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Conserved domains on  [gi|568954042|ref|XP_006509157|]
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dynactin subunit 6 isoform X1 [Mus musculus]

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 ...
 10-197 5.85e-92

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: 266.11  E-value: 5.85e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  10 KIAPGAVVCVESEIRGDVTIEcmwlssplrrntssqlfcPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIi 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIG------------------PGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  90 pdtedTEPKPMIIGTNNVFEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRR 169
Cdd:cd04646   62 -----AEPKPMIIGSNNVFEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRR 136

                        170       180
                 ....*....|....*....|....*...
gi 568954042 170 VQTERPQPQTLQLDFLMKILPNYHHLKK 197
Cdd:cd04646  137 TQTDRPKPQTLQLDFLRKILPNYHHLKK 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 ...
 10-197 5.85e-92

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: 266.11  E-value: 5.85e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  10 KIAPGAVVCVESEIRGDVTIEcmwlssplrrntssqlfcPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIi 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIG------------------PGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  90 pdtedTEPKPMIIGTNNVFEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRR 169
Cdd:cd04646   62 -----AEPKPMIIGSNNVFEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRR 136

                        170       180
                 ....*....|....*....|....*...
gi 568954042 170 VQTERPQPQTLQLDFLMKILPNYHHLKK 197
Cdd:cd04646  137 TQTDRPKPQTLQLDFLRKILPNYHHLKK 164
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 7-202 1.73e-06

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 46.17  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042   7 KSVKIAPGAVVCveseirGDVTIEcmwlssplrRNTSsqlfcprtvIHPKARIIAEAGPIIIGEGNLIEEQALIinaHPD 86
Cdd:COG0663   15 PSAFVAPTAVVI------GDVTIG---------EDVS---------VWPGAVLRGDVGPIRIGEGSNIQDGVVL---HVD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  87 niipdtedtEPKPMIIGtNNVFeVGcHsQAM----KMGDNNVIESKAYVGRNVILTSGCIIGACC--SLNTFeaIPENTV 160
Cdd:COG0663   68 ---------PGYPLTIG-DDVT-IG-H-GAIlhgcTIGDNVLIGMGAIVLDGAVIGDGSIVGAGAlvTEGKV--VPPGSL 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568954042 161 IYG--ADCLRRVQTErpqpqtlQLDFLMKILPNYHHLKKTMKGS 202
Cdd:COG0663  133 VVGspAKVVRELTEE-------EIAFLRESAENYVELARRYLAE 169
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 44-167 6.45e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  44 SQLFcprtviHPKARIIAEAGpiiigegnlIEEQALIinaHPDNIIPDTedtepkpMIIGTNNVFEVGChsqamKMGDNN 123
Cdd:PRK00892  88 AQLF------DPPATPSPAAG---------IHPSAVI---DPSAKIGEG-------VSIGPNAVIGAGV-----VIGDGV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568954042 124 VIESKAYVGRNVILTSGCIIGACCSLNtfeaipENTVIyGADCL 167
Cdd:PRK00892 138 VIGAGAVIGDGVKIGADCRLHANVTIY------HAVRI-GNRVI 174
 
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 ...
 10-197 5.85e-92

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: 266.11  E-value: 5.85e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  10 KIAPGAVVCVESEIRGDVTIEcmwlssplrrntssqlfcPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIi 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIG------------------PGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  90 pdtedTEPKPMIIGTNNVFEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRR 169
Cdd:cd04646   62 -----AEPKPMIIGSNNVFEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRR 136

                        170       180
                 ....*....|....*....|....*...
gi 568954042 170 VQTERPQPQTLQLDFLMKILPNYHHLKK 197
Cdd:cd04646  137 TQTDRPKPQTLQLDFLRKILPNYHHLKK 164
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 49-132 4.92e-11

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: 56.49  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  49 PRTVIHPKARIIaeaGPIIIGEGNLIEEQALIINAhpdniipdTEDTEPKPMIIGTNNVFEVGCH-SQAMKMGDNNVIES 127
Cdd:cd00208    5 EGVKIHPKAVIR---GPVVIGDNVNIGPGAVIGAA--------TGPNEKNPTIIGDNVEIGANAViHGGVKIGDNAVIGA 73


                 ....*
gi 568954042 128 KAYVG 132
Cdd:cd00208   74 GAVVT 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 7-202 1.73e-06

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 46.17  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042   7 KSVKIAPGAVVCveseirGDVTIEcmwlssplrRNTSsqlfcprtvIHPKARIIAEAGPIIIGEGNLIEEQALIinaHPD 86
Cdd:COG0663   15 PSAFVAPTAVVI------GDVTIG---------EDVS---------VWPGAVLRGDVGPIRIGEGSNIQDGVVL---HVD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  87 niipdtedtEPKPMIIGtNNVFeVGcHsQAM----KMGDNNVIESKAYVGRNVILTSGCIIGACC--SLNTFeaIPENTV 160
Cdd:COG0663   68 ---------PGYPLTIG-DDVT-IG-H-GAIlhgcTIGDNVLIGMGAIVLDGAVIGDGSIVGAGAlvTEGKV--VPPGSL 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568954042 161 IYG--ADCLRRVQTErpqpqtlQLDFLMKILPNYHHLKKTMKGS 202
Cdd:COG0663  133 VVGspAKVVRELTEE-------EIAFLRESAENYVELARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 7-161 1.01e-04

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 40.86  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042   7 KSVKIAPGAVVCveseirGDVTIEcmwlssplrrntssqlfcPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIinaHPD 86
Cdd:cd04645    4 PSAFIAPNATVI------GDVTLG------------------EGSSVWFGAVLRGDVNPIRIGERTNIQDGSVL---HVD 56

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954042  87 niipdtedtEPKPMIIGtNNVFeVGcHsQAM----KMGDNNVIESKAYVGRNVILTSGCIIGAccslNTFeaIPENTVI 161
Cdd:cd04645   57 ---------PGYPTIIG-DNVT-VG-H-GAVlhgcTIGDNCLIGMGAIILDGAVIGKGSIVAA----GSL--VPPGKVI 116
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 44-167 6.45e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  44 SQLFcprtviHPKARIIAEAGpiiigegnlIEEQALIinaHPDNIIPDTedtepkpMIIGTNNVFEVGChsqamKMGDNN 123
Cdd:PRK00892  88 AQLF------DPPATPSPAAG---------IHPSAVI---DPSAKIGEG-------VSIGPNAVIGAGV-----VIGDGV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568954042 124 VIESKAYVGRNVILTSGCIIGACCSLNtfeaipENTVIyGADCL 167
Cdd:PRK00892 138 VIGAGAVIGDGVKIGADCRLHANVTIY------HAVRI-GNRVI 174
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-144 1.05e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.85  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042   7 KSVKIAPGAVVCVESEIrGDvtiecmwlssplrrntssqlfcpRTVIHPKARIIaeaGPIIIGEGNLIEEQAlIINAHPD 86
Cdd:PRK12461  16 SGVEIGPFAVIGANVEI-GD-----------------------GTWIGPHAVIL---GPTRIGKNNKIHQGA-VVGDEPQ 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568954042  87 NIipdTEDTEPKPMIIGTNNVFEVGC--H-----SQAMKMGDNNVIESKAYVGRNVILTSGCIIG 144
Cdd:PRK12461  68 DF---TYKGEESRLEIGDRNVIREGVtiHrgtkgGGVTRIGNDNLLMAYSHVAHDCQIGNNVILV 129
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 50-161 1.44e-03

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: 37.96  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  50 RTVIHPKARIIAEAGPIIIGEGNLIEEQALIINahPDNIIPDTEDTepKPMIIGTNNVFEVGCHSQAMKMGDNNVIESKA 129
Cdd:cd03359   27 KTIIQSDVIIRGDLATVSIGRYCILSEGCVIRP--PFKKFSKGVAF--FPLHIGDYVFIGENCVVNAAQIGSYVHIGKNC 102

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568954042 130 YVGRNVILTSGCIIGAccslNTfeAIPENTVI 161
Cdd:cd03359  103 VIGRRCIIKDCVKILD----GT--VVPPDTVI 128
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 51-163 3.69e-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: 37.08  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954042  51 TVIHPKARIIAEAgpiIIGEGNLIeeqaliinaHPDNII-PDTEdtepkpmiIGTNNVFEVGC----HSqamKMGDNN-- 123
Cdd:cd03360   85 TLIHPSAVVSPSA---VIGEGCVI---------MAGAVInPDAR--------IGDNVIINTGAvighDC---VIGDFVhi 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568954042 124 ----------VIESKAYVG------RNVILTSGCIIGACCSLntFEAIPENTVIYG 163
Cdd:cd03360  142 apgvvlsggvTIGEGAFIGagatiiQGVTIGAGAIIGAGAVV--TKDVPDGSVVVG 195
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 107-167 9.19e-03

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: 36.15  E-value: 9.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954042 107 VFEVGCHSQAM-----KMGDNNVIESKAYVGRNVILTSGCIIGACCSlntfeaIPENTVIyGADCL 167
Cdd:COG1044   94 APAPGIHPSAVidpsaKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVV------IGDGVVI-GDDCV 152
 
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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