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Conserved domains on  [gi|149057926|gb|EDM09169|]
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dynactin 6 (predicted), isoform CRA_b [Rattus norvegicus]

Protein Classification

LbH_Dynactin_6 domain-containing protein( domain architecture ID 10140303)

LbH_Dynactin_6 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 10-179 2.17e-96

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: 276.51  E-value: 2.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  10 KIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIipdtedPEPKPMIIGTNNV 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP------AEPKPMIIGSNNV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  90 FEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRRVQTERPQPQTLQLDFLMK 169
Cdd:cd04646   75 FEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTDRPKPQTLQLDFLRK 154

                        170
                 ....*....|
gi 149057926 170 ILPNYHHLKK 179
Cdd:cd04646  155 ILPNYHHLKK 164
 
Name Accession Description Interval E-value
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 10-179 2.17e-96

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: 276.51  E-value: 2.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  10 KIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIipdtedPEPKPMIIGTNNV 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP------AEPKPMIIGSNNV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  90 FEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRRVQTERPQPQTLQLDFLMK 169
Cdd:cd04646   75 FEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTDRPKPQTLQLDFLRK 154

                        170
                 ....*....|
gi 149057926 170 ILPNYHHLKK 179
Cdd:cd04646  155 ILPNYHHLKK 164
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 7-184 2.27e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.57  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVVCveseirGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIinaHPDniipdtedpEPKPMIIGt 86
Cdd:COG0663   15 PSAFVAPTAVVI------GDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVL---HVD---------PGYPLTIG- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  87 NNVFeVGcHsQAM----KMGDNNVIESKAYVGRNVILTSGCIIGACC--SLNTFeaIPENTVIYG--ADCLRRVQTErpq 158
Cdd:COG0663   76 DDVT-IG-H-GAIlhgcTIGDNVLIGMGAIVLDGAVIGDGSIVGAGAlvTEGKV--VPPGSLVVGspAKVVRELTEE--- 147

                        170       180
                 ....*....|....*....|....*.
gi 149057926 159 pqtlQLDFLMKILPNYHHLKKTMKGS 184
Cdd:COG0663  148 ----EIAFLRESAENYVELARRYLAE 169
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-126 3.08e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.87  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVvcveseIRGDVTIGPRTVIHPKARIIaeaGPIIIGEGNLIEEQAlIINAHPDNIipdTEDPEPKPMIIGT 86
Cdd:PRK12461  16 SGVEIGPFAV------IGANVEIGDGTWIGPHAVIL---GPTRIGKNNKIHQGA-VVGDEPQDF---TYKGEESRLEIGD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149057926  87 NNVFEVGC-------HSQAMKMGDNNVIESKAYVGRNVILTSGCIIG 126
Cdd:PRK12461  83 RNVIREGVtihrgtkGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILV 129
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 6-151 2.84e-04

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: 40.32  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926    6 QKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARI---------IAEAGPIIIGEGNLIEEQALIinaHPDNiipdteD 76
Cdd:TIGR01852  26 GPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIggvpqdlkyKGEKTRLIIGDNNTIREFVTI---NRGT------A 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149057926   77 PEPKPMIIGTNNVFEVGCH-SQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRR 151
Cdd:TIGR01852  97 SGGGVTRIGNNNLLMAYSHiAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSK 172
 
Name Accession Description Interval E-value
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 10-179 2.17e-96

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: 276.51  E-value: 2.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  10 KIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIipdtedPEPKPMIIGTNNV 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP------AEPKPMIIGSNNV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  90 FEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRRVQTERPQPQTLQLDFLMK 169
Cdd:cd04646   75 FEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTDRPKPQTLQLDFLRK 154

                        170
                 ....*....|
gi 149057926 170 ILPNYHHLKK 179
Cdd:cd04646  155 ILPNYHHLKK 164
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 27-114 5.10e-12

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: 58.80  E-value: 5.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  27 VTIGPRTVIHPKARIIaeaGPIIIGEGNLIEEQALIINAHPDNiipdtedpEPKPMIIGTNNVFEVGCH-SQAMKMGDNN 105
Cdd:cd00208    1 VFIGEGVKIHPKAVIR---GPVVIGDNVNIGPGAVIGAATGPN--------EKNPTIIGDNVEIGANAViHGGVKIGDNA 69


                 ....*....
gi 149057926 106 VIESKAYVG 114
Cdd:cd00208   70 VIGAGAVVT 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 7-184 2.27e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.57  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVVCveseirGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIinaHPDniipdtedpEPKPMIIGt 86
Cdd:COG0663   15 PSAFVAPTAVVI------GDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVL---HVD---------PGYPLTIG- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  87 NNVFeVGcHsQAM----KMGDNNVIESKAYVGRNVILTSGCIIGACC--SLNTFeaIPENTVIYG--ADCLRRVQTErpq 158
Cdd:COG0663   76 DDVT-IG-H-GAIlhgcTIGDNVLIGMGAIVLDGAVIGDGSIVGAGAlvTEGKV--VPPGSLVVGspAKVVRELTEE--- 147

                        170       180
                 ....*....|....*....|....*.
gi 149057926 159 pqtlQLDFLMKILPNYHHLKKTMKGS 184
Cdd:COG0663  148 ----EIAFLRESAENYVELARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 7-143 1.58e-08

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: 51.26  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVVCveseirGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIinaHPDniipdtedpEPKPMIIGt 86
Cdd:cd04645    4 PSAFIAPNATVI------GDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVL---HVD---------PGYPTIIG- 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149057926  87 NNVFeVGcHsQAM----KMGDNNVIESKAYVGRNVILTSGCIIGAccslNTFeaIPENTVI 143
Cdd:cd04645   65 DNVT-VG-H-GAVlhgcTIGDNCLIGMGAIILDGAVIGKGSIVAA----GSL--VPPGKVI 116
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-126 3.08e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.87  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVvcveseIRGDVTIGPRTVIHPKARIIaeaGPIIIGEGNLIEEQAlIINAHPDNIipdTEDPEPKPMIIGT 86
Cdd:PRK12461  16 SGVEIGPFAV------IGANVEIGDGTWIGPHAVIL---GPTRIGKNNKIHQGA-VVGDEPQDF---TYKGEESRLEIGD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149057926  87 NNVFEVGC-------HSQAMKMGDNNVIESKAYVGRNVILTSGCIIG 126
Cdd:PRK12461  83 RNVIREGVtihrgtkGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILV 129
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-117 2.15e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 45.25  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   1 MAEKTQKSVKIAPGAVVCVESEIRG-DVTIGPRTVIHPKARIIAeAGPIIIGEGNLIEEQALIINAHPDNIIPDTEDPEP 79
Cdd:COG0110    1 MKLLLLFGARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIDD-PGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 149057926  80 KPMIIGtNNVFeVGCHSQAM---KMGDNNVIESKAYVGRNV 117
Cdd:COG0110   80 GPVTIG-DDVW-IGAGATILpgvTIGDGAVVGAGSVVTKDV 118
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 7-131 8.38e-06

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: 44.73  E-value: 8.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVvcveseIRGDVTIGPRTVIHPKARIiaeAGPIIIGEGNLIEEQALIINAHPDNiipdTEDPEPKPMIIGT 86
Cdd:cd03351   16 ENVEIGPFCV------IGPNVEIGDGTVIGSHVVI---DGPTTIGKNNRIFPFASIGEAPQDL----KYKGEPTRLEIGD 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149057926  87 NNVFEVGC--------HSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSL 131
Cdd:cd03351   83 NNTIREFVtihrgtaqGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATL 135
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 8-131 2.45e-05

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: 43.47  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   8 SVKIAPGAVV---CVeseIRGDVTIGPRTVIHPKARIiaeAGPIIIGEGNLIEEQALIinahpdniipdTEDP------- 77
Cdd:COG1043   13 GAKLGENVEIgpfCV---IGPDVEIGDGTVIGSHVVI---EGPTTIGKNNRIFPFASI-----------GEEPqdlkykg 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149057926  78 EPKPMIIGTNNVFEVGC--------HSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSL 131
Cdd:COG1043   76 EPTRLEIGDNNTIREFVtihrgtvqGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATL 137
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 11-155 4.46e-05

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 41.97  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  11 IAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQAlIINAHPDNIIPDTEDPEpkpmiIGTNNVF 90
Cdd:cd04745    3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNC-VIHGFPGQDTVLEENGH-----IGHGAIL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149057926  91 EvGCH--SQAMkMGDNNVIESKAYVGRNviltsgCIIGACCSLNTFEAIPENTVIYG--ADCLRRVQTE 155
Cdd:cd04745   77 H-GCTigRNAL-VGMNAVVMDGAVIGEE------SIVGAMAFVKAGTVIPPRSLIAGspAKVIRELSDE 137
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
7-131 8.70e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926   7 KSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAE---------AGPIIIGEGNLIeeqaliinaHPDNIIpdTEDP 77
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGtvigshvviDGHTTIGKNNRI---------FPFASI--GEDP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149057926  78 -------EPKPMIIGTNNVFEVGC--------HSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSL 131
Cdd:PRK05289  70 qdlkykgEPTRLVIGDNNTIREFVtinrgtvqGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATL 138
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 17-143 2.19e-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: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  17 VCVESEIRG--DVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIInahPDNIIpdtEDPEPK--PMIIGTNNVFEV 92
Cdd:cd03359   10 VSRKSVICGsqNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIR---PPFKK---FSKGVAffPLHIGDYVFIGE 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149057926  93 GCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGAccslNTfeAIPENTVI 143
Cdd:cd03359   84 NCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILD----GT--VVPPDTVI 128
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 6-151 2.84e-04

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: 40.32  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926    6 QKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARI---------IAEAGPIIIGEGNLIEEQALIinaHPDNiipdteD 76
Cdd:TIGR01852  26 GPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIggvpqdlkyKGEKTRLIIGDNNTIREFVTI---NRGT------A 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149057926   77 PEPKPMIIGTNNVFEVGCH-SQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRR 151
Cdd:TIGR01852  97 SGGGVTRIGNNNLLMAYSHiAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSK 172
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 56-149 2.20e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  56 IEEQALIinaHPDNIIPDTedpepkpMIIGTNNVFEVGChsqamKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNtfe 135
Cdd:PRK00892 103 IHPSAVI---DPSAKIGEG-------VSIGPNAVIGAGV-----VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIY--- 164

                         90
                 ....*....|....
gi 149057926 136 aipENTVIyGADCL 149
Cdd:PRK00892 165 ---HAVRI-GNRVI 174
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 26-146 2.78e-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: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  26 DVTIGPRTVIHPKARIIAEAGpIIIGEGNLIEEQALIINA-HPdniIPDTEDPEPKPMIIGtnnvfEVgchsqamkmgdn 104
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGG-ITIGDNVLIGPNVTIYDHnHD---IDDPERPIEQGVTSA-----PI------------ 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 149057926 105 nVIESKAYVGRNVILTSG------CIIGAcCSLNTFEaIPENTVIYGA 146
Cdd:cd04647   60 -VIGDDVWIGANVVILPGvtigdgAVVGA-GSVVTKD-VPPNSIVAGN 104
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-62 3.05e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 3.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 149057926  23 IRGDVTIGPRTVIHPKARIiaeAGPIIIGEGNLIEEQALI 62
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCI---SGDTRIGEGCTIEQGVVI 301
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 11-128 3.53e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057926  11 IAPGAVVCVESEIRGDVTIGPRTVIHPKARIiaeagpiiiGEGNlieeqaliinahpdniipdtedpepkpmIIGTNNVF 90
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVI---------GDGV----------------------------VIGAGAVI 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 149057926  91 EVGChsqamKMGDNNVIESKA------YVGRNVILTSGCIIGAC 128
Cdd:PRK00892 146 GDGV-----KIGADCRLHANVtiyhavRIGNRVIIHSGAVIGSD 184
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 11-56 6.03e-03

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: 35.92  E-value: 6.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 149057926  11 IAPGAVVCveseirGDVTIGPRTVIHPKARIIaeaGPIIIGEGNLI 56
Cdd:cd03360  141 IAPGVVLS------GGVTIGEGAFIGAGATII---QGVTIGAGAII 177
 
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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