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Conserved domains on  [gi|71985811|ref|NP_001024481|]
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Choline kinase A2 [Caenorhabditis elegans]

Protein Classification

choline/ethanolamine kinase family protein( domain architecture ID 10142383)

choline/ethanolamine kinase family protein catalyzes the phosphorylation of choline and/or ethanolamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
55-399 3.78e-168

Euykaryotic Choline 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. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. 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: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 473.65  E-value: 3.78e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCRLSEVYPPIRNEPNKVLLRVYFNP-ETESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYI 133
Cdd:cd05156   1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQIlQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 134 PSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPDYLCEALQRWLKQLTGTVDAEHRFDLpeECGVSSVNCLDLARE 213
Cdd:cd05156  81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKP--SKQLELLLSYDLAKE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 214 LEFLRAHISLSKSPVTFCHNDLQEGNILLPKASSgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASYNYRAFDF 293
Cdd:cd05156 159 LGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPE----------------------NSEDDKLVLIDFEYCSYNYRGFDL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 294 ANHFIEWTIDYDIDEAPFYKIQTENFPENDQMLEFFLNYLREQGNTREN----ELYKKSEDLVQETLPFVPVSHFFWGVW 369
Cdd:cd05156 217 ANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNdlteERSKEEEKLLLEVNRFALASHFFWGLW 296
                       330       340       350
                ....*....|....*....|....*....|
gi 71985811 370 GLLQVELSPVGFGFADYGRDRLSLYFKHKQ 399
Cdd:cd05156 297 SIVQAKISSIEFGYLEYAQARLDAYFKQKE 326
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
55-399 3.78e-168

Euykaryotic Choline 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. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. 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: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 473.65  E-value: 3.78e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCRLSEVYPPIRNEPNKVLLRVYFNP-ETESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYI 133
Cdd:cd05156   1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQIlQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 134 PSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPDYLCEALQRWLKQLTGTVDAEHRFDLpeECGVSSVNCLDLARE 213
Cdd:cd05156  81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKP--SKQLELLLSYDLAKE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 214 LEFLRAHISLSKSPVTFCHNDLQEGNILLPKASSgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASYNYRAFDF 293
Cdd:cd05156 159 LGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPE----------------------NSEDDKLVLIDFEYCSYNYRGFDL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 294 ANHFIEWTIDYDIDEAPFYKIQTENFPENDQMLEFFLNYLREQGNTREN----ELYKKSEDLVQETLPFVPVSHFFWGVW 369
Cdd:cd05156 217 ANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNdlteERSKEEEKLLLEVNRFALASHFFWGLW 296
                       330       340       350
                ....*....|....*....|....*....|
gi 71985811 370 GLLQVELSPVGFGFADYGRDRLSLYFKHKQ 399
Cdd:cd05156 297 SIVQAKISSIEFGYLEYAQARLDAYFKQKE 326
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
83-324 7.19e-83

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 252.58  E-value: 7.19e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811    83 EPNKVLLRVYFNP-ETESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQ 161
Cdd:pfam01633   1 SPRKVLLRIYGPGtELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   162 LEVPiWKEPDYLCEALQRWLKQLTGTVDAEhrfDLPEECGVSSVNCLDLARELEFLRAHISLSKSPVTFCHNDLQEGNIL 241
Cdd:pfam01633  81 LEMP-GKKSPSLWKTMRKWLSLLKNLGAPE---SVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   242 LpkassgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASYNYRAFDFANHFIEWTIDYDiDEAPFYKIQTENFPE 321
Cdd:pfam01633 157 L---------------------------LNETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYH-DPTPFFKCDYSLYPT 208

                  ...
gi 71985811   322 NDQ 324
Cdd:pfam01633 209 REE 211
PLN02236 PLN02236
choline kinase
43-401 3.45e-51

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 175.23  E-value: 3.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   43 LGGAWKTV-PLEHLRISRIKGGMSNMLFLCRLsevypPIR--NEPNKVLLRVY-------FNPETESHlvaesvIFTLLS 112
Cdd:PLN02236  26 LASKWGDVvDDEALQVIPLKGAMTNEVFQIKW-----PTKegNLGRKVLVRIYgegvelfFDRDDEIR------TFECMS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  113 ERHLGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPdYLCEALQRWLKQLTGTVDAEH 192
Cdd:PLN02236  95 RHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNV-LLWDRLRNWLKEAKNLCSPEE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  193 RFDLpeecgvssvnCLD-LARELEFLRAHISLSKSPVTFCHNDLQEGNILlpkassgnirmpsLSDETQAlgnslsafnp 271
Cdd:PLN02236 174 AKEF----------RLDsLEDEINLLEKELSGDDQEIGFCHNDLQYGNIM-------------IDEETRA---------- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  272 adprLVLIDFEYASYNYRAFDFANHFIEWTIDYDIDEApfYKIQTENFPENDQMLEFFLNYLREQGN-TRENELykksED 350
Cdd:PLN02236 221 ----ITIIDYEYASYNPVAYDIANHFCEMAADYHSETP--HILDYSKYPGEEERRRFIRTYLSSSGEePSDEEV----EQ 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71985811  351 LVQETLPFVPVSHFFWGVWGLLQVELSPVGFGFADYGRDRLSLYFKHKQLL 401
Cdd:PLN02236 291 LLDDVEKYTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
209-305 5.82e-10

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 57.48  E-value: 5.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 209 DLARELEFLRAHISLSKSPVTFCHNDLQEGNILLPKassgnirmpslsdetqalgnslsafnpaDPRLVLIDFEYASYNY 288
Cdd:COG0510  30 ELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD----------------------------DGRLYLIDWEYAGLGD 81
                        90
                ....*....|....*..
gi 71985811 289 RAFDFANHFIEWTIDYD 305
Cdd:COG0510  82 PAFDLAALLVEYGLSPE 98
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
55-399 3.78e-168

Euykaryotic Choline 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. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. 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: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 473.65  E-value: 3.78e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCRLSEVYPPIRNEPNKVLLRVYFNP-ETESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYI 133
Cdd:cd05156   1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQIlQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 134 PSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPDYLCEALQRWLKQLTGTVDAEHRFDLpeECGVSSVNCLDLARE 213
Cdd:cd05156  81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKP--SKQLELLLSYDLAKE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 214 LEFLRAHISLSKSPVTFCHNDLQEGNILLPKASSgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASYNYRAFDF 293
Cdd:cd05156 159 LGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPE----------------------NSEDDKLVLIDFEYCSYNYRGFDL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 294 ANHFIEWTIDYDIDEAPFYKIQTENFPENDQMLEFFLNYLREQGNTREN----ELYKKSEDLVQETLPFVPVSHFFWGVW 369
Cdd:cd05156 217 ANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNdlteERSKEEEKLLLEVNRFALASHFFWGLW 296
                       330       340       350
                ....*....|....*....|....*....|
gi 71985811 370 GLLQVELSPVGFGFADYGRDRLSLYFKHKQ 399
Cdd:cd05156 297 SIVQAKISSIEFGYLEYAQARLDAYFKQKE 326
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
83-324 7.19e-83

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 252.58  E-value: 7.19e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811    83 EPNKVLLRVYFNP-ETESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQ 161
Cdd:pfam01633   1 SPRKVLLRIYGPGtELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   162 LEVPiWKEPDYLCEALQRWLKQLTGTVDAEhrfDLPEECGVSSVNCLDLARELEFLRAHISLSKSPVTFCHNDLQEGNIL 241
Cdd:pfam01633  81 LEMP-GKKSPSLWKTMRKWLSLLKNLGAPE---SVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   242 LpkassgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASYNYRAFDFANHFIEWTIDYDiDEAPFYKIQTENFPE 321
Cdd:pfam01633 157 L---------------------------LNETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYH-DPTPFFKCDYSLYPT 208

                  ...
gi 71985811   322 NDQ 324
Cdd:pfam01633 209 REE 211
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
55-397 2.23e-82

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: 254.81  E-value: 2.23e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCrlsevYPPIRNEPNKVLLRVYfNPETEsHLV---AESVIFTLLSERHLGPKLYGIFSGGRLEE 131
Cdd:cd05157   1 IKVKRITGGITNALYKV-----TYPSGDTPKTVLVRIY-GPGTE-LLIdrdRELRILQLLSRAGIGPKLYGRFENGRVEE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 132 YIPSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPI----WKEPDyLCEALQRWLKQLTGTVDAEHRFDLPEECgvSSVNC 207
Cdd:cd05157  74 FLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGeiegKKKPI-LWTTIRKWLDLAPEVFEDEKNKEKKLEK--VDLER 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 208 LDlaRELEFLRAHI-SLSKSPVTFCHNDLQEGNILLpkassgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASY 286
Cdd:cd05157 151 LR--KELEWLEKWLeSLEKSPIVFCHNDLLYGNILY---------------------------NEDDDSVTFIDFEYAGP 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 287 NYRAFDFANHFIEWTIDYDIdeaPFYKiqteNFPENDQMLEFFLNYLREQGNTRENELYKKSE--DLVQETLPFVPVSHF 364
Cdd:cd05157 202 NPRAFDIANHFCEWAGFYCV---LDYS----RYPTKEEQRNFLRAYLESLDGLPGGEEVSEEEveKLYNEVNLFRLASHL 274
                       330       340       350
                ....*....|....*....|....*....|...
gi 71985811 365 FWGVWGLLQVELSPVGFGFADYGRDRLSLYFKH 397
Cdd:cd05157 275 FWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
55-371 7.85e-79

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: 242.94  E-value: 7.85e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCRLSEVYPPirNEPNKVLLRVYFNPE-TESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYI 133
Cdd:cd14021   1 ILVIRILSGLTNQVYKVSLKDESDS--LEPKKVLFRIYGKYLsTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 134 PSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPiwkepdylcealqrwlkqltgtvdaehrfdlpeecgvssvncldlare 213
Cdd:cd14021  79 DGRPLTTDELRNPSVLTSIAKLLAKFHKIKTP------------------------------------------------ 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 214 leflrahislsksPVTFCHNDLQEGNILLpkassgnirmpslsdetqalgnslsafNPADPRLVLIDFEYASYNYRAFDF 293
Cdd:cd14021 111 -------------PVVFCHNDLQENNILL---------------------------TNDQDGLRLIDFEYSGFNYRGYDI 150
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71985811 294 ANHFIEWTIDYDIDEAPFYKIQTENFPENDQMLEFFLNYLREQGNTRENELYKKS-EDLVQETLPFVPVSHFFWGVWGL 371
Cdd:cd14021 151 ANFFNESMIDYDHPEPPYFKIYKENYISEEEKRLFVSVYLSEYLEKNVLPSLDKLvEQFLQEVEIFTLGSHLYWGLWSI 229
PLN02236 PLN02236
choline kinase
43-401 3.45e-51

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 175.23  E-value: 3.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   43 LGGAWKTV-PLEHLRISRIKGGMSNMLFLCRLsevypPIR--NEPNKVLLRVY-------FNPETESHlvaesvIFTLLS 112
Cdd:PLN02236  26 LASKWGDVvDDEALQVIPLKGAMTNEVFQIKW-----PTKegNLGRKVLVRIYgegvelfFDRDDEIR------TFECMS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  113 ERHLGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPdYLCEALQRWLKQLTGTVDAEH 192
Cdd:PLN02236  95 RHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNV-LLWDRLRNWLKEAKNLCSPEE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  193 RFDLpeecgvssvnCLD-LARELEFLRAHISLSKSPVTFCHNDLQEGNILlpkassgnirmpsLSDETQAlgnslsafnp 271
Cdd:PLN02236 174 AKEF----------RLDsLEDEINLLEKELSGDDQEIGFCHNDLQYGNIM-------------IDEETRA---------- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  272 adprLVLIDFEYASYNYRAFDFANHFIEWTIDYDIDEApfYKIQTENFPENDQMLEFFLNYLREQGN-TRENELykksED 350
Cdd:PLN02236 221 ----ITIIDYEYASYNPVAYDIANHFCEMAADYHSETP--HILDYSKYPGEEERRRFIRTYLSSSGEePSDEEV----EQ 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71985811  351 LVQETLPFVPVSHFFWGVWGLLQVELSPVGFGFADYGRDRLSLYFKHKQLL 401
Cdd:PLN02236 291 LLDDVEKYTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
38-406 2.82e-40

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 146.04  E-value: 2.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   38 LCARFLGGaWKTVPLEHLRISRIKGGMSNMLFLCRLSEVyppiRNEPNKVLLRVYfNPETESHLVAESVIFTL--LSERH 115
Cdd:PLN02421   1 VCKALFKG-WSDLDDSDFSVERISGGITNLLLKVSVKEE----NGNEVSVTVRLF-GPNTDYVIDRERELQAIkyLSAAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  116 LGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPDyLCEALQRWLKQLTGTVdaehrFD 195
Cdd:PLN02421  75 FGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVK-----FE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  196 LPE-ECGVSSVNCLDLARELEFLRAHISLSKSPVTFCHNDLQEGNILLpkassgnirmpslsdetqalgnslsafNPADP 274
Cdd:PLN02421 149 DPEkQKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLML---------------------------NEDEG 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  275 RLVLIDFEYASYNYRAFDFANHFIEWTiDYDIDeapfYKIqtenFPENDQMLEFFLNYLREQgntRENELYKKS-EDLVQ 353
Cdd:PLN02421 202 KLYFIDFEYGSYSYRGYDIGNHFNEYA-GFDCD----YSL----YPSKEEQYHFFRHYLRPD---DPEEVSDAElEELFV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71985811  354 ETLPFVPVSHFFWGVWGLLQVELSPVGFGFADYGRDRLSLYFKHKQLLKNLAS 406
Cdd:PLN02421 270 ETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSLVR 322
PTZ00296 PTZ00296
choline kinase; Provisional
47-403 5.32e-32

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 125.77  E-value: 5.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   47 WKTVPLEHLRISRIKGGMSNMLFLCRLSEV----YPPIRNepnKVLLRVY-------FNPeteshlVAESVIFTLLSERH 115
Cdd:PTZ00296 100 WRRFTEDDVRVNQILSGLTNQLFEVSLKEEtannYPSIRR---RVLFRIYgkdvdelYNP------ISEFEVYKTMSKYR 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  116 LGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQL----EVP-IWKEPDYLCEALQRWLKQLTGTVDA 190
Cdd:PTZ00296 171 IAPQLLNTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLsrkrHLPeHWDRTPCIFKMMEKWKNQLSKYKNI 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  191 EhrfdlPEECGVSSvncldLARELEFLRAHISLSK------SPVTFCHNDLQEGNILlpkassgnirmpslsdETQALgn 264
Cdd:PTZ00296 251 E-----KYQRDIHK-----YIKESEKFIKFMKVYSksdnlaNDIVFCHNDLQENNII----------------NTNKC-- 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  265 slsafnpadprLVLIDFEYASYNYRAFDFANHFIEWTIDYDIDEAPFYKIQTENFPENDQMLEFFLNYLreqGNTRENEL 344
Cdd:PTZ00296 303 -----------LRLIDFEYSGYNFLATDIANFFIETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYL---SNYLDKSL 368
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71985811  345 YKKSEDLVQETLPFVPV----SHFFWGVWGLLQVELSPV--GFGFADYGRDRLSLYFKHKQ-LLKN 403
Cdd:PTZ00296 369 VVPNPKIIDQILEAVEVqalgAHLLWGFWSIIRGYQTKSynEFDFFLYAKERFKMYDEQKEyLISN 434
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
55-302 7.18e-27

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: 104.56  E-value: 7.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCRLsevyppirnEPNKVLLRVyFNPETESHL--VAESVIFTLLSERHLGPKLYGIF--SGGRLE 130
Cdd:cd05151   1 ITIEPLKGGLTNKNYLVEV---------AGKKYVLRI-PGAGTELLIdrENEKANSKAAAELGIAPEVIYFDpeTGVKIT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 131 EYIPSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPiwkepdylcealqrwlkqltgtvdaehrfdlpeecgvssvncldl 210
Cdd:cd05151  71 EFIEGATLLTNDFSDPENLERIAALLRKLHSSPLE--------------------------------------------- 105
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 211 areleflrahislsksPVTFCHNDLQEGNILLpkassgnirmpslsdetqalgnslsafnpADPRLVLIDFEYASYNYRA 290
Cdd:cd05151 106 ----------------DLVLCHNDLVPGNFLL-----------------------------DDDRLYLIDWEYAGMNDPL 140
                       250
                ....*....|..
gi 71985811 291 FDFANHFIEWTI 302
Cdd:cd05151 141 FDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
55-302 2.82e-11

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: 61.55  E-value: 2.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  55 LRISRIKGGMSNMLFLCRlsevyppirnEPNKVLLRVYFNPETESHlVAESVIFTLLSERH--LGPKLYGIF----SGGR 128
Cdd:cd05120   1 ISVKLIKEGGDNKVYLLG----------DPREYVLKIGPPRLKKDL-EKEAAMLQLLAGKLslPVPKVYGFGesdgWEYL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 129 LEEYIPSRPLScheislahmstkiakrvakvhqlevpiwkepdylcealQRWLkqltgTVDAEHRFDLpeecgvssvnCL 208
Cdd:cd05120  70 LMERIEGETLS--------------------------------------EVWP-----RLSEEEKEKI----------AD 96
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 209 DLARELEFLRahislSKSPVTFCHNDLQEGNILLPKassgnirmpslsdetqalGNSLSAfnpadprlvLIDFEYASYNY 288
Cdd:cd05120  97 QLAEILAALH-----RIDSSVLTHGDLHPGNILVKP------------------DGKLSG---------IIDWEFAGYGP 144
                       250
                ....*....|....
gi 71985811 289 RAFDFANHFIEWTI 302
Cdd:cd05120 145 PAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
209-305 5.82e-10

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 57.48  E-value: 5.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 209 DLARELEFLRAHISLSKSPVTFCHNDLQEGNILLPKassgnirmpslsdetqalgnslsafnpaDPRLVLIDFEYASYNY 288
Cdd:COG0510  30 ELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD----------------------------DGRLYLIDWEYAGLGD 81
                        90
                ....*....|....*..
gi 71985811 289 RAFDFANHFIEWTIDYD 305
Cdd:COG0510  82 PAFDLAALLVEYGLSPE 98
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
33-306 7.69e-09

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 56.28  E-value: 7.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  33 ERAHMLCARFLGGAWKTVPLEhlrisRIKGGMSNMLFLCRLsevyppirnePNKVLLRVY-FNPETESHLVAESVIFTLL 111
Cdd:COG3173   6 AALRALLAAQLPGLAGLPEVE-----PLSGGWSNLTYRLDT----------GDRLVLRRPpRGLASAHDVRREARVLRAL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 112 sERHLG---PKLYGIFSGGR-------LEEYIPSRPL-----SCHEISLAHMSTKIAKRVAKVHQLEVP----IWKEPDY 172
Cdd:COG3173  71 -APRLGvpvPRPLALGEDGEvigapfyVMEWVEGETLedalpDLSPAERRALARALGEFLAALHAVDPAaaglADGRPEG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 173 LCEALQRWLKQLTGTVDAEHRFDlpeecgvssvnclDLAREL-EFLRAHISLSkSPVTFCHNDLQEGNILlpkassgnir 251
Cdd:COG3173 150 LERQLARWRAQLRRALARTDDLP-------------ALRERLaAWLAANLPEW-GPPVLVHGDLRPGNLL---------- 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71985811 252 mpslsdetqalgnslsaFNPADPRLV-LIDFEYASYNYRAFDFANHFIEWTIDYDI 306
Cdd:COG3173 206 -----------------VDPDDGRLTaVIDWELATLGDPAADLAYLLLYWRLPDDL 244
PTZ00384 PTZ00384
choline kinase; Provisional
217-372 1.08e-07

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 53.63  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  217 LRAHISLSKS---PVTFCHNDLQEGNILlpkassgnirmpslsDETQALgnslsafnpadprlVLIDFEYASYNYRAFDF 293
Cdd:PTZ00384 213 LNNHLNTSNSitnSVLFCHNDLFFTNIL---------------DFNQGI--------------YFIDFDFAGFNYVGWEI 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811  294 ANHFIEWTIDYDIDEAPFYkIQTENFPENDQMLEFFLN-YLREQgnTRENELykKSEDLVQETLPFVPVS----HFFWGV 368
Cdd:PTZ00384 264 ANFFVKLYIVYDPPTPPYF-NSDDSLALSEEMKTIFVSvYLSQL--LGKNVL--PSDDLVKEFLQSLEIHtlgvNLFWTY 338

                 ....
gi 71985811  369 WGLL 372
Cdd:PTZ00384 339 WGIV 342
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
57-319 2.64e-06

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: 48.27  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811    57 ISRIKGGMSNMLFLcrlsevyppIRNEPNKVLLRVYFNPETESHLVAESVIFTLLSERHLG--PKLYGIFSGGRLE---- 130
Cdd:pfam01636   2 LRPISSGASNRTYL---------VTTGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPpvPRVLAGCTDAELLglpf 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   131 ---EYIPSRPLS--CHEISLAHMSTKIAKRVAKVHQLEV----PIWKEPDYLceALQRWLKQLTGTVDAEHRFDLPEECg 201
Cdd:pfam01636  73 llmEYLPGEVLArpLLPEERGALLEALGRALARLHAVDPaalpLAGRLARLL--ELLRQLEAALARLLAAELLDRLEEL- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811   202 vssvncldLARELEFLRAHIsLSKSPVTFCHNDLQEGNILlpkassgnirmpslsdetqalgnslsaFNPADPRLVLIDF 281
Cdd:pfam01636 150 --------EERLLAALLALL-PAELPPVLVHGDLHPGNLL---------------------------VDPGGRVSGVIDF 193
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 71985811   282 EYASYNYRAFDFANHFIEWTIDYDIDEAPFYKIQTENF 319
Cdd:pfam01636 194 EDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
114-309 1.43e-03

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: 40.32  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 114 RHLGPKLYGIFsggrleEYIPSRPLSchEISLAHMSTkIAKRVAKVHQL--EVPIWKEPDYLCEALQRWLKQLTGTVDAE 191
Cdd:cd05153  84 GELNGKPAALF------PFLPGESLT--TPTPEQCRA-IGAALARLHLAlaGFPPPRPNPRGLAWWKPLAERLKARLDLL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 192 HRFDLPEecgvssvncldLARELEFLRAHIsLSKSPVTFCHNDLQEGNILLpkassgnirmpslsdetqaLGNSLSAFnp 271
Cdd:cd05153 155 AADDRAL-----------LEDELARLQALA-PSDLPRGVIHADLFRDNVLF-------------------DGDRLSGI-- 201
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71985811 272 adprlvlIDFEYASYNYRAFD---FANHFI-EWTIDYDIDEA 309
Cdd:cd05153 202 -------IDFYDACYDPLLYDlaiALNDWCfDDDGKLDPERA 236
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
210-294 6.00e-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: 38.37  E-value: 6.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985811 210 LARELEFLRAHISLSKSPVTF--CHNDLQEGNILLpkassgnirmpslsdetqaLGNSLSAFnpadprlvlIDFEYASYN 287
Cdd:COG2334 159 LEELLDRLEARLAPLLGALPRgvIHGDLHPDNVLF-------------------DGDGVSGL---------IDFDDAGYG 210

                ....*..
gi 71985811 288 YRAFDFA 294
Cdd:COG2334 211 PRLYDLA 217
 
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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