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Conserved domains on  [gi|1109572898|gb|APG50334|]
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thiamine kinase [Providencia stuartii]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
25-282 1.33e-73

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member TIGR02721:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 256  Bit Score: 226.13  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  25 VTPLAGLSGGTYHLRSHTLNLIARAQSQAQTALFVNRRKEARVLHQLQHFGQAPKVLARNSDWLLLSWCDGQQPSDTQFL 104
Cdd:TIGR02721   2 QTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWLEGEVITLDQFV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 105 TPTFQSLLAATIAKLHTQPLLTYRLQLRQEIAHYGYLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCT 184
Cdd:TIGR02721  82 ALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 185 ESGqLALLDWEYAANTDIGLSLETYFQANqlNTTQRDFFLSEYCNKYHAYgDVERLAHQCRLWTPWVKYMMLMWYEVQWN 264
Cdd:TIGR02721 162 PQG-LKLIDWEYASDGDIALELAAIIRAN--DEEQQQDFVQRYCQRRRIY-SISVLWRQVKAWQPWVDYMAALWFELRWQ 237
                         250
                  ....*....|....*...
gi 1109572898 265 QSQNNDFLLHSRSLRQYF 282
Cdd:TIGR02721 238 QTGDPQFLELAQELRHRL 255
 
Name Accession Description Interval E-value
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
25-282 1.33e-73

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 226.13  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  25 VTPLAGLSGGTYHLRSHTLNLIARAQSQAQTALFVNRRKEARVLHQLQHFGQAPKVLARNSDWLLLSWCDGQQPSDTQFL 104
Cdd:TIGR02721   2 QTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWLEGEVITLDQFV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 105 TPTFQSLLAATIAKLHTQPLLTYRLQLRQEIAHYGYLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCT 184
Cdd:TIGR02721  82 ALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 185 ESGqLALLDWEYAANTDIGLSLETYFQANqlNTTQRDFFLSEYCNKYHAYgDVERLAHQCRLWTPWVKYMMLMWYEVQWN 264
Cdd:TIGR02721 162 PQG-LKLIDWEYASDGDIALELAAIIRAN--DEEQQQDFVQRYCQRRRIY-SISVLWRQVKAWQPWVDYMAALWFELRWQ 237
                         250
                  ....*....|....*...
gi 1109572898 265 QSQNNDFLLHSRSLRQYF 282
Cdd:TIGR02721 238 QTGDPQFLELAQELRHRL 255
thiK PRK10271
thiamine kinase; Provisional
112-272 2.44e-31

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 115.23  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 112 LAATIAKLHTQPLLTYRLQLRQEIAHYGYLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCTESGqLAL 191
Cdd:PRK10271   20 LAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPLRLAPLHMDVHAGNLVHSASG-LRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 192 LDWEYAANTDIGLSLETYFQAnqlNTTQRDFFLSEYCNKYHAygDVERLAHQCRLWTPWVKYMMLMWYEVQWNQSQNNDF 271
Cdd:PRK10271   99 IDWEYAGDGDIALELAAVWVE---NTEQHRQLVNDYATRAKI--DAAQLWRQVRRWFPWVLMLKAGWFEYRWRQTGDQQF 173

                  .
gi 1109572898 272 L 272
Cdd:PRK10271  174 I 174
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
118-272 1.25e-27

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 104.48  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 118 KLHTQPLLtYRLQLRQEIAHYgyLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCTESGQLALLDWEYA 197
Cdd:COG0510     1 RLHASPAL-LRFDLFARLERY--LALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109572898 198 ANTDIGLSLETYFQANQLNTTQRDFFLSEYCnkyhAYGDVERLAHQCRLWTPWVKYMMLMWYEVQWNQSQNNDFL 272
Cdd:COG0510    78 GLGDPAFDLAALLVEYGLSPEQAEELLEAYG----FGRPTEELLRRLRAYRALADLLWALWALVRAAQEANGDLL 148
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
26-215 3.67e-13

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: 65.65  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  26 TPLAGLSGGTYHLRSHTLNLIARaQSQAQTALFVNRRKEARVLHQLQHFGQAPKVLA--RNSDWLLLSWCDGQQPSDTQF 103
Cdd:cd05151     5 PLKGGLTNKNYLVEVAGKKYVLR-IPGAGTELLIDRENEKANSKAAAELGIAPEVIYfdPETGVKITEFIEGATLLTNDF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 104 LTPTFQSLLAATIAKLHTQPLltyrlqlrqeiahygylvdpkrqgprwhrwhqhflsapmprvLKLAPAHMDIHKGNIVc 183
Cdd:cd05151    84 SDPENLERIAALLRKLHSSPL------------------------------------------EDLVLCHNDLVPGNFL- 120
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1109572898 184 TESGQLALLDWEYAANTDIGLSLETYFQANQL 215
Cdd:cd05151   121 LDDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
24-202 7.15e-10

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: 57.90  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  24 EVTPLA-GLSGGTYHLRSHTLNLIARAQSQAQTAlfVNRRKEARVLHQL--QHFGQAPKVLARNSD-------WLLLSWC 93
Cdd:pfam01636   1 TLRPISsGASNRTYLVTTGDGRYVLRLPPPGRAA--EELRRELALLRHLaaAGVPPVPRVLAGCTDaellglpFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  94 DGQQPSDTQFLTPTFQSL--LAATIAKLHTQP---------LLTYRLQLRQEIAHYGYLVDPK---RQGPRWHRWHQHFL 159
Cdd:pfam01636  79 PGEVLARPLLPEERGALLeaLGRALARLHAVDpaalplagrLARLLELLRQLEAALARLLAAElldRLEELEERLLAALL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1109572898 160 sAPMPRVLKLAPAHMDIHKGNIVCTESGQL-ALLDWEYAANTDI 202
Cdd:pfam01636 159 -ALLPAELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDP 201
 
Name Accession Description Interval E-value
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
25-282 1.33e-73

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 226.13  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  25 VTPLAGLSGGTYHLRSHTLNLIARAQSQAQTALFVNRRKEARVLHQLQHFGQAPKVLARNSDWLLLSWCDGQQPSDTQFL 104
Cdd:TIGR02721   2 QTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWLEGEVITLDQFV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 105 TPTFQSLLAATIAKLHTQPLLTYRLQLRQEIAHYGYLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCT 184
Cdd:TIGR02721  82 ALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 185 ESGqLALLDWEYAANTDIGLSLETYFQANqlNTTQRDFFLSEYCNKYHAYgDVERLAHQCRLWTPWVKYMMLMWYEVQWN 264
Cdd:TIGR02721 162 PQG-LKLIDWEYASDGDIALELAAIIRAN--DEEQQQDFVQRYCQRRRIY-SISVLWRQVKAWQPWVDYMAALWFELRWQ 237
                         250
                  ....*....|....*...
gi 1109572898 265 QSQNNDFLLHSRSLRQYF 282
Cdd:TIGR02721 238 QTGDPQFLELAQELRHRL 255
thiK PRK10271
thiamine kinase; Provisional
112-272 2.44e-31

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 115.23  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 112 LAATIAKLHTQPLLTYRLQLRQEIAHYGYLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCTESGqLAL 191
Cdd:PRK10271   20 LAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPLRLAPLHMDVHAGNLVHSASG-LRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 192 LDWEYAANTDIGLSLETYFQAnqlNTTQRDFFLSEYCNKYHAygDVERLAHQCRLWTPWVKYMMLMWYEVQWNQSQNNDF 271
Cdd:PRK10271   99 IDWEYAGDGDIALELAAVWVE---NTEQHRQLVNDYATRAKI--DAAQLWRQVRRWFPWVLMLKAGWFEYRWRQTGDQQF 173

                  .
gi 1109572898 272 L 272
Cdd:PRK10271  174 I 174
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
118-272 1.25e-27

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 104.48  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 118 KLHTQPLLtYRLQLRQEIAHYgyLVDPKRQGPRWHRWHQHFLSAPMPRVLKLAPAHMDIHKGNIVCTESGQLALLDWEYA 197
Cdd:COG0510     1 RLHASPAL-LRFDLFARLERY--LALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109572898 198 ANTDIGLSLETYFQANQLNTTQRDFFLSEYCnkyhAYGDVERLAHQCRLWTPWVKYMMLMWYEVQWNQSQNNDFL 272
Cdd:COG0510    78 GLGDPAFDLAALLVEYGLSPEQAEELLEAYG----FGRPTEELLRRLRAYRALADLLWALWALVRAAQEANGDLL 148
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
26-215 3.67e-13

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: 65.65  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  26 TPLAGLSGGTYHLRSHTLNLIARaQSQAQTALFVNRRKEARVLHQLQHFGQAPKVLA--RNSDWLLLSWCDGQQPSDTQF 103
Cdd:cd05151     5 PLKGGLTNKNYLVEVAGKKYVLR-IPGAGTELLIDRENEKANSKAAAELGIAPEVIYfdPETGVKITEFIEGATLLTNDF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 104 LTPTFQSLLAATIAKLHTQPLltyrlqlrqeiahygylvdpkrqgprwhrwhqhflsapmprvLKLAPAHMDIHKGNIVc 183
Cdd:cd05151    84 SDPENLERIAALLRKLHSSPL------------------------------------------EDLVLCHNDLVPGNFL- 120
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1109572898 184 TESGQLALLDWEYAANTDIGLSLETYFQANQL 215
Cdd:cd05151   121 LDDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
3-241 3.74e-10

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 59.36  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898   3 NDSALLALLAGCFPNINVKTwEVTPLA-GLSGGTYHLRSHTlNLIAR-AQSQAQTALFVnrRKEARVLHQLQ--HFGQAP 78
Cdd:COG3173     4 DEAALRALLAAQLPGLAGLP-EVEPLSgGWSNLTYRLDTGD-RLVLRrPPRGLASAHDV--RREARVLRALAprLGVPVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  79 KVLARNSD-------WLLLSWCDGQQPSD-----TQFLTPTFQSLLAATIAKLHTQPLLTYRL----------QLRQEIA 136
Cdd:COG3173    80 RPLALGEDgevigapFYVMEWVEGETLEDalpdlSPAERRALARALGEFLAALHAVDPAAAGLadgrpeglerQLARWRA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 137 HYGYLVDPKRQGP----RWHRWhqhfLSAPMPRVLKLAPAHMDIHKGNIVCTESGQ--LALLDWEYAanT------DIGL 204
Cdd:COG3173   160 QLRRALARTDDLPalreRLAAW----LAANLPEWGPPVLVHGDLRPGNLLVDPDDGrlTAVIDWELA--TlgdpaaDLAY 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1109572898 205 SLETYFQANQLnTTQRDFFLSEYCnkyHAYGDVERLA 241
Cdd:COG3173   234 LLLYWRLPDDL-LGPRAAFLAAYE---EATGDLDDLT 266
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
24-202 7.15e-10

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: 57.90  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  24 EVTPLA-GLSGGTYHLRSHTLNLIARAQSQAQTAlfVNRRKEARVLHQL--QHFGQAPKVLARNSD-------WLLLSWC 93
Cdd:pfam01636   1 TLRPISsGASNRTYLVTTGDGRYVLRLPPPGRAA--EELRRELALLRHLaaAGVPPVPRVLAGCTDaellglpFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  94 DGQQPSDTQFLTPTFQSL--LAATIAKLHTQP---------LLTYRLQLRQEIAHYGYLVDPK---RQGPRWHRWHQHFL 159
Cdd:pfam01636  79 PGEVLARPLLPEERGALLeaLGRALARLHAVDpaalplagrLARLLELLRQLEAALARLLAAElldRLEELEERLLAALL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1109572898 160 sAPMPRVLKLAPAHMDIHKGNIVCTESGQL-ALLDWEYAANTDI 202
Cdd:pfam01636 159 -ALLPAELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDP 201
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
53-249 8.77e-07

Euykaryotic Ethanolamine kinase; 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. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK 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: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 49.50  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  53 AQTALFVNRRKEARVLHQLQHFGQAPKVLARNSDWLLLSWCDGQQPSDTQFLTPTFQSLLAATIAKLHTQPLLTYRLQLR 132
Cdd:cd05157    35 PGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 133 Q---------------EIAHYGYLVDPKRQGPRWHR------WHQHFLSAPM--PRVLklapAHMDIHKGNIVCTES-GQ 188
Cdd:cd05157   115 KpilwttirkwldlapEVFEDEKNKEKKLEKVDLERlrkeleWLEKWLESLEksPIVF----CHNDLLYGNILYNEDdDS 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898 189 LALLDWEYA-ANT---DIglsletyfqANQLN----------------TTQRDFFLSEYCNKYHAYG--------DVERL 240
Cdd:cd05157   191 VTFIDFEYAgPNPrafDI---------ANHFCewagfycvldysryptKEEQRNFLRAYLESLDGLPggeevseeEVEKL 261

                  ....*....
gi 1109572898 241 AHQCRLWTP 249
Cdd:cd05157   262 YNEVNLFRL 270
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
24-198 3.06e-05

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like 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: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 44.53  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  24 EVTPLA-GLSGGTYHLR----SHTLNLIARAQSQAqTALFVN--RRKEARVLHQLQHFG-QAPKVLARNSD-------WL 88
Cdd:cd05154     2 AVRRLSgGASNETYLVDaggdGGGRRLVLRRPPPG-GLLPSAhdLEREYRVLRALAGTGvPVPRVLALCEDpsvlgapFY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  89 LLSWCDGQQPSDT---QFLTPTFQSLLA----ATIAKLHTQPLltYRLQLRQEIAHYGYLVdpkRQGPRWHRWHQHFLSA 161
Cdd:cd05154    81 VMERVDGRVLPDPlprPDLSPEERRALArslvDALAALHSVDP--AALGLADLGRPEGYLE---RQVDRWRRQLEAAATD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1109572898 162 PMPRVLKL-------APA-------HMDIHKGNIVCTESGQL-ALLDWEYAA 198
Cdd:cd05154   156 PPPALEEAlrwlranLPAdgrpvlvHGDFRLGNLLFDPDGRVtAVLDWELAT 207
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
57-198 1.47e-03

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. 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. 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: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 39.17  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  57 LFVNRRKEARVLHQLQHFGQAPKVLARNSDWLLLSWCDGQQPSDTQFLTPTFQSLLAATIAKLHTQPLLTYRLqlrqeia 136
Cdd:cd14021    42 TLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHKIKTPPVVF------- 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109572898 137 hygylvdpkrqgprwhrwhqhflsapmprvlklapAHMDIHKGNIVCTESGQ-LALLDWEYAA 198
Cdd:cd14021   115 -----------------------------------CHNDLQENNILLTNDQDgLRLIDFEYSG 142
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
87-227 5.65e-03

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: 37.60  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109572898  87 WLLLSWCDGQQPSDtqfLTPTFQSLLAATIAKLH------TQPLLTYRLQLRQEIAHygyLVDPKRQGPRWHRWHQHFLS 160
Cdd:COG2334    91 AALFPFLPGRSPEE---PSPEQLEELGRLLARLHraladfPRPNARDLAWWDELLER---LLGPLLPDPEDRALLEELLD 164
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109572898 161 ------APMPRVLKLAPAHMDIHKGNIVCTESGQLALLDWEYAANT----DIGLSLeTYFQANQLNTTQRDFFLSEY 227
Cdd:COG2334   165 rlearlAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGprlyDLAIAL-NGWADGPLDPARLAALLEGY 240
 
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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