdtvigdgtkidnlvQ 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 118 IAHDCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAV--HqfVRIGTYSFIGGGSGISMDVPPYMLVVGS--RPAKLYGL 193
Cdd:COG1044  237 IAHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIagH--LTIGDGVIIGAQSGVTKSIPEGGVYSGSpaQPHREWLR 314


                 ....*..
gi 500019826 194 NTTGLKR 200
Cdd:COG1044  315 NAAALRR 321
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 3-213 1.02e-21

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 92.12  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   3 IHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHP---------------P 67
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAvrignrviihsgaviG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  68 QD-FSYRDEET---------RVLIGDDnvfrehVSIhrgtrrgrgttrvGSRNYIMSAA----------------HIAHD 121
Cdd:PRK00892 183 SDgFGFANDRGgwvkipqlgRVIIGDD------VEI-------------GANTTIDRGAlddtvigegvkidnlvQIAHN 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 122 CQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSRPAKLYGL---NTTGL 198
Cdd:PRK00892 244 VVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEwlrTAARL 323

                        250
                 ....*....|....*
gi 500019826 199 KRHDFSANVLSALKK 213
Cdd:PRK00892 324 RRLDELRKRLKALEK 338
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 41-185 2.46e-14

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: 69.44  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  41 PHAVIDGWTTIGARNQVCSFVAIGhppqdfsyrdeeTRVLIGDDNVfrehvsihrgtrrgrgttrvgsrnyIMSAAHIAH 120
Cdd:cd03360   89 PSAVVSPSAVIGEGCVIMAGAVIN------------PDARIGDNVI-------------------------INTGAVIGH 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500019826 121 DCQIGDNVVMANVAVLGGHVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGS 185
Cdd:cd03360  132 DCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGN 196
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 35-188 5.74e-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: 65.59  E-value: 5.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   35 PGTSVGPHAVIDGWTTIGARNQVCSFVAIGhppqdfsyrdeeTRVLIGDdnvfreHVSIHrgtrrgrgttrvgsrnyimS 114
Cdd:TIGR03570  86 FATLIHPSAIVSPSASIGEGTVIMAGAVIN------------PDVRIGD------NVIIN-------------------T 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500019826  115 AAHIAHDCQIGDNVVMANVAVLGGHVEIGDFAALG-GAVaVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSrPA 188
Cdd:TIGR03570 129 GAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGaGAT-IIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGV-PA 201
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 2-189 3.42e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 54.65  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   2 QIHPTAIVDSKAeladdvvikaySIIGpNVKIGPGTSVGPHAVIDG---WTTIGARNQVcsfvaighppQDFS--YRDEE 76
Cdd:COG0663   12 QIHPSAFVAPTA-----------VVIG-DVTIGEDVSVWPGAVLRGdvgPIRIGEGSNI----------QDGVvlHVDPG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  77 TRVLIGDDnvfrehVSIhrgtrrgrgttrvgsrnyimsaAHIA--HDCQIGDNVVmanvavlgghveIGDfaalgGAVaV 154
Cdd:COG0663   70 YPLTIGDD------VTI----------------------GHGAilHGCTIGDNVL------------IGM-----GAI-V 103

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 500019826 155 HQFVRIGTYSFIGGGSGIS--MDVPPYMLVVGSrPAK 189
Cdd:COG0663  104 LDGAVIGDGSIVGAGALVTegKVVPPGSLVVGS-PAK 139
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
89-189 1.31e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 52.18  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  89 EHVSIHRGTRRGRGTTRVGSRNYIMSAAHI--AHDCQIGDNVVMA-NVAVLG---------------GHVEIGDFAALGG 150
Cdd:COG0110   13 DGVVIGPGVRIYGGNITIGDNVYIGPGVTIddPGGITIGDNVLIGpGVTILTgnhpiddpatfplrtGPVTIGDDVWIGA 92

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500019826 151 AVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSrPAK 189
Cdd:COG0110   93 GATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGN-PAR 130
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 106-192 2.40e-08

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: 50.96  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 106 VGSRNYIMSAAHIAHDCQIGDNV------VMANVAVLGGHVE---------IGDFAALGGAVAVHQFVRIGTYSFIGGGS 170
Cdd:cd03358   19 IGDNVKIQSNVSIYEGVTIEDDVfigpnvVFTNDLYPRSKIYrkwelkgttVKRGASIGANATILPGVTIGEYALVGAGA 98

                         90       100
                 ....*....|....*....|..
gi 500019826 171 GISMDVPPYMLVVGSrPAKLYG 192
Cdd:cd03358   99 VVTKDVPPYALVVGN-PARIIG 119
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 2-189 2.13e-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: 49.33  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   2 QIHPTAIVDSKAeladdvvikaySIIGpNVKIGPGTSVGPHAVIDG---WTTIGARNQVcsfvaighppQDFS--YRDEE 76
Cdd:cd04645    1 EIDPSAFIAPNA-----------TVIG-DVTLGEGSSVWFGAVLRGdvnPIRIGERTNI----------QDGSvlHVDPG 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  77 TRVLIGDDnvfrehVSIhrgtrrgrgttrvgsrnyimsaAH--IAHDCQIGDNVVMANVAVLgghveigdfaaLGGAVav 154
Cdd:cd04645   59 YPTIIGDN------VTV----------------------GHgaVLHGCTIGDNCLIGMGAII-----------LDGAV-- 97

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 500019826 155 hqfvrIGTYSFIGGGSGIS--MDVPPYMLVVGSrPAK 189
Cdd:cd04645   98 -----IGKGSIVAAGSLVPpgKVIPPGSLVAGS-PAK 128
PLN02739 PLN02739
serine acetyltransferase
 118-193 2.42e-06

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 47.72  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 118 IAHDCQIGDNVVMANVAVLGG--------HVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSrPAK 189
Cdd:PLN02739 228 IGETAVIGDRVSILHGVTLGGtgketgdrHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN-PAK 306


                 ....
gi 500019826 190 LYGL 193
Cdd:PLN02739 307 LIGF 310
PLN02694 PLN02694
serine O-acetyltransferase
 124-192 5.64e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 46.56  E-value: 5.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500019826 124 IGDNVVMANVAVLGG--------HVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSrPAKLYG 192
Cdd:PLN02694 189 IGNNVSILHHVTLGGtgkacgdrHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGN-PARLVG 264
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 2-129 6.86e-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: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   2 QIHPTAIVDSKAELADDvvikaysiigpnVKIGPGTSVGPHAVID---GWTTIGARNQVCSFVAIGHPPQDFSyrDEETR 78
Cdd:cd04646    1 KIAPGAVVCQESEIRGD------------VTIGPGTVVHPRATIIaeaGPIIIGENNIIEEQVTIVNKKPKDP--AEPKP 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500019826  79 VLIGDDNVFREHVSIHrgtrrgrgTTRVGSRNYIMSAAHIAHDCQIGDNVV 129
Cdd:cd04646   67 MIIGSNNVFEVGCKCE--------ALKIGNNNVFESKSFVGKNVIITDGCI 109
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-184 1.01e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.21  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  27 IGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAIGHppqdfSY--------RDEETRVLIGDD------------NV 86
Cdd:PRK14357 252 IHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVD-----CEignnvkiiRSECEKSVIEDDvsvgpfsrlregTV 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  87 FREHVSIHRGTRRGRGTTRVGSRnyimsAAHIAHdcqIGDNVVMANVAVLGGHVE------------IGDFAALGGAVAV 154
Cdd:PRK14357 327 LKKSVKIGNFVEIKKSTIGENTK-----AQHLTY---LGDATVGKNVNIGAGTITcnydgkkknptfIEDGAFIGSNSSL 398

                        170       180       190
                 ....*....|....*....|....*....|
gi 500019826 155 HQFVRIGTYSFIGGGSGISMDVPPYMLVVG 184
Cdd:PRK14357 399 VAPVRIGKGALIGAGSVITEDVPPYSLALG 428
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 3-183 1.83e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.27  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   3 IHPTAIVDSKAELADDVVIKAYSIIGPNVkIGPGTSVGPHAVIDGwTTIGARNQVCSFvaighppqdfsyrdeeTRVLIG 82
Cdd:PRK14358 279 IEPGVLLRGQTRVADGVTIGAYSVVTDSV-LHEGAVIKPHSVLEG-AEVGAGSDVGPF----------------ARLRPG 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  83 ddNVFREHVSIHRGTRRGRGTTRVGsrnyiMSAAHIAH--------DCQIGDNVVMANVAVLGGH-VEIGDFAALGGAVA 153
Cdd:PRK14358 341 --TVLGEGVHIGNFVETKNARLDAG-----VKAGHLAYlgdvtigaETNVGAGTIVANFDGVNKHqSKVGAGVFIGSNTT 413

                        170       180       190
                 ....*....|....*....|....*....|
gi 500019826 154 VHQFVRIGTYSFIGGGSGISMDVPPYMLVV 183
Cdd:PRK14358 414 LIAPRVVGDAAFIAAGSAVHDDVPEGAMAV 443
PLN02357 PLN02357
serine acetyltransferase
 124-192 1.99e-04

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 42.18  E-value: 1.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500019826 124 IGDNVVMANVAVLGG--------HVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSrPAKLYG 192
Cdd:PLN02357 255 VGNNVSILHNVTLGGtgkqsgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGN-PARLIG 330
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 3-189 2.69e-04

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: 40.43  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   3 IHPTAIVDSKAeladdvvikaySIIGpNVKIGPGTSVGPHAVIDGwttigarnqvcsfvaighppqDFSyrdeetRVLIG 82
Cdd:cd04745    3 VDPSSFVHPTA-----------VLIG-DVIIGKNCYIGPHASLRG---------------------DFG------RIVIR 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  83 DDNVFREHVSIHrgtRRGRGTTRVGSRNYIMSAAhIAHDCQIGDNVVMANVAVLGGHVEIGDFAalggAVAVHQFVRIGt 162
Cdd:cd04745   44 DGANVQDNCVIH---GFPGQDTVLEENGHIGHGA-ILHGCTIGRNALVGMNAVVMDGAVIGEES----IVGAMAFVKAG- 114

                        170       180
                 ....*....|....*....|....*..
gi 500019826 163 ysfigggsgisMDVPPYMLVVGSrPAK 189
Cdd:cd04745  115 -----------TVIPPRSLIAGS-PAK 129
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 6-184 4.98e-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: 40.10  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   6 TAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGwTTIGARNQVCSFVAIghppqdfsyrdEETrvlIGDDN 85
Cdd:cd03353    9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD-STIGDGVVIKASSVI-----------EGA---VIGNG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  86 VfrehvsihrgtrrgrgttRVGSRNYIMSAAHIAHDCQIGDNVVMANvAVLGGHVEIGDFAALG----------GA---- 151
Cdd:cd03353   74 A------------------TVGPFAHLRPGTVLGEGVHIGNFVEIKK-STIGEGSKANHLSYLGdaeigegvniGAgtit 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500019826 152 -----VAVHQ-------F----------VRIGTYSFIGGGSGISMDVPPYMLVVG 184
Cdd:cd03353  135 cnydgVNKHRtvigdnvFigsnsqlvapVTIGDGATIAAGSTITKDVPPGALAIA 189
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-64 6.82e-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: 6.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500019826   2 QIHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARnqvcSFVAIG 64
Cdd:cd03360  104 VIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG----AFIGAG 162
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 3-63 7.95e-04

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: 39.11  E-value: 7.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500019826   3 IHPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTIGARNQVCSFVAI 63
Cdd:cd05636    8 VEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEV 68
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-187 8.69e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   6 TAIVDSKAELAD-DVVIKAYSIIGPNVKIGPGTSVGPHAVIDGWTTI-GARNQVCSFVAIGHPPQDFSYRDEetrVLIG- 82
Cdd:PRK14355 255 VTLIDPETTYIDrGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIkGCRIGDDVTVKAGSVLEDSVVGDD---VAIGp 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  83 -----DDNVFREHVSIHRGTRRGRGTTRVGSRnyimsAAHIAH--DCQIGDNV------VMANVAVLGGH-VEIGDFAAL 148
Cdd:PRK14355 332 mahlrPGTELSAHVKIGNFVETKKIVMGEGSK-----ASHLTYlgDATIGRNVnigcgtITCNYDGVKKHrTVIEDDVFV 406

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 500019826 149 GGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGSRP 187
Cdd:PRK14355 407 GSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSP 445
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 117-190 1.18e-03

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 38.29  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500019826 117 HIAHDCQIGDNVVmanvaVLGGhVEIGDfaalgGAVavhqfvrigtysfIGGGSGISMDVPPYMLVVGSrPAKL 190
Cdd:cd03349   75 IIGNDVWIGHGAT-----ILPG-VTIGD-----GAV-------------IAAGAVVTKDVPPYAIVGGN-PAKV 123
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 9-184 1.61e-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: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826   9 VDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVIDGwTTIGARNQVcsfvaighppqDFSYRDEETrvlIGDDNVfr 88
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD-STIGDGVVI-----------KYSVIEDAV---VGAGAT-- 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826  89 ehvsihrgtrrgrgttrVGSRNYIMSAAHIAHDCQIGDNVVMANvAVLG-----GHVE-IGDfAALG-----GA------ 151
Cdd:COG1207  326 -----------------VGPFARLRPGTVLGEGVKIGNFVEVKN-STIGegskvNHLSyIGD-AEIGegvniGAgtitcn 386

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 500019826 152 ---VAVHQ-------F----------VRIGTYSFIGGGSGISMDVPPYMLVVG 184
Cdd:COG1207  387 ydgVNKHRtvigdgaFigsntnlvapVTIGDGATIGAGSTITKDVPAGALAIA 439
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 106-172 3.21e-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: 37.77  E-value: 3.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500019826 106 VGSRNYIMSAAHIAHDCQIGDNVV-MANVaVLGGHVEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGI 172
Cdd:cd03352    4 IGENVSIGPNAVIGEGVVIGDGVViGPGV-VIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 106-189 3.90e-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: 35.90  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 106 VGSRNYIMSAAH--IAHDCQIGDNVVM-------------ANVAVLGGHVEIGDFAALGGAVAVHQFVRIGTYSFIGGGS 170
Cdd:cd04647   10 IGPGCVISAGGGitIGDNVLIGPNVTIydhnhdiddperpIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGS 89

                         90
                 ....*....|....*....
gi 500019826 171 GISMDVPPYMLVVGSrPAK 189
Cdd:cd04647   90 VVTKDVPPNSIVAGN-PAK 107
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 123-189 4.26e-03

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: 36.99  E-value: 4.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500019826 123 QIGDNVVM-ANVAVLGGhVEIGDFAAlggavavhqfvrigtysfIGGGSGISMDVPPYMLVVGSrPAK 189
Cdd:COG1045  119 TIGDNVVIgAGAKILGP-ITIGDNAK------------------IGANSVVLKDVPPGSTVVGV-PAR 166
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
4-45 4.46e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 36.39  E-value: 4.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 500019826   4 HPTAIVDSKAELADDVVIKAYSIIGPNVKIGPGTSVGPHAVI 45
Cdd:COG0110   67 HPIDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVV 108
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 124-189 8.30e-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: 36.25  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500019826 124 IGDNVVMA-NVAVL-GGH----------------VEIGDFAALGGAVAVHQFVRIGTYSFIGGGSGISMDVPPYMLVVGS 185
Cdd:cd03357   85 IGDNVLIGpNVQIYtAGHpldpeernrgleyakpITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGN 164


                 ....
gi 500019826 186 rPAK 189
Cdd:cd03357  165 -PAR 167
 
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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