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Conserved domains on  [gi|513012678|ref|XP_004867712|]
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dynactin subunit 6 [Heterocephalus glaber]

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 1.53e-97

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: 279.60  E-value: 1.53e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  10 KIAPGAVVCVESEIRGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIINAHPDNItpdtddPEPKPMIIGTNNV 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP------AEPKPMIIGSNNV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  90 FEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEVIPENTVIYGGDCLRRVQTERPQPQTLQLDFLMK 169
Cdd:cd04646   75 FEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTDRPKPQTLQLDFLRK 154

                        170
                 ....*....|
gi 513012678 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 1.53e-97

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: 279.60  E-value: 1.53e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  10 KIAPGAVVCVESEIRGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIINAHPDNItpdtddPEPKPMIIGTNNV 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP------AEPKPMIIGSNNV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  90 FEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEVIPENTVIYGGDCLRRVQTERPQPQTLQLDFLMK 169
Cdd:cd04646   75 FEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTDRPKPQTLQLDFLRK 154

                        170
                 ....*....|
gi 513012678 170 ILPNYHHLKK 179
Cdd:cd04646  155 ILPNYHHLKK 164
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 7-179 3.56e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.19  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVVCveseirGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIinaHpdnITPDTddpepkPMIIGT 86
Cdd:COG0663   15 PSAFVAPTAVVI------GDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVL---H---VDPGY------PLTIGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  87 N-----NVFEVGCYsqamkMGDNNVIESKAYVGRNVILTSGCIIGACC--SLNTfeVIPENTVIYG--GDCLRRVQTErp 157
Cdd:COG0663   77 DvtighGAILHGCT-----IGDNVLIGMGAIVLDGAVIGDGSIVGAGAlvTEGK--VVPPGSLVVGspAKVVRELTEE-- 147

                        170       180
                 ....*....|....*....|..
gi 513012678 158 qpqtlQLDFLMKILPNYHHLKK 179
Cdd:COG0663  148 -----EIAFLRESAENYVELAR 164
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-149 8.15e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 53.49  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVvcveseIRGDVTIGPRTVVHPKARIIaeaGPIVIGEGNLIEEQAlIINAHPDNITPDTddpEPKPMIIGT 86
Cdd:PRK12461  16 SGVEIGPFAV------IGANVEIGDGTWIGPHAVIL---GPTRIGKNNKIHQGA-VVGDEPQDFTYKG---EESRLEIGD 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  87 NNVFEVGCY-------SQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTfEVIPENTVIYGGDCL 149
Cdd:PRK12461  83 RNVIREGVTihrgtkgGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAG-HVTVGDRAIISGNCL 151
 
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 1.53e-97

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: 279.60  E-value: 1.53e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  10 KIAPGAVVCVESEIRGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIINAHPDNItpdtddPEPKPMIIGTNNV 89
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDP------AEPKPMIIGSNNV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  90 FEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEVIPENTVIYGGDCLRRVQTERPQPQTLQLDFLMK 169
Cdd:cd04646   75 FEVGCKCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLRRTQTDRPKPQTLQLDFLRK 154

                        170
                 ....*....|
gi 513012678 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 9.64e-13

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: 60.73  E-value: 9.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  27 VTIGPRTVVHPKARIIaeaGPIVIGEGNLIEEQALIINAHPDNitpdtddpEPKPMIIGTNNVFEVGC-YSQAMKMGDNN 105
Cdd:cd00208    1 VFIGEGVKIHPKAVIR---GPVVIGDNVNIGPGAVIGAATGPN--------EKNPTIIGDNVEIGANAvIHGGVKIGDNA 69


                 ....*....
gi 513012678 106 VIESKAYVG 114
Cdd:cd00208   70 VIGAGAVVT 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 7-179 3.56e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.19  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVVCveseirGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIinaHpdnITPDTddpepkPMIIGT 86
Cdd:COG0663   15 PSAFVAPTAVVI------GDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVL---H---VDPGY------PLTIGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  87 N-----NVFEVGCYsqamkMGDNNVIESKAYVGRNVILTSGCIIGACC--SLNTfeVIPENTVIYG--GDCLRRVQTErp 157
Cdd:COG0663   77 DvtighGAILHGCT-----IGDNVLIGMGAIVLDGAVIGDGSIVGAGAlvTEGK--VVPPGSLVVGspAKVVRELTEE-- 147

                        170       180
                 ....*....|....*....|..
gi 513012678 158 qpqtlQLDFLMKILPNYHHLKK 179
Cdd:COG0663  148 -----EIAFLRESAENYVELAR 164
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 7-146 1.44e-09

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: 53.95  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVVCveseirGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIinaHPDnitpdtddpEPKPMIIGT 86
Cdd:cd04645    4 PSAFIAPNATVI------GDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVL---HVD---------PGYPTIIGD 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 513012678  87 N-----NVFEVGCysqamKMGDNNVIESKAYVGRNVILTSGCIIGAccslNTfeVIPENTVIYGG 146
Cdd:cd04645   66 NvtvghGAVLHGC-----TIGDNCLIGMGAIILDGAVIGKGSIVAA----GS--LVPPGKVIPPG 119
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-149 8.15e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 53.49  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVvcveseIRGDVTIGPRTVVHPKARIIaeaGPIVIGEGNLIEEQAlIINAHPDNITPDTddpEPKPMIIGT 86
Cdd:PRK12461  16 SGVEIGPFAV------IGANVEIGDGTWIGPHAVIL---GPTRIGKNNKIHQGA-VVGDEPQDFTYKG---EESRLEIGD 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  87 NNVFEVGCY-------SQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTfEVIPENTVIYGGDCL 149
Cdd:PRK12461  83 RNVIREGVTihrgtkgGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAG-HVTVGDRAIISGNCL 151
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-145 3.65e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 41.78  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   1 MAEKTQKSVKIAPGAVVCVESEIRG-DVTIGPRTVVHPKARIIAeAGPIVIGEGNLIEEQALIINAHPDNITPDTDDPEP 79
Cdd:COG0110    1 MKLLLLFGARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIDD-PGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  80 KPMIIGtNNVFevgcysqamkmgdnnvIESKAYVGRNVILTSGCIIGACCslntfeV----IPENTVIYG 145
Cdd:COG0110   80 GPVTIG-DDVW----------------IGAGATILPGVTIGDGAVVGAGS------VvtkdVPPYAIVAG 126
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 7-149 3.88e-05

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: 42.80  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVvcveseIRGDVTIGPRTVVHPKARIiaeAGPIVIGEGNLIEEQALIINAHPDNitpdTDDPEPKPMIIGT 86
Cdd:cd03351   16 ENVEIGPFCV------IGPNVEIGDGTVIGSHVVI---DGPTTIGKNNRIFPFASIGEAPQDL----KYKGEPTRLEIGD 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513012678  87 NNVFEVGCY--------SQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTfEVIPENTVIYGGDCL 149
Cdd:cd03351   83 NNTIREFVTihrgtaqgGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAG-HVEIGDYAIIGGLSA 152
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 17-143 9.94e-05

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: 41.05  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  17 VCVESEIRG--DVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQALIINahPDNITPDTddPEPKPMIIGTNNVFEVGC 94
Cdd:cd03359   10 VSRKSVICGsqNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRP--PFKKFSKG--VAFFPLHIGDYVFIGENC 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 513012678  95 YSQAMKMGDNNVIESKAYVGRNVILTSGCIIGAccslNTfeVIPENTVI 143
Cdd:cd03359   86 VVNAAQIGSYVHIGKNCVIGRRCIIKDCVKILD----GT--VVPPDTVI 128
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 7-131 1.95e-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: 40.77  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVvcveseIRGDVTIGPRTVVHPKARIiaeAGPIVIGEGNLIEEQALIinahpdnitpdTDDP-------EP 79
Cdd:COG1043   18 ENVEIGPFCV------IGPDVEIGDGTVIGSHVVI---EGPTTIGKNNRIFPFASI-----------GEEPqdlkykgEP 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  80 KPMIIGTNNVFEVGC--------YSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSL 131
Cdd:COG1043   78 TRLEIGDNNTIREFVtihrgtvqGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATL 137
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
7-131 2.87e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.47  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678   7 KSVKIAPGAVVCVESEIRGDVTIGPRTVVHPKARIIAE---------AGPIVIGEGNLIEEQALIINAHPDNitpdTDDP 77
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGtvigshvviDGHTTIGKNNRIFPFASIGEDPQDL----KYKG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513012678  78 EPKPMIIGTNNVFEVGC--------YSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSL 131
Cdd:PRK05289  77 EPTRLVIGDNNTIREFVtinrgtvqGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATL 138
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 11-145 4.43e-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: 38.89  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  11 IAPGAVVCVESEIRGDVTIGPRTVVHPKARIIAEAGPIVIGEGNLIEEQAlIINAHPDNITPDTDDPEpkpmiIGTNNVF 90
Cdd:cd04745    3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNC-VIHGFPGQDTVLEENGH-----IGHGAIL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 513012678  91 EvGCY--SQAMkMGDNNVIESKAYVGRNviltsgCIIGACCSLNTFEVIPENTVIYG 145
Cdd:cd04745   77 H-GCTigRNAL-VGMNAVVMDGAVIGEE------SIVGAMAFVKAGTVIPPRSLIAG 125
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 84-146 1.97e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 513012678  84 IGTNNVFEVGCysqamKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEVIPENTVIYGG 146
Cdd:PRK00892 121 IGPNAVIGAGV-----VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSG 178
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-62 2.42e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.80  E-value: 2.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 513012678  23 IRGDVTIGPRTVVHPKARIiaeAGPIVIGEGNLIEEQALI 62
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCI---SGDTRIGEGCTIEQGVVI 301
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 11-128 9.41e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 35.89  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513012678  11 IAPGAVVCVESEIRGDVTIGPRTVVHPKAriiaeagpiVIGEGNlieeqaliinahpdnitpdtddpepkpmIIGTNNVF 90
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGV---------VIGDGV----------------------------VIGAGAVI 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 513012678  91 EVGCysqamKMGDNNVIESKA------YVGRNVILTSGCIIGAC 128
Cdd:PRK00892 146 GDGV-----KIGADCRLHANVtiyhavRIGNRVIIHSGAVIGSD 184
 
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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