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Conserved domains on  [gi|1972227313|ref|NP_001380049|]
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Dynactin subunit 5 [Caenorhabditis elegans]

Protein Classification

dynactin subunit 5( domain architecture ID 10129731)

dynactin subunit 5 is a member of the pointed-end complex of the dynactin shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 13-173 1.77e-82

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: 240.96  E-value: 1.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  13 WAKTHTGNKVNKKHAIAGTQNILIAGKTIIEEGVTIRGDLATVKIGKYCVLKSRCNIRPCMKIFSKKPTMCNVMIGDYVF 92
Cdd:cd03359     1 YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  93 IEEECVVNAAQIYAFVHLGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVVGTEPRCTENLMMEAITMY 172
Cdd:cd03359    81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEY 160


                  .
gi 1972227313 173 Y 173
Cdd:cd03359   161 Y 161
 
Name Accession Description Interval E-value
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 13-173 1.77e-82

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: 240.96  E-value: 1.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  13 WAKTHTGNKVNKKHAIAGTQNILIAGKTIIEEGVTIRGDLATVKIGKYCVLKSRCNIRPCMKIFSKKPTMCNVMIGDYVF 92
Cdd:cd03359     1 YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  93 IEEECVVNAAQIYAFVHLGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVVGTEPRCTENLMMEAITMY 172
Cdd:cd03359    81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEY 160


                  .
gi 1972227313 173 Y 173
Cdd:cd03359   161 Y 161
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
33-156 4.42e-10

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 55.26  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTIRGdlATVKIGKYCVLKSRCNIrpcmkifskkPTMCNVMIGDYVFIEEECVVNAAQ--------- 103
Cdd:COG0110     8 GARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTI----------DDPGGITIGDNVLIGPGVTILTGNhpiddpatf 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972227313 104 --------IYAFVHLGARAVLGNGCVIRECSRVLPDTVVPADalFPPYSTIGGNPAQVVGT 156
Cdd:COG0110    76 plrtgpvtIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD--VPPYAIVAGNPARVIRK 134
PLN02472 PLN02472
uncharacterized protein
 33-154 2.34e-04

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 40.33  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTI------RGDLATVKIGKYCVLKSRCNIRPCMKIFSKKPTmcNVMIGDYVFIEEECVVNAAQIYA 106
Cdd:PLN02472   71 NVVLAGQVTVWDGASVwngavlRGDLNKITVGFCSNVQERCVLHAAWNSPTGLPA--ETLIDRYVTIGAYSLLRSCTIEP 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1972227313 107 FVHLGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVV 154
Cdd:PLN02472  149 ECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFV 196
 
Name Accession Description Interval E-value
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 13-173 1.77e-82

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: 240.96  E-value: 1.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  13 WAKTHTGNKVNKKHAIAGTQNILIAGKTIIEEGVTIRGDLATVKIGKYCVLKSRCNIRPCMKIFSKKPTMCNVMIGDYVF 92
Cdd:cd03359     1 YIETASGNKVSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  93 IEEECVVNAAQIYAFVHLGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVVGTEPRCTENLMMEAITMY 172
Cdd:cd03359    81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEY 160


                  .
gi 1972227313 173 Y 173
Cdd:cd03359   161 Y 161
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 36-156 4.79e-11

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: 57.81  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  36 IAGKTIIEE------GVTIRGDLATVKIGKYCVLKSRCNIRpcmkIFSKKPTMcnvmIGDYVFIEEECVVNAAQIYAFVH 109
Cdd:cd04645    14 VIGDVTLGEgssvwfGAVLRGDVNPIRIGERTNIQDGSVLH----VDPGYPTI----IGDNVTVGHGAVLHGCTIGDNCL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1972227313 110 LGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVVGT 156
Cdd:cd04645    86 IGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRE 132
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 33-173 5.78e-11

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 57.97  E-value: 5.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTIRGDLATVKIGKYCVLKSRCNIRPCMKIfskkptmcNVMIGDYVFIEEECVVNAAQIYAFVHLGA 112
Cdd:cd04650    18 DVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGY--------PTEIGDYVTIGHNAVVHGAKVGNYVIVGM 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972227313 113 RAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVVgTEPRCTENLMMEAITMYY 173
Cdd:cd04650    90 GAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVV-RKLTEEEIEWIKKNAEEY 149
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
33-156 4.42e-10

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 55.26  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTIRGdlATVKIGKYCVLKSRCNIrpcmkifskkPTMCNVMIGDYVFIEEECVVNAAQ--------- 103
Cdd:COG0110     8 GARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTI----------DDPGGITIGDNVLIGPGVTILTGNhpiddpatf 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972227313 104 --------IYAFVHLGARAVLGNGCVIRECSRVLPDTVVPADalFPPYSTIGGNPAQVVGT 156
Cdd:COG0110    76 plrtgpvtIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD--VPPYAIVAGNPARVIRK 134
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 36-156 2.44e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.88  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  36 IAGKTIIEEGV------TIRGDLATVKIGKYCVLKSRCNIRpcmkIFSKKPTMcnvmIGDYVFIEEECVVNAAQI--YAF 107
Cdd:COG0663    25 VIGDVTIGEDVsvwpgaVLRGDVGPIRIGEGSNIQDGVVLH----VDPGYPLT----IGDDVTIGHGAILHGCTIgdNVL 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972227313 108 VHLGA----RAVLGNGCVIRECSRVLPDTVVPadalfpPYSTIGGNPAQVVGT 156
Cdd:COG0663    97 IGMGAivldGAVIGDGSIVGAGALVTEGKVVP------PGSLVVGSPAKVVRE 143
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 42-122 3.21e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 46.16  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  42 IEEGVTIrGDLATvkIGKYCVLKSRCNIRPcmkifskkptmcNVMIGDYVFIEEECVVNA-AQIYAFVHLGARAVLGNGC 120
Cdd:COG1044   111 IGEGVSI-GPFAV--IGAGVVIGDGVVIGP------------GVVIGDGVVIGDDCVLHPnVTIYERCVIGDRVIIHSGA 175


                  ..
gi 1972227313 121 VI 122
Cdd:COG1044   176 VI 177
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 33-154 2.67e-05

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: 41.29  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTIrGDLATVKIGKYCVLKSRCNI-----------RPCMKIFSKKPtmcnVMIGDYVFIeeecvvna 101
Cdd:cd04647     1 NISIGDNVYIGPGCVI-SAGGGITIGDNVLIGPNVTIydhnhdiddpeRPIEQGVTSAP----IVIGDDVWI-------- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972227313 102 aqiyafvhlGARAVLGNGCVIRECSRVLPDTVVPADalFPPYSTIGGNPAQVV 154
Cdd:cd04647    68 ---------GANVVILPGVTIGDGAVVGAGSVVTKD--VPPNSIVAGNPAKVI 109
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 84-134 2.80e-05

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: 43.47  E-value: 2.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972227313  84 NVMIGDYVFIEEECVVNA-AQIYAFVHLGARAVLGNGCVIRECSRVLPDTVV 134
Cdd:COG1044   114 GVSIGPFAVIGAGVVIGDgVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVI 165
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 55-147 1.33e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 38.77  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  55 VKIGKYCVLKSRCNIRPCmkifskkptmcnVMIGDYVFIEEECVVNAAQIYafvHLGARAVLGNGCVIRECSRVLPDTVV 134
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGP------------VVIGDNVNIGPGAVIGAATGP---NEKNPTIIGDNVEIGANAVIHGGVKI 65

                          90
                  ....*....|...
gi 1972227313 135 PADALFPPYSTIG 147
Cdd:cd00208    66 GDNAVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 84-148 1.38e-04

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: 40.85  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972227313  84 NVMIGDYVFIEEECVV-NAAQIYAFVHLGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGG 148
Cdd:cd03352     7 NVSIGPNAVIGEGVVIgDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGS 72
PLN02472 PLN02472
uncharacterized protein
 33-154 2.34e-04

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 40.33  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTI------RGDLATVKIGKYCVLKSRCNIRPCMKIFSKKPTmcNVMIGDYVFIEEECVVNAAQIYA 106
Cdd:PLN02472   71 NVVLAGQVTVWDGASVwngavlRGDLNKITVGFCSNVQERCVLHAAWNSPTGLPA--ETLIDRYVTIGAYSLLRSCTIEP 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1972227313 107 FVHLGARAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVV 154
Cdd:PLN02472  149 ECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFV 196
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 36-155 2.62e-04

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: 39.02  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  36 IAGKTIIEEGVTIRGDlatVKIGKYCVLKSRCNIRPcmkifskkptmcNVMIGDYVFIEEECV----------VNAAQIY 105
Cdd:cd03358     1 IGDNCIIGTNVFIEND---VKIGDNVKIQSNVSIYE------------GVTIEDDVFIGPNVVftndlyprskIYRKWEL 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972227313 106 AFVHLGARAVLGNGCVIRECSRVLPDTVVPADALF----PPYSTIGGNPAQVVG 155
Cdd:cd03358    66 KGTTVKRGASIGANATILPGVTIGEYALVGAGAVVtkdvPPYALVVGNPARIIG 119
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 33-135 3.41e-04

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: 39.23  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTIRGDLATVKIGKYCVLKSRCNIRpcmKIFSKKPTMCNVM-IGDYVFIEEECVVNAAQIYAFVHLG 111
Cdd:cd04646    17 DVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIV---NKKPKDPAEPKPMiIGSNNVFEVGCKCEALKIGNNNVFE 93

                          90       100       110
                  ....*....|....*....|....*....|
gi 1972227313 112 ARAVLG------NGCVIRECSRVLPDTVVP 135
Cdd:cd04646    94 SKSFVGknviitDGCIIGAGCKLPSSEILP 123
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 36-122 5.76e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  36 IAGKTIIEEGVTIrGDLATvkIGKYCVLKSRCNIRPcmkifskkptmcNVMIGDYVFIEEECVVNA-AQIYAFVHLGARA 114
Cdd:PRK00892  109 IDPSAKIGEGVSI-GPNAV--IGAGVVIGDGVVIGA------------GAVIGDGVKIGADCRLHAnVTIYHAVRIGNRV 173


                  ....*...
gi 1972227313 115 VLGNGCVI 122
Cdd:PRK00892  174 IIHSGAVI 181
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
40-155 6.36e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  40 TIIEEGVTIRGD----LATVKIGKYCVLKSRCnirpcmkIFSKkptmcNVM------IGDYVFIEEECVVNaaQiyaFVH 109
Cdd:PRK05289   99 TVQGGGVTRIGDnnllMAYVHVAHDCVVGNHV-------ILAN-----NATlaghveVGDYAIIGGLTAVH--Q---FVR 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1972227313 110 LGARAVLGnGCvirecSRVLPDTvvpadalfPPYSTIGGNPAQVVG 155
Cdd:PRK05289  162 IGAHAMVG-GM-----SGVSQDV--------PPYVLAEGNPARLRG 193
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 40-155 9.78e-04

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: 38.46  E-value: 9.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  40 TIIEEGVTIRGD----LATVKIGKYCVLKSRCnirpcmkIFSKkptmcNVMIGDYVFIEEECVV--NAAqIYAFVHLGAR 113
Cdd:COG1043    98 TVQGGGVTRIGDdnllMAYVHVAHDCVVGNNV-------ILAN-----NATLAGHVEVGDHAIIggLSA-VHQFVRIGAH 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1972227313 114 AVLGNGCVIRecsrvlpdtvvpADAlfPPYSTIGGNPAQVVG 155
Cdd:COG1043   165 AMVGGGSGVV------------KDV--PPYVLAAGNPARLRG 192
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 40-128 1.40e-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: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  40 TIIEEGVTIRGDlatVKIGKYCVLKSRCNIRPCMkifskkptmcnvmIGDYVFIEEECVVNAAQIYAFVHLGARAVLGNG 119
Cdd:cd03353    22 VVIDPGVILEGK---TVIGEDCVIGPNCVIKDST-------------IGDGVVIKASSVIEGAVIGNGATVGPFAHLRPG 85


                  ....*....
gi 1972227313 120 CVIRECSRV 128
Cdd:cd03353    86 TVLGEGVHI 94
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 33-154 2.74e-03

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: 36.58  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  33 NILIAGKTIIEEGVTIRGDLATVKIGKYCVLKSRCNIRpcmkIFSKKPTMcnvmIGDYVFIEEECVVNAAQIYAFVHLGA 112
Cdd:cd04745    18 DVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIH----GFPGQDTV----LEENGHIGHGAILHGCTIGRNALVGM 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1972227313 113 RAVLGNGCVIRECSRVLPDTVVPADALFPPYSTIGGNPAQVV 154
Cdd:cd04745    90 NAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVI 131
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 41-125 2.98e-03

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: 37.31  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  41 IIEEGVTIrGDlaTVKIGKYCVLKSRCNIRPCMKIFSkkptmcNVMIGDYVFIEEECvvnaaQIYAFVHLGA-------- 112
Cdd:COG1043     9 IVDPGAKL-GE--NVEIGPFCVIGPDVEIGDGTVIGS------HVVIEGPTTIGKNN-----RIFPFASIGEepqdlkyk 74

                          90
                  ....*....|....*..
gi 1972227313 113 ----RAVLGNGCVIREC 125
Cdd:COG1043    75 geptRLEIGDNNTIREF 91
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 36-155 5.13e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.54  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  36 IAGKTIIEEGVTI-RGDLA-TV-KIGKYCVLKSRCNIRPcmkifskkptmcNVMIGDYVFieeecVVNAAQIYAFVHLGA 112
Cdd:PRK12461   80 IGDRNVIREGVTIhRGTKGgGVtRIGNDNLLMAYSHVAH------------DCQIGNNVI-----LVNGALLAGHVTVGD 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1972227313 113 RAVLGNGCVIRECSRV------LPDTVVPADAlfPPYSTIGGNPAQVVG 155
Cdd:PRK12461  143 RAIISGNCLVHQFCRIgalammAGGSRISKDV--PPYCMMAGHPTNVHG 189
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
41-125 6.05e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 36.23  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  41 IIEEGVTIrGDlaTVKIGKYCVLKSrcnirpcmkifskkptmcNVMIGDYVFIEEECVVNAA-------QIYAFVHLGA- 112
Cdd:PRK05289   10 IVEPGAKI-GE--NVEIGPFCVIGP------------------NVVIGDGTVIGSHVVIDGHttigknnRIFPFASIGEd 68

                          90       100
                  ....*....|....*....|....
gi 1972227313 113 -----------RAVLGNGCVIREC 125
Cdd:PRK05289   69 pqdlkykgeptRLVIGDNNTIREF 92
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 40-155 7.58e-03

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: 35.87  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  40 TIIEEGVTIRGD----LATVKIGKYCVLKSRCnirpcmkIFSKKPTMC-NVMIGDYVFIEEECVVNaaQiyaFVHLGARA 114
Cdd:cd03351    96 TAQGGGVTRIGNnnllMAYVHVAHDCVIGNNV-------ILANNATLAgHVEIGDYAIIGGLSAVH--Q---FCRIGRHA 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1972227313 115 VLGNGCVIREcsrvlpdtvvpaDAlfPPYSTIGGNPAQVVG 155
Cdd:cd03351   164 MVGGGSGVVQ------------DV--PPYVIAAGNRARLRG 190
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 41-136 9.24e-03

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 33.71  E-value: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227313  41 IIEEGVTIrGDLATVK---IGKYCVLKSRCNIrpcmkifskkpTMCNVMigDYVFIEEECVVNAAQIyafvhlGARAVLG 117
Cdd:cd04652     1 LVGENTQV-GEKTSIKrsvIGANCKIGKRVKI-----------TNCVIM--DNVTIEDGCTLENCII------GNGAVIG 60

                          90
                  ....*....|....*....
gi 1972227313 118 NGCVIRECSrVLPDTVVPA 136
Cdd:cd04652    61 EKCKLKDCL-VGSGYRVEA 78
 
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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