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Conserved domains on  [gi|1590257259|ref|WP_131631586|]
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MULTISPECIES: homoserine kinase [Rhizobium]

Protein Classification

homoserine kinase( domain architecture ID 10142355)

homoserine kinase catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-233 1.40e-54

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 178.22  E-value: 1.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259   9 DEDRNSIAAAYGMTSLSSVIGIADGDRETTYLFRTAGGEFIVTLFENGAEPLDLERAFATMEKLNNRGIPCPKPTRTVDG 88
Cdd:cd05153     1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRRSAAELPFELELLDHLAQAGLPVPRPLADKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  89 DATFQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQGG--------------------------------- 135
Cdd:cd05153    81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFppprpnprglawwkplaerlkarldllaaddra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 136 ---------RKHSLDELPTGALHGALVPSNVFFLGENVSGVINFRLRHDDVLISEIADVLISWASQPAGELDEQKARAIL 206
Cdd:cd05153   161 lledelarlQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                         250       260
                  ....*....|....*....|....*..
gi 1590257259 207 AGYESVRQLTEAEKKALPAFVLASAAR 233
Cdd:cd05153   241 AGYQSVRPLTEEEKAALPLLLRAAALR 267
 
Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-233 1.40e-54

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 178.22  E-value: 1.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259   9 DEDRNSIAAAYGMTSLSSVIGIADGDRETTYLFRTAGGEFIVTLFENGAEPLDLERAFATMEKLNNRGIPCPKPTRTVDG 88
Cdd:cd05153     1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRRSAAELPFELELLDHLAQAGLPVPRPLADKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  89 DATFQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQGG--------------------------------- 135
Cdd:cd05153    81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFppprpnprglawwkplaerlkarldllaaddra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 136 ---------RKHSLDELPTGALHGALVPSNVFFLGENVSGVINFRLRHDDVLISEIADVLISWASQPAGELDEQKARAIL 206
Cdd:cd05153   161 lledelarlQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                         250       260
                  ....*....|....*....|....*..
gi 1590257259 207 AGYESVRQLTEAEKKALPAFVLASAAR 233
Cdd:cd05153   241 AGYQSVRPLTEEEKAALPLLLRAAALR 267
PRK05231 PRK05231
homoserine kinase; Provisional
1-233 2.35e-51

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 170.36  E-value: 2.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259   1 MAVFTEISDEDRNSIAAAYGMTSLSSVIGIADGDRETTYLFRTAGGEFIVTLFENGAePLDLERAFATMEKLNNRGIPCP 80
Cdd:PRK05231    1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLT-AEDLPFFLGLMQHLAARGVPVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  81 KPTRTVDGDATFQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQG---GRKHSLD---------------- 141
Cdd:PRK05231   80 APVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDfplERPNLRGlawwrelaprllpfla 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 142 ------------------------ELPTGALHGALVPSNVFFLGENVSGVINFRLRHDDVLISEIADVLISWASQPAGEL 197
Cdd:PRK05231  160 deqaalleaelaaqlaflasaawpALPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSL 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1590257259 198 DEQKARAILAGYESVRQLTEAEKKALPAFVLASAAR 233
Cdd:PRK05231  240 DATKARALLAAYQSVRPLTAAERAALPVMLRGAALR 275
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-237 5.71e-48

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 160.86  E-value: 5.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  14 SIAAAYGMTSLSSVIGIADGdRETTYLFRTA-GGEFIVTLFENG-AEPLDLERAFATMEKLNNRGIPCPKPTRTVDGDAT 91
Cdd:COG2334     5 AALERYGLGPLSSLKPLNSG-ENRNYRVETEdGRRYVLKLYRPGrWSPEEIPFELALLAHLAAAGLPVPAPVPTRDGETL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  92 FQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQG-----GR------------------------------ 136
Cdd:COG2334    84 LELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADfprpnARdlawwdellerllgpllpdpedralleell 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 137 -------KHSLDELPTGALHGALVPSNVFFLGENVSGVINFrlrhDDV----LISEIADVLISWASqpaGELDEQKARAI 205
Cdd:COG2334   164 drlearlAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDF----DDAgygpRLYDLAIALNGWAD---GPLDPARLAAL 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1590257259 206 LAGYESVRQLTEAEKKALPAFVLASAARHYAS 237
Cdd:COG2334   237 LEGYRAVRPLTEAELAALPPLLRLRALRFLAW 268
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
26-215 8.43e-13

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 65.99  E-value: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  26 SVIGIADGDRETTYLFRTAGGEFIVTLFENGAEPLDLERAFATMEKLNNRGI-PCPKPtrtVDGDATFQAAGRLVAIVSF 104
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVpPVPRV---LAGCTDAELLGLPFLLMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 105 VAGSSTNNPTPEKS-----ENLGRLMARIHVILQGGR------------------------------------------- 136
Cdd:pfam01636  78 LPGEVLARPLLPEErgallEALGRALARLHAVDPAALplagrlarllellrqleaalarllaaelldrleeleerllaal 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 137 -KHSLDELPTGALHGALVPSNVFFLGEN-VSGVINF-RLRHDDVLIsEIADVLISWASQPAGELDEQKARAILA-GYESV 212
Cdd:pfam01636 158 lALLPAELPPVLVHGDLHPGNLLVDPGGrVSGVIDFeDAGLGDPAY-DLAILLNSWGRELGAELLAAYLAAYGAfGYARL 236

                  ...
gi 1590257259 213 RQL 215
Cdd:pfam01636 237 REL 239
 
Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-233 1.40e-54

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 178.22  E-value: 1.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259   9 DEDRNSIAAAYGMTSLSSVIGIADGDRETTYLFRTAGGEFIVTLFENGAEPLDLERAFATMEKLNNRGIPCPKPTRTVDG 88
Cdd:cd05153     1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRRSAAELPFELELLDHLAQAGLPVPRPLADKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  89 DATFQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQGG--------------------------------- 135
Cdd:cd05153    81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFppprpnprglawwkplaerlkarldllaaddra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 136 ---------RKHSLDELPTGALHGALVPSNVFFLGENVSGVINFRLRHDDVLISEIADVLISWASQPAGELDEQKARAIL 206
Cdd:cd05153   161 lledelarlQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                         250       260
                  ....*....|....*....|....*..
gi 1590257259 207 AGYESVRQLTEAEKKALPAFVLASAAR 233
Cdd:cd05153   241 AGYQSVRPLTEEEKAALPLLLRAAALR 267
PRK05231 PRK05231
homoserine kinase; Provisional
1-233 2.35e-51

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 170.36  E-value: 2.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259   1 MAVFTEISDEDRNSIAAAYGMTSLSSVIGIADGDRETTYLFRTAGGEFIVTLFENGAePLDLERAFATMEKLNNRGIPCP 80
Cdd:PRK05231    1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLT-AEDLPFFLGLMQHLAARGVPVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  81 KPTRTVDGDATFQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQG---GRKHSLD---------------- 141
Cdd:PRK05231   80 APVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDfplERPNLRGlawwrelaprllpfla 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 142 ------------------------ELPTGALHGALVPSNVFFLGENVSGVINFRLRHDDVLISEIADVLISWASQPAGEL 197
Cdd:PRK05231  160 deqaalleaelaaqlaflasaawpALPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSL 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1590257259 198 DEQKARAILAGYESVRQLTEAEKKALPAFVLASAAR 233
Cdd:PRK05231  240 DATKARALLAAYQSVRPLTAAERAALPVMLRGAALR 275
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-237 5.71e-48

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 160.86  E-value: 5.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  14 SIAAAYGMTSLSSVIGIADGdRETTYLFRTA-GGEFIVTLFENG-AEPLDLERAFATMEKLNNRGIPCPKPTRTVDGDAT 91
Cdd:COG2334     5 AALERYGLGPLSSLKPLNSG-ENRNYRVETEdGRRYVLKLYRPGrWSPEEIPFELALLAHLAAAGLPVPAPVPTRDGETL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  92 FQAAGRLVAIVSFVAGSSTNNPTPEKSENLGRLMARIHVILQG-----GR------------------------------ 136
Cdd:COG2334    84 LELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADfprpnARdlawwdellerllgpllpdpedralleell 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 137 -------KHSLDELPTGALHGALVPSNVFFLGENVSGVINFrlrhDDV----LISEIADVLISWASqpaGELDEQKARAI 205
Cdd:COG2334   164 drlearlAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDF----DDAgygpRLYDLAIALNGWAD---GPLDPARLAAL 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1590257259 206 LAGYESVRQLTEAEKKALPAFVLASAARHYAS 237
Cdd:COG2334   237 LEGYRAVRPLTEAELAALPPLLRLRALRFLAW 268
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
26-215 8.43e-13

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 65.99  E-value: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  26 SVIGIADGDRETTYLFRTAGGEFIVTLFENGAEPLDLERAFATMEKLNNRGI-PCPKPtrtVDGDATFQAAGRLVAIVSF 104
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVpPVPRV---LAGCTDAELLGLPFLLMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 105 VAGSSTNNPTPEKS-----ENLGRLMARIHVILQGGR------------------------------------------- 136
Cdd:pfam01636  78 LPGEVLARPLLPEErgallEALGRALARLHAVDPAALplagrlarllellrqleaalarllaaelldrleeleerllaal 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259 137 -KHSLDELPTGALHGALVPSNVFFLGEN-VSGVINF-RLRHDDVLIsEIADVLISWASQPAGELDEQKARAILA-GYESV 212
Cdd:pfam01636 158 lALLPAELPPVLVHGDLHPGNLLVDPGGrVSGVIDFeDAGLGDPAY-DLAILLNSWGRELGAELLAAYLAAYGAfGYARL 236

                  ...
gi 1590257259 213 RQL 215
Cdd:pfam01636 237 REL 239
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
25-170 5.47e-05

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family 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: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 42.29  E-value: 5.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  25 SSVIGIADGDRETTYLFRTaGGEFIVTLFENgAEPLDLERAFATMEKLNNR-GIPCPKPTRTVDGDatfqaaGRLVAIVS 103
Cdd:cd05120     1 ISVKLIKEGGDNKVYLLGD-PREYVLKIGPP-RLKKDLEKEAAMLQLLAGKlSLPVPKVYGFGESD------GWEYLLME 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590257259 104 FVAGSS----TNNPTPEKSENLGRLMARIHVILqggrkHSLDelPTGALHGALVPSNVFFLGEN-VSGVINF 170
Cdd:cd05120    73 RIEGETlsevWPRLSEEEKEKIADQLAEILAAL-----HRID--SSVLTHGDLHPGNILVKPDGkLSGIIDW 137
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
37-164 1.89e-03

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: 37.92  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590257259  37 TTYLFRTAGGEFIVTLFENGAEPL-DLERAFATMEKLNNRGIpCPKptrTVDGDATFQaagrlVAIVSFVAGSSTNNPTP 115
Cdd:cd05151    13 KNYLVEVAGKKYVLRIPGAGTELLiDRENEKANSKAAAELGI-APE---VIYFDPETG-----VKITEFIEGATLLTNDF 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1590257259 116 EKSENLGRLMARIHVIlqggrkHSLDELPTGALHGALVPSNVFFLGENV 164
Cdd:cd05151    84 SDPENLERIAALLRKL------HSSPLEDLVLCHNDLVPGNFLLDDDRL 126
 
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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