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Conserved domains on  [gi|6671748|ref|NP_031718|]
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choline/ethanolamine kinase [Mus musculus]

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 ...
73-385 0e+00

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: 528.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   73 PVSGGLSNLLFRCSLPNHVPSVGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRP 152
Cdd:cd05156   5 TITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  153 LKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLP-----QMNLVEMYSLKDEMNSLRK 227
Cdd:cd05156  85 LTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPtkpskQLELLLSYDLAKELGWLRS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  228 LLDDTPSPVVFCHNDIQEGNILLLSEP--DSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPTDYPT 305
Cdd:cd05156 165 LLESTPSPVVFCHNDLQEGNILLLNGPenSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPT 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  306 REQQLHFIRHYLAEVQKGE-ILSEEEQKKREEELLLEISRYSLASHFFWGLWSTLQASMSTIEFGYLEYAQSRFQFYFQQ 384
Cdd:cd05156 245 REQQLHFIRAYLDEQYKDKtNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQ 324

                .
gi 6671748  385 K 385
Cdd:cd05156 325 K 325
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
73-385 0e+00

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: 528.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   73 PVSGGLSNLLFRCSLPNHVPSVGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRP 152
Cdd:cd05156   5 TITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  153 LKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLP-----QMNLVEMYSLKDEMNSLRK 227
Cdd:cd05156  85 LTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPtkpskQLELLLSYDLAKELGWLRS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  228 LLDDTPSPVVFCHNDIQEGNILLLSEP--DSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPTDYPT 305
Cdd:cd05156 165 LLESTPSPVVFCHNDLQEGNILLLNGPenSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPT 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  306 REQQLHFIRHYLAEVQKGE-ILSEEEQKKREEELLLEISRYSLASHFFWGLWSTLQASMSTIEFGYLEYAQSRFQFYFQQ 384
Cdd:cd05156 245 REQQLHFIRAYLDEQYKDKtNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQ 324

                .
gi 6671748  385 K 385
Cdd:cd05156 325 K 325
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
97-308 2.38e-96

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: 286.48  E-value: 2.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748     97 EPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHG 176
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    177 MEMPFTKEPrWLFGTMERYLKQIQDL----PSTSLPQMNLVEMYSLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLLs 252
Cdd:pfam01633  81 LEMPGKKSP-SLWKTMRKWLSLLKNLgapeSVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLL- 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6671748    253 epDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEwPFYKARPTDYPTREQ 308
Cdd:pfam01633 159 --NETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
57-391 8.05e-71

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 225.69  E-value: 8.05e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    57 LGGAWRR-ARPEELSVCPVSGGLSNLLFRCSLPNhvpSVGGEPREVLLRLYGailQGVDSLVL---ESVMFAILAERSLG 132
Cdd:PLN02236  26 LASKWGDvVDDEALQVIPLKGAMTNEVFQIKWPT---KEGNLGRKVLVRIYG---EGVELFFDrddEIRTFECMSRHGQG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   133 PQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRwLFGTMERYLKQIQDLPSTSlpQMNL 212
Cdd:PLN02236 100 PRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLCSPE--EAKE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   213 VEMYSLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLLSEPDSddnLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEE 292
Cdd:PLN02236 177 FRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRA---ITIIDYEYASYNPVAYDIANHFCEMAADYHSET 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   293 wpfykarP-----TDYPTREQQLHFIRHYLA----EVQKGEIlseeeqkkreEELLLEISRYSLASHFFWGLWSTLQASM 363
Cdd:PLN02236 254 -------PhildySKYPGEEERRRFIRTYLSssgeEPSDEEV----------EQLLDDVEKYTLASHLFWGLWGIISGHV 316
                        330       340
                 ....*....|....*....|....*...
gi 6671748   364 STIEFGYLEYAQSRFQFYFQQKGQLTSS 391
Cdd:PLN02236 317 NKIDFDYMEYARQRFEQYWLRKPELLGS 344
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
173-379 1.35e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 73.66  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  173 RFHGMEMPFtkePRWLFGTMERYL-KQIQDLPStslpqmnlvemysLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLl 251
Cdd:COG0510   1 RLHASPALL---RFDLFARLERYLaLGPRDLPE-------------LLRRLEELERALAARPLPLVLCHGDLHPGNFLV- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  252 sepDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDytyeewpfykarptdyptREQQLHFIRHYLAEVqkgeilseeeq 331
Cdd:COG0510  64 ---TDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLS------------------PEQAEELLEAYGFGR----------- 111
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6671748  332 kkREEELLLEISRYSLASHFFWGLWSTLQASmSTIEFGYLEYAQSRFQ 379
Cdd:COG0510 112 --PTEELLRRLRAYRALADLLWALWALVRAA-QEANGDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
157-279 6.37e-05

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 44.58  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    157 ELRDPVLSGAIATRMARFH----GMEMPFTKEPRWLFGTM-ERYLKQIQDLPSTslpqMNLVEMYSLKDEM--------- 222
Cdd:TIGR02906  83 DFNNPIDLKKAAKGLALFHhaskGYVPPDGSKIRSKLGKWpKQFEKRLKELERF----KKIALEKKYKDEFdklylkevd 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671748    223 -------NSLRKLLD--------DTPSPVVFCHNDIQEGNILLlsepdSDDNLMLVDFEYSSYNYRGFDIGN 279
Cdd:TIGR02906 159 yflergkKALELLNKskyydlckEAKKIRGFCHQDYAYHNILL-----KDNEVYVIDFDYCTIDLPVRDLRK 225
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
73-385 0e+00

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: 528.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   73 PVSGGLSNLLFRCSLPNHVPSVGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRP 152
Cdd:cd05156   5 TITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  153 LKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLP-----QMNLVEMYSLKDEMNSLRK 227
Cdd:cd05156  85 LTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPtkpskQLELLLSYDLAKELGWLRS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  228 LLDDTPSPVVFCHNDIQEGNILLLSEP--DSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPTDYPT 305
Cdd:cd05156 165 LLESTPSPVVFCHNDLQEGNILLLNGPenSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPT 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  306 REQQLHFIRHYLAEVQKGE-ILSEEEQKKREEELLLEISRYSLASHFFWGLWSTLQASMSTIEFGYLEYAQSRFQFYFQQ 384
Cdd:cd05156 245 REQQLHFIRAYLDEQYKDKtNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQ 324

                .
gi 6671748  385 K 385
Cdd:cd05156 325 K 325
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
69-382 8.52e-99

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: 296.03  E-value: 8.52e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   69 LSVCPVSGGLSNLLFRCSLPNhvpsvGGEPREVLLRLYGAilqGVDSLV---LESVMFAILAERSLGPQLYGVFPEGRLE 145
Cdd:cd05157   1 IKVKRITGGITNALYKVTYPS-----GDTPKTVLVRIYGP---GTELLIdrdRELRILQLLSRAGIGPKLYGRFENGRVE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  146 QYLPSRPLKTQELRDPVLSGAIATRMARFHG----MEMPFTKEPRwLFGTMERYLKQIQDLPSTSLPQMNLVEMYS---L 218
Cdd:cd05157  73 EFLPGRTLTPEDLRDPKISRLIARRLAELHSivplGEIEGKKKPI-LWTTIRKWLDLAPEVFEDEKNKEKKLEKVDlerL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  219 KDEMNSLRKLLDD-TPSPVVFCHNDIQEGNILLlsePDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWpfyk 297
Cdd:cd05157 152 RKELEWLEKWLESlEKSPIVFCHNDLLYGNILY---NEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVLDY---- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  298 arpTDYPTREQQLHFIRHYLAEVQKGEiLSEEEQKKREEELLLEISRYSLASHFFWGLWSTLQASMSTIEFGYLEYAQSR 377
Cdd:cd05157 225 ---SRYPTKEEQRNFLRAYLESLDGLP-GGEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKER 300

                ....*
gi 6671748  378 FQFYF 382
Cdd:cd05157 301 LDEYW 305
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
97-308 2.38e-96

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: 286.48  E-value: 2.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748     97 EPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHG 176
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    177 MEMPFTKEPrWLFGTMERYLKQIQDL----PSTSLPQMNLVEMYSLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLLs 252
Cdd:pfam01633  81 LEMPGKKSP-SLWKTMRKWLSLLKNLgapeSVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLL- 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6671748    253 epDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEwPFYKARPTDYPTREQ 308
Cdd:pfam01633 159 --NETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
69-357 2.86e-87

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: 263.74  E-value: 2.86e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   69 LSVCPVSGGLSNLLFRCSLPNHVPSVggEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYL 148
Cdd:cd14021   1 ILVIRILSGLTNQVYKVSLKDESDSL--EPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  149 PSRPLKTQELRDPVLSGAIATRMARFHGMEMPftkeprwlfgtmerylkqiqdlpstslpqmnlvemyslkdemnslrkl 228
Cdd:cd14021  79 DGRPLTTDELRNPSVLTSIAKLLAKFHKIKTP------------------------------------------------ 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  229 lddtpsPVVFCHNDIQEGNILLLSEpdsDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPTDYPTREQ 308
Cdd:cd14021 111 ------PVVFCHNDLQENNILLTND---QDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHPEPPYFKIYKENYISEEE 181
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 6671748  309 QLHFIRHYLAEVQKGEILSeeEQKKREEELLLEISRYSLASHFFWGLWS 357
Cdd:cd14021 182 KRLFVSVYLSEYLEKNVLP--SLDKLVEQFLQEVEIFTLGSHLYWGLWS 228
PLN02236 PLN02236
choline kinase
57-391 8.05e-71

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 225.69  E-value: 8.05e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    57 LGGAWRR-ARPEELSVCPVSGGLSNLLFRCSLPNhvpSVGGEPREVLLRLYGailQGVDSLVL---ESVMFAILAERSLG 132
Cdd:PLN02236  26 LASKWGDvVDDEALQVIPLKGAMTNEVFQIKWPT---KEGNLGRKVLVRIYG---EGVELFFDrddEIRTFECMSRHGQG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   133 PQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRwLFGTMERYLKQIQDLPSTSlpQMNL 212
Cdd:PLN02236 100 PRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLCSPE--EAKE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   213 VEMYSLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLLSEPDSddnLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEE 292
Cdd:PLN02236 177 FRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRA---ITIIDYEYASYNPVAYDIANHFCEMAADYHSET 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   293 wpfykarP-----TDYPTREQQLHFIRHYLA----EVQKGEIlseeeqkkreEELLLEISRYSLASHFFWGLWSTLQASM 363
Cdd:PLN02236 254 -------PhildySKYPGEEERRRFIRTYLSssgeEPSDEEV----------EQLLDDVEKYTLASHLFWGLWGIISGHV 316
                        330       340
                 ....*....|....*....|....*...
gi 6671748   364 STIEFGYLEYAQSRFQFYFQQKGQLTSS 391
Cdd:PLN02236 317 NKIDFDYMEYARQRFEQYWLRKPELLGS 344
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
53-394 3.33e-65

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 210.75  E-value: 3.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    53 CREYLGGaWRRARPEELSVCPVSGGLSNLLFRCSlpnhVPSVGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLG 132
Cdd:PLN02421   2 CKALFKG-WSDLDDSDFSVERISGGITNLLLKVS----VKEENGNEVSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   133 PQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRwLFGTMERYLKQIQDLPSTSLPQMNL 212
Cdd:PLN02421  77 AKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVKFEDPEKQKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   213 VEMYS---LKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLlsePDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWV-YDY 288
Cdd:PLN02421 156 YETISfeeLRDEIVELKEITDSLKAPVVFAHNDLLSGNLML---NEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAgFDC 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   289 TYeewpfykarpTDYPTREQQLHFIRHYLA-----EVQKGEIlseeeqkkreEELLLEISRYSLASHFFWGLWSTLQASM 363
Cdd:PLN02421 233 DY----------SLYPSKEEQYHFFRHYLRpddpeEVSDAEL----------EELFVETNFYALASHLYWAIWAIVQAKM 292
                        330       340       350
                 ....*....|....*....|....*....|.
gi 6671748   364 STIEFGYLEYAQSRFQFYFQQKGQLTSSPSS 394
Cdd:PLN02421 293 SPIDFDYLGYFFLRYKEYKRQKEKLLSLVRS 323
PTZ00296 PTZ00296
choline kinase; Provisional
61-390 6.59e-50

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 173.92  E-value: 6.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    61 WRRARPEELSVCPVSGGLSNLLFRCSLP----NHVPSVGgepREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLY 136
Cdd:PTZ00296 100 WRRFTEDDVRVNQILSGLTNQLFEVSLKeetaNNYPSIR---RRVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   137 GVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHGM----EMP--FTKEPrWLFGTMERYLKQIQDLPSTSLPQM 210
Cdd:PTZ00296 177 NTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLsrkrHLPehWDRTP-CIFKMMEKWKNQLSKYKNIEKYQR 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   211 NLVEMYSlkdEMNSLRKLL------DDTPSPVVFCHNDIQEGNILllsepDSDDNLMLVDFEYSSYNYRGFDIGNHFCEW 284
Cdd:PTZ00296 256 DIHKYIK---ESEKFIKFMkvysksDNLANDIVFCHNDLQENNII-----NTNKCLRLIDFEYSGYNFLATDIANFFIET 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   285 VYDYTYEEWPFYKARPTDYPTREQQLHFIRHYLAEVQKGEILSeeEQKKREEELLLEISRYSLASHFFWGLWSTLQA--S 362
Cdd:PTZ00296 328 TIDYSVSHYPFFAIDKKKYISYENRKLFITAYLSNYLDKSLVV--PNPKIIDQILEAVEVQALGAHLLWGFWSIIRGyqT 405
                        330       340
                 ....*....|....*....|....*...
gi 6671748   363 MSTIEFGYLEYAQSRFQFYFQQKGQLTS 390
Cdd:PTZ00296 406 KSYNEFDFFLYAKERFKMYDEQKEYLIS 433
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
71-286 1.50e-29

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: 111.88  E-value: 1.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   71 VCPVSGGLSNLLFRCSLPNhvpsvggepREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPE--GRLEQYL 148
Cdd:cd05151   3 IEPLKGGLTNKNYLVEVAG---------KKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPEtgVKITEFI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  149 PSRPLKTQELRDPVLSGAIATRMARFHGMEMPftkeprwlfgtmerylkqiqdlpstslpqmnlvemyslkdemnslrkl 228
Cdd:cd05151  74 EGATLLTNDFSDPENLERIAALLRKLHSSPLE------------------------------------------------ 105
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6671748  229 lddtpsPVVFCHNDIQEGNILLlsepdSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVY 286
Cdd:cd05151 106 ------DLVLCHNDLVPGNFLL-----DDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
69-286 1.74e-17

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: 78.88  E-value: 1.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   69 LSVCPVSGGLSNLLFRCslpnhvpsvgGEPREVLLRLYGAILQgvDSLVLESVMFAILAERS--LGPQLYGVFP----EG 142
Cdd:cd05120   1 ISVKLIKEGGDNKVYLL----------GDPREYVLKIGPPRLK--KDLEKEAAMLQLLAGKLslPVPKVYGFGEsdgwEY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  143 RLEQYLPSRPLKTQ-----ELRDPVLSGAIATRMARFHGMEMPftkeprwlfgtmerylkqiqdlpstslpqmnlvemys 217
Cdd:cd05120  69 LLMERIEGETLSEVwprlsEEEKEKIADQLAEILAALHRIDSS------------------------------------- 111
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671748  218 lkdemnslrkllddtpspvVFCHNDIQEGNILLLSEPDSddnLMLVDFEYSSYNYRGFDIGNHFCEWVY 286
Cdd:cd05120 112 -------------------VLTHGDLHPGNILVKPDGKL---SGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
173-379 1.35e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 73.66  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  173 RFHGMEMPFtkePRWLFGTMERYL-KQIQDLPStslpqmnlvemysLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLl 251
Cdd:COG0510   1 RLHASPALL---RFDLFARLERYLaLGPRDLPE-------------LLRRLEELERALAARPLPLVLCHGDLHPGNFLV- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  252 sepDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDytyeewpfykarptdyptREQQLHFIRHYLAEVqkgeilseeeq 331
Cdd:COG0510  64 ---TDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLS------------------PEQAEELLEAYGFGR----------- 111
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6671748  332 kkREEELLLEISRYSLASHFFWGLWSTLQASmSTIEFGYLEYAQSRFQ 379
Cdd:COG0510 112 --PTEELLRRLRAYRALADLLWALWALVRAA-QEANGDLLKYLLRRLE 156
PTZ00384 PTZ00384
choline kinase; Provisional
61-381 2.60e-11

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 64.41  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    61 WRRARPEELSVCPVSGGLSNLLFRCSLpnhvpSVGGEPREVLLRLYGAILQGVDSLVLES-VMFAI---LAERSLGPQLY 136
Cdd:PTZ00384  45 WNNVNPEFIEIKKMNNGITNQVYQATL-----VDGDKDRYPIKSVCIKKSSTYNSLVIDNdLQYNIaklLGDNNFGPKII 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   137 GVFPEGRLEQYLPSRPLKTQELRD-PVLSGaIATRMARFHG------------MEMPFTKEPRWlFGTMERYLKQIQ-DL 202
Cdd:PTZ00384 120 GRFGDFTIQEWVEGNTMGIDSLQNlSVLTG-IASSLAKFHKrvtelvpkewdrTPMFLTKISTW-SQHVERIIKKYNlDF 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   203 PSTSLPQMnlVEMYS--LKDEMNSLrkllDDTPSPVVFCHNDIQEGNILllsepDSDDNLMLVDFEYSSYNYRGFDIGNH 280
Cdd:PTZ00384 198 DYNELVQN--YELFKkiLNNHLNTS----NSITNSVLFCHNDLFFTNIL-----DFNQGIYFIDFDFAGFNYVGWEIANF 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   281 FCEWVYDYTYEEWPFYKARPTDYPTREQQLHFIRHYLAEVQkGEILSEEEQKKREEELLLEIsrYSLASHFFWGLWSTLQ 360
Cdd:PTZ00384 267 FVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFVSVYLSQLL-GKNVLPSDDLVKEFLQSLEI--HTLGVNLFWTYWGIVM 343
                        330       340
                 ....*....|....*....|...
gi 6671748   361 ASMSTIE--FGYLEYAQSRFQFY 381
Cdd:PTZ00384 344 NDKPKNElsKPVKFEAYAKFQYN 366
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
70-284 1.97e-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: 48.65  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748     70 SVCPVSGGLSNLLFRcslpnhvpsVGGEPREVLLRLYgAILQGVDSLVLESVMFAILAERSLGP---QLYGVFPEGRLE- 145
Cdd:pfam01636   1 TLRPISSGASNRTYL---------VTTGDGRYVLRLP-PPGRAAEELRRELALLRHLAAAGVPPvprVLAGCTDAELLGl 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    146 -----QYLPSRPLKTQELRDPVlsGAIATRMARFHG-------MEMPFTKEPRWLfGTMERYLKQIQDLPSTSLPQMNLV 213
Cdd:pfam01636  71 pfllmEYLPGEVLARPLLPEER--GALLEALGRALArlhavdpAALPLAGRLARL-LELLRQLEAALARLLAAELLDRLE 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671748    214 EMysLKDEMNSLRKLLDDTpSPVVFCHNDIQEGNILLlsepDSDDNLM-LVDFEYSSYNYRGFDIG---NHFCEW 284
Cdd:pfam01636 148 EL--EERLLAALLALLPAE-LPPVLVHGDLHPGNLLV----DPGGRVSgVIDFEDAGLGDPAYDLAillNSWGRE 215
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
51-285 2.39e-05

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 45.49  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748   51 QWCREYLGGAWRRARPEelsvcPVSGGLSNLLFRCSLPnhvpsvggepREVLLRLYGAILQGVDSLVLEsvmFAILA--E 128
Cdd:COG3173  10 ALLAAQLPGLAGLPEVE-----PLSGGWSNLTYRLDTG----------DRLVLRRPPRGLASAHDVRRE---ARVLRalA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  129 RSLG---PQLYGVFPEGR-------LEQYLPSRPLKTQ-ELRDPVLSGAIATRMARF----HGMEMP----FTKEPRWLF 189
Cdd:COG3173  72 PRLGvpvPRPLALGEDGEvigapfyVMEWVEGETLEDAlPDLSPAERRALARALGEFlaalHAVDPAaaglADGRPEGLE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  190 GTMERYLKQIQDLPSTSLPQMNLVEmyslkdemnSLRKLLDDT---PSPVVFCHNDIQEGNILLlsEPDSDDNLMLVDFE 266
Cdd:COG3173 152 RQLARWRAQLRRALARTDDLPALRE---------RLAAWLAANlpeWGPPVLVHGDLRPGNLLV--DPDDGRLTAVIDWE 220
                       250
                ....*....|....*....
gi 6671748  267 YSSYNYRGFDIGNHFCEWV 285
Cdd:COG3173 221 LATLGDPAADLAYLLLYWR 239
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
157-279 6.37e-05

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 44.58  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748    157 ELRDPVLSGAIATRMARFH----GMEMPFTKEPRWLFGTM-ERYLKQIQDLPSTslpqMNLVEMYSLKDEM--------- 222
Cdd:TIGR02906  83 DFNNPIDLKKAAKGLALFHhaskGYVPPDGSKIRSKLGKWpKQFEKRLKELERF----KKIALEKKYKDEFdklylkevd 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671748    223 -------NSLRKLLD--------DTPSPVVFCHNDIQEGNILLlsepdSDDNLMLVDFEYSSYNYRGFDIGN 279
Cdd:TIGR02906 159 yflergkKALELLNKskyydlckEAKKIRGFCHQDYAYHNILL-----KDNEVYVIDFDYCTIDLPVRDLRK 225
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
147-282 8.79e-04

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: 40.70  E-value: 8.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671748  147 YLPSRPLKTqelRDPVLSGAIATRMARFH--GMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLPqmNLVEMysLKDEMNS 224
Cdd:cd05153  96 FLPGESLTT---PTPEQCRAIGAALARLHlaLAGFPPPRPNPRGLAWWKPLAERLKARLDLLAA--DDRAL--LEDELAR 168
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671748  225 LRKLLDDTPsPVVFCHNDIQEGNILLLsepdsDDNLM-LVDFEYSSYNYRGFDIG---NHFC 282
Cdd:cd05153 169 LQALAPSDL-PRGVIHADLFRDNVLFD-----GDRLSgIIDFYDACYDPLLYDLAialNDWC 224
 
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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