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Conserved domains on  [gi|446562610|ref|WP_000639956|]
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lipopolysaccharide core heptose(II) kinase RfaY [Escherichia coli]

Protein Classification

lipopolysaccharide core heptose(II) kinase RfaY( domain architecture ID 10013499)

lipopolysaccharide core heptose(II) kinase RfaY catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10359 PRK10359
lipopolysaccharide core heptose(II) kinase RfaY;
1-229 2.65e-121

lipopolysaccharide core heptose(II) kinase RfaY;


:

Pssm-ID: 182407  Cd Length: 232  Bit Score: 344.04  E-value: 2.65e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610   1 MIYNKTINGVKVFIKDNDPFYEQVLNDFLTCRVKTLKVFRSIDDTKVILIDTARGPLVLKVYAPKHKMTERFLKSCIKKD 80
Cdd:PRK10359   1 MITKKKIKGYTVFYKDNDNKYKEIFDDFLSYNIKTIKVFRNIDDTKVSLIDTDYGKYILKVFAPKVKRTERFLKSFVKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610  81 YYENLIYQTDRVRGEGIQSINDYFLLAERKTLNFAHYYIMLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVSGD 160
Cdd:PRK10359  81 YYENLIVQTDRVRSEGLASLNDFYLLAERKTLRYAHTYIMLIEYIEGVELNDMPEISEDVKAKIKASIESLHQHGMVSGD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610 161 PHKGNFIVSEKGLRLIDLSGKKTTAVLKAKDRIDLERHYNIKNELKDFGYTYLIFKKKIKKVIRDVKVK 229
Cdd:PRK10359 161 PHKGNFIVSKNGLRIIDLSGKRCTAQRKAKDRIDLERHYGIKNEIKDLGYYLLIYKKKLRKFIRKLKGK 229
 
Name Accession Description Interval E-value
PRK10359 PRK10359
lipopolysaccharide core heptose(II) kinase RfaY;
1-229 2.65e-121

lipopolysaccharide core heptose(II) kinase RfaY;


Pssm-ID: 182407  Cd Length: 232  Bit Score: 344.04  E-value: 2.65e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610   1 MIYNKTINGVKVFIKDNDPFYEQVLNDFLTCRVKTLKVFRSIDDTKVILIDTARGPLVLKVYAPKHKMTERFLKSCIKKD 80
Cdd:PRK10359   1 MITKKKIKGYTVFYKDNDNKYKEIFDDFLSYNIKTIKVFRNIDDTKVSLIDTDYGKYILKVFAPKVKRTERFLKSFVKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610  81 YYENLIYQTDRVRGEGIQSINDYFLLAERKTLNFAHYYIMLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVSGD 160
Cdd:PRK10359  81 YYENLIVQTDRVRSEGLASLNDFYLLAERKTLRYAHTYIMLIEYIEGVELNDMPEISEDVKAKIKASIESLHQHGMVSGD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610 161 PHKGNFIVSEKGLRLIDLSGKKTTAVLKAKDRIDLERHYNIKNELKDFGYTYLIFKKKIKKVIRDVKVK 229
Cdd:PRK10359 161 PHKGNFIVSKNGLRIIDLSGKRCTAQRKAKDRIDLERHYGIKNEIKDLGYYLLIYKKKLRKFIRKLKGK 229
WaaY pfam06176
Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial ...
 1-229 6.91e-91

Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial lipopolysaccharide core biosynthesis proteins (WaaY or RfaY). The waaY, waaQ, and waaP genes are located in the central operon of the waa (formerly rfa) locus on the chromosome of Escherichia coli. This locus contains genes whose products are involved in the assembly of the core region of the lipopolysaccharide molecule. WaaY is the enzyme that phosphorylates HepII in this system.


Pssm-ID: 283765  Cd Length: 229  Bit Score: 267.08  E-value: 6.91e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610    1 MIYNKTINGVKVFIKDNDPFYEQVLNDFLTCRVKTLKVFRSIDDTKVILIDTARGPLVLKVYAPKHKMTERFLKSCIKKD 80
Cdd:pfam06176   1 MITSIKIKGFSVFYKDNDNKYKEIFDDFLSYNFKTIKVFRNIDDTKVSLIDTDYGKYILKVFSPKVKRNERFFKSLVKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610   81 YYENLIYQTDRVRGEGIQSINDYFLLAERKTLNFAHYYIMLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVSGD 160
Cdd:pfam06176  81 YYENLFVQTDRVRSEGLTFLNDFYLLAERKTLRYVSTYIMIIEYIEGIELNDMPIIPDNVKAKIKQSIEKLHQHGMVSGD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610  161 PHKGNFIVSEKGLRLIDLSGKKTTAVLKAKDRIDLERHYNIKNELKDFGYTYLIFKKKIKKVIRDVKVK 229
Cdd:pfam06176 161 PHRGNFIVSKDEVRIIDLSGKRCSAQRKAKDRIDLERHYGIKNEIRDYGYYLLIYRKKLRNFIRRLKGK 229
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 118-205 1.23e-08

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 52.65  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610 118 YIMLIEYIEGVGLNEYLEISEDLKD---QLSESIKELHQHGMVSGDPHKGNFIVSEKGLRLID--LSGKKTTAVLKAKDR 192
Cdd:COG3642   31 ADLVMEYIEGETLADLLEEGELPPEllrELGRLLARLHRAGIVHGDLTTSNILVDDGGVYLIDfgLARYSDPLEDKAVDL 110

                         90
                 ....*....|....*...
gi 446562610 193 IDLER-----HYNIKNEL 205
Cdd:COG3642  111 AVLKRslestHPDPAEEL 128
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 118-207 7.17e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610  118 YIMLIEYIEGVGLNEYLEiseDLKDQLSESIKE----LHQHGMVSGDPHKGNFIVSEKGLRLIDLS-GKKTTAVL-KAKD 191
Cdd:TIGR03724  72 KTIVMEYIEGKPLKDVIE---ENGDELAREIGRlvgkLHKAGIVHGDLTTSNIIVRDDKVYLIDFGlGKYSDEIEdKAVD 148

                          90       100
                  ....*....|....*....|.
gi 446562610  192 RIDLER-----HYNIKNELKD 207
Cdd:TIGR03724 149 LHVLKRslestHPDKAEELFE 169
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 123-176 1.35e-05

Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This subfamily is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Subfamily 13 (ABC1K13) of plant ABC1 kinases belongs in this subfamily with yeast Abc1p and human ADCK3. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270872 [Multi-domain]  Cd Length: 251  Bit Score: 44.81  E-value: 1.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610 123 EYIEGVGLNEYLEISEDLKDQLSESI-----KELHQHGMVSGDPHKGNFIVSEKGLRLI 176
Cdd:cd13970  152 EFVDGVPLDEAADLSQEERNRIGELLlrlclRELFEFGFMQTDPNPGNFLYDPEDGRLG 210
 
Name Accession Description Interval E-value
PRK10359 PRK10359
lipopolysaccharide core heptose(II) kinase RfaY;
1-229 2.65e-121

lipopolysaccharide core heptose(II) kinase RfaY;


Pssm-ID: 182407  Cd Length: 232  Bit Score: 344.04  E-value: 2.65e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610   1 MIYNKTINGVKVFIKDNDPFYEQVLNDFLTCRVKTLKVFRSIDDTKVILIDTARGPLVLKVYAPKHKMTERFLKSCIKKD 80
Cdd:PRK10359   1 MITKKKIKGYTVFYKDNDNKYKEIFDDFLSYNIKTIKVFRNIDDTKVSLIDTDYGKYILKVFAPKVKRTERFLKSFVKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610  81 YYENLIYQTDRVRGEGIQSINDYFLLAERKTLNFAHYYIMLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVSGD 160
Cdd:PRK10359  81 YYENLIVQTDRVRSEGLASLNDFYLLAERKTLRYAHTYIMLIEYIEGVELNDMPEISEDVKAKIKASIESLHQHGMVSGD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610 161 PHKGNFIVSEKGLRLIDLSGKKTTAVLKAKDRIDLERHYNIKNELKDFGYTYLIFKKKIKKVIRDVKVK 229
Cdd:PRK10359 161 PHKGNFIVSKNGLRIIDLSGKRCTAQRKAKDRIDLERHYGIKNEIKDLGYYLLIYKKKLRKFIRKLKGK 229
WaaY pfam06176
Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial ...
 1-229 6.91e-91

Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial lipopolysaccharide core biosynthesis proteins (WaaY or RfaY). The waaY, waaQ, and waaP genes are located in the central operon of the waa (formerly rfa) locus on the chromosome of Escherichia coli. This locus contains genes whose products are involved in the assembly of the core region of the lipopolysaccharide molecule. WaaY is the enzyme that phosphorylates HepII in this system.


Pssm-ID: 283765  Cd Length: 229  Bit Score: 267.08  E-value: 6.91e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610    1 MIYNKTINGVKVFIKDNDPFYEQVLNDFLTCRVKTLKVFRSIDDTKVILIDTARGPLVLKVYAPKHKMTERFLKSCIKKD 80
Cdd:pfam06176   1 MITSIKIKGFSVFYKDNDNKYKEIFDDFLSYNFKTIKVFRNIDDTKVSLIDTDYGKYILKVFSPKVKRNERFFKSLVKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610   81 YYENLIYQTDRVRGEGIQSINDYFLLAERKTLNFAHYYIMLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVSGD 160
Cdd:pfam06176  81 YYENLFVQTDRVRSEGLTFLNDFYLLAERKTLRYVSTYIMIIEYIEGIELNDMPIIPDNVKAKIKQSIEKLHQHGMVSGD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610  161 PHKGNFIVSEKGLRLIDLSGKKTTAVLKAKDRIDLERHYNIKNELKDFGYTYLIFKKKIKKVIRDVKVK 229
Cdd:pfam06176 161 PHRGNFIVSKDEVRIIDLSGKRCSAQRKAKDRIDLERHYGIKNEIRDYGYYLLIYRKKLRNFIRRLKGK 229
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 118-205 1.23e-08

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 52.65  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610 118 YIMLIEYIEGVGLNEYLEISEDLKD---QLSESIKELHQHGMVSGDPHKGNFIVSEKGLRLID--LSGKKTTAVLKAKDR 192
Cdd:COG3642   31 ADLVMEYIEGETLADLLEEGELPPEllrELGRLLARLHRAGIVHGDLTTSNILVDDGGVYLIDfgLARYSDPLEDKAVDL 110

                         90
                 ....*....|....*...
gi 446562610 193 IDLER-----HYNIKNEL 205
Cdd:COG3642  111 AVLKRslestHPDPAEEL 128
PRK14879 PRK14879
Kae1-associated kinase Bud32;
118-207 1.34e-08

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 53.37  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610 118 YIMLIEYIEGVGLNEYLEISEDLKDQLSESIKE----LHQHGMVSGDPHKGNFIVSEKGLRLID--LSGKKTTAVLKAKD 191
Cdd:PRK14879  74 FIIVMEYIEGEPLKDLINSNGMEELELSREIGRlvgkLHSAGIIHGDLTTSNMILSGGKIYLIDfgLAEFSKDLEDRAVD 153

                         90       100
                 ....*....|....*....|.
gi 446562610 192 -----RIDLERHYNIKNELKD 207
Cdd:PRK14879 154 lhvllRSLESTHPDWAEELFE 174
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
120-190 3.42e-06

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 47.19  E-value: 3.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446562610 120 MLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVSGDPHKGNFIVSEKGLRLIDLSGKKTTAVLKAK 190
Cdd:PRK09605 413 IVMEYIGGKDLKDVLEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDFGLGKYSDLIEDK 483
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 118-207 7.17e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610  118 YIMLIEYIEGVGLNEYLEiseDLKDQLSESIKE----LHQHGMVSGDPHKGNFIVSEKGLRLIDLS-GKKTTAVL-KAKD 191
Cdd:TIGR03724  72 KTIVMEYIEGKPLKDVIE---ENGDELAREIGRlvgkLHKAGIVHGDLTTSNIIVRDDKVYLIDFGlGKYSDEIEdKAVD 148

                          90       100
                  ....*....|....*....|.
gi 446562610  192 RIDLER-----HYNIKNELKD 207
Cdd:TIGR03724 149 LHVLKRslestHPDKAEELFE 169
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 123-176 1.35e-05

Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This subfamily is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Subfamily 13 (ABC1K13) of plant ABC1 kinases belongs in this subfamily with yeast Abc1p and human ADCK3. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270872 [Multi-domain]  Cd Length: 251  Bit Score: 44.81  E-value: 1.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610 123 EYIEGVGLNEYLEISEDLKDQLSESI-----KELHQHGMVSGDPHKGNFIVSEKGLRLI 176
Cdd:cd13970  152 EFVDGVPLDEAADLSQEERNRIGELLlrlclRELFEFGFMQTDPNPGNFLYDPEDGRLG 210
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 115-177 2.61e-04

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 40.66  E-value: 2.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446562610 115 AHYYIMLIEYIEGVGLNEY-LEISEDLKDQLSESIKELHQHGMVSGDPHKGN-FIVSEKGLRLID 177
Cdd:COG0478   69 ANRHAIVMERIEGVELARLkLEDPEEVLDKILEEIRRAHDAGIVHADLSEYNiLVDDDGGVWIID 133
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 119-177 4.13e-04

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 39.46  E-value: 4.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446562610 119 IMLIEYIEGVGLNEYLEISEDLKDQLSESIKELHQHGMVS-----GDPHKGNFIVSEKGLRLID 177
Cdd:cd05151   67 VKITEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLEDlvlchNDLVPGNFLLDDDRLYLID 130
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 123-177 7.21e-04

Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms]; Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440425 [Multi-domain]  Cd Length: 487  Bit Score: 40.19  E-value: 7.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446562610 123 EYIEGVGLNEYLEISEDLKD--QLSESI-----KELHQHGMVSGDPHKGNFIVSEKG-LRLID 177
Cdd:COG0661  240 EWIDGIKISDLEALDAAGIDrkRLAERLvraflRQVFRDGFFHADPHPGNIFVLPDGrLVLLD 302
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 123-178 1.07e-03

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 39.02  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446562610 123 EYIEGVGLNEYLEISE---DLKD---QLSESI-KELHQHGMVSGDPHKGNFIVSEKG-LRLIDL 178
Cdd:cd05121  151 EYIDGVKLTDLEALRAagiDRKElarRLVDAYlKQIFEDGFFHADPHPGNILVLPDGrIALLDF 214
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
51-177 2.39e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 38.46  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610  51 DTARGPLV-LKVYAPKHKMTERFLKScikkdyYENLIYQTDRVRGEGIQSINDYFLLAERktlnfaHYYIMliEYIEGVG 129
Cdd:COG0515   28 DLRLGRPVaLKVLRPELAADPEARER------FRREARALARLNHPNIVRVYDVGEEDGR------PYLVM--EYVEGES 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446562610 130 LNEYLE----ISED----LKDQLSESIKELHQHGMVSGD--PhkGNFIVSEKG-LRLID 177
Cdd:COG0515   94 LADLLRrrgpLPPAealrILAQLAEALAAAHAAGIVHRDikP--ANILLTPDGrVKLID 150
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 119-177 5.99e-03

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and E. coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 36.83  E-value: 5.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446562610  119 IMLIEYIEGVGLNEYLEISE---DLKD---QLSES-IKELHQHGMVSGDPHKGNFIVSEKG-LRLID 177
Cdd:pfam03109 145 VLTMEYVDGIKIDDLDALSEagiDRKEiarRLVELfLEQIFRDGFFHADPHPGNILVRKDGrIVLLD 211
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 108-183 8.76e-03

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 36.57  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446562610 108 ERKTLNFAHYYIMLIEYIEGVGLNEYLEISEDLK--------DQLSESIKELHQHGMVSGDPHKGNFIVSEKGL----RL 175
Cdd:cd14012   69 ERRGRSDGWKVYLLTEYAPGGSLSELLDSVGSVPldtarrwtLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgivKL 148


                 ....*...
gi 446562610 176 IDLSGKKT 183
Cdd:cd14012  149 TDYSLGKT 156
 
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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