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Conserved domains on  [gi|22330627|ref|NP_177572|]
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Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

choline kinase family protein( domain architecture ID 11476557)

choline kinase (ChoK) family protein similar to ChoK that 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)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02236 PLN02236
choline kinase
3-346 0e+00

choline kinase


:

Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 721.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627    3 MGGTEKNVENKQYRLPREVKEALQAIASEWEDVIDSKALQVIPLKGAMTNEVFQIKWPTREKGPSRKVLVRIYGEGVEIF 82
Cdd:PLN02236   1 MGMVEKTVGLSSGRIPDELKRILHSLASKWGDVVDDEALQVIPLKGAMTNEVFQIKWPTKEGNLGRKVLVRIYGEGVELF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   83 FDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLEMPGAKKALLWDRLRN 162
Cdd:PLN02236  81 FDRDDEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVLLWDRLRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  163 WLTACKRLASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIAN 242
Cdd:PLN02236 161 WLKEAKNLCSPEEAKEFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAYDIAN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  243 HFCEMAADYHTETPHIMDYSKYPGVEERQRFLKTYMSYSDEKPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEID 322
Cdd:PLN02236 241 HFCEMAADYHSETPHILDYSKYPGEEERRRFIRTYLSSSGEEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISGHVNKID 320
                        330       340
                 ....*....|....*....|....
gi 22330627  323 FDYMEYARQRFEQYWLTKPRLLAA 346
Cdd:PLN02236 321 FDYMEYARQRFEQYWLRKPELLGS 344
 
Name Accession Description Interval E-value
PLN02236 PLN02236
choline kinase
3-346 0e+00

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 721.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627    3 MGGTEKNVENKQYRLPREVKEALQAIASEWEDVIDSKALQVIPLKGAMTNEVFQIKWPTREKGPSRKVLVRIYGEGVEIF 82
Cdd:PLN02236   1 MGMVEKTVGLSSGRIPDELKRILHSLASKWGDVVDDEALQVIPLKGAMTNEVFQIKWPTKEGNLGRKVLVRIYGEGVELF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   83 FDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLEMPGAKKALLWDRLRN 162
Cdd:PLN02236  81 FDRDDEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVLLWDRLRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  163 WLTACKRLASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIAN 242
Cdd:PLN02236 161 WLKEAKNLCSPEEAKEFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAYDIAN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  243 HFCEMAADYHTETPHIMDYSKYPGVEERQRFLKTYMSYSDEKPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEID 322
Cdd:PLN02236 241 HFCEMAADYHSETPHILDYSKYPGEEERRRFIRTYLSSSGEEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISGHVNKID 320
                        330       340
                 ....*....|....*....|....
gi 22330627  323 FDYMEYARQRFEQYWLTKPRLLAA 346
Cdd:PLN02236 321 FDYMEYARQRFEQYWLRKPELLGS 344
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
41-337 8.10e-131

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: 375.77  E-value: 8.10e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  41 LQVIPLKGAMTNEVFQIKWPTREKGPSrkVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHAR 120
Cdd:cd05157   1 IKVKRITGGITNALYKVTYPSGDTPKT--VLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 121 TLSACDLRDPEISGRIATRMKEFHGLEMPGA----KKALLWDRLRNWLTACK-----RLASPEEAKSFRLDVMEMEINML 191
Cdd:cd05157  79 TLTPEDLRDPKISRLIARRLAELHSIVPLGEiegkKKPILWTTIRKWLDLAPevfedEKNKEKKLEKVDLERLRKELEWL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 192 EKSLFD-NDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIANHFCEMAADYHTetphiMDYSKYPGVEER 270
Cdd:cd05157 159 EKWLESlEKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCV-----LDYSRYPTKEEQ 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330627 271 QRFLKTYMSYSDE-----KPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEIDFDYMEYARQRFEQYW 337
Cdd:cd05157 234 RNFLRAYLESLDGlpggeEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYW 305
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
68-269 1.80e-103

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: 303.04  E-value: 1.80e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627    68 RKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLE 147
Cdd:pfam01633   3 RKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   148 MPGAKKALLWDRLRNWLTACKRL------ASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETK 221
Cdd:pfam01633  83 MPGKKSPSLWKTMRKWLSLLKNLgapesvNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNETK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 22330627   222 AITIIDYEYSCYNPVAYDIANHFCEMAADYHTETP-HIMDYSKYPGVEE 269
Cdd:pfam01633 163 RLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPTPfFKCDYSLYPTREE 211
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
168-334 2.37e-16

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 75.20  E-value: 2.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 168 KRLASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETKaITIIDYEYSCYNPVAYDIANHFCEM 247
Cdd:COG0510  15 ARLERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGR-LYLIDWEYAGLGDPAFDLAALLVEY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 248 AADYhtetphimdyskypgvEERQRFLKTYMSysdEKPSDTMVKKLLEdvekYTLASHLIWGLWGIISEHvNEIDFDYME 327
Cdd:COG0510  94 GLSP----------------EQAEELLEAYGF---GRPTEELLRRLRA----YRALADLLWALWALVRAA-QEANGDLLK 149

                ....*..
gi 22330627 328 YARQRFE 334
Cdd:COG0510 150 YLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
125-242 6.69e-04

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: 41.11  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   125 CDLRDPEISGRIATRMKEFH----GLEMP-GAKKALLWDRLRNW-------LTACKRLASPEEAKS----FRLDVMEMEI 188
Cdd:TIGR02906  82 CDFNNPIDLKKAAKGLALFHhaskGYVPPdGSKIRSKLGKWPKQfekrlkeLERFKKIALEKKYKDefdkLYLKEVDYFL 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330627   189 NMLEKSLF------------DNDENIGFCHNDLQYGNIMMDEEtkAITIIDYEYSCYNPVAYDIAN 242
Cdd:TIGR02906 162 ERGKKALEllnkskyydlckEAKKIRGFCHQDYAYHNILLKDN--EVYVIDFDYCTIDLPVRDLRK 225
 
Name Accession Description Interval E-value
PLN02236 PLN02236
choline kinase
3-346 0e+00

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 721.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627    3 MGGTEKNVENKQYRLPREVKEALQAIASEWEDVIDSKALQVIPLKGAMTNEVFQIKWPTREKGPSRKVLVRIYGEGVEIF 82
Cdd:PLN02236   1 MGMVEKTVGLSSGRIPDELKRILHSLASKWGDVVDDEALQVIPLKGAMTNEVFQIKWPTKEGNLGRKVLVRIYGEGVELF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   83 FDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLEMPGAKKALLWDRLRN 162
Cdd:PLN02236  81 FDRDDEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVLLWDRLRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  163 WLTACKRLASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIAN 242
Cdd:PLN02236 161 WLKEAKNLCSPEEAKEFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAYDIAN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  243 HFCEMAADYHTETPHIMDYSKYPGVEERQRFLKTYMSYSDEKPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEID 322
Cdd:PLN02236 241 HFCEMAADYHSETPHILDYSKYPGEEERRRFIRTYLSSSGEEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISGHVNKID 320
                        330       340
                 ....*....|....*....|....
gi 22330627  323 FDYMEYARQRFEQYWLTKPRLLAA 346
Cdd:PLN02236 321 FDYMEYARQRFEQYWLRKPELLGS 344
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
41-337 8.10e-131

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: 375.77  E-value: 8.10e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  41 LQVIPLKGAMTNEVFQIKWPTREKGPSrkVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHAR 120
Cdd:cd05157   1 IKVKRITGGITNALYKVTYPSGDTPKT--VLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 121 TLSACDLRDPEISGRIATRMKEFHGLEMPGA----KKALLWDRLRNWLTACK-----RLASPEEAKSFRLDVMEMEINML 191
Cdd:cd05157  79 TLTPEDLRDPKISRLIARRLAELHSIVPLGEiegkKKPILWTTIRKWLDLAPevfedEKNKEKKLEKVDLERLRKELEWL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 192 EKSLFD-NDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIANHFCEMAADYHTetphiMDYSKYPGVEER 270
Cdd:cd05157 159 EKWLESlEKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCV-----LDYSRYPTKEEQ 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330627 271 QRFLKTYMSYSDE-----KPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEIDFDYMEYARQRFEQYW 337
Cdd:cd05157 234 RNFLRAYLESLDGlpggeEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYW 305
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
68-269 1.80e-103

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: 303.04  E-value: 1.80e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627    68 RKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLE 147
Cdd:pfam01633   3 RKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   148 MPGAKKALLWDRLRNWLTACKRL------ASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETK 221
Cdd:pfam01633  83 MPGKKSPSLWKTMRKWLSLLKNLgapesvNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNETK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 22330627   222 AITIIDYEYSCYNPVAYDIANHFCEMAADYHTETP-HIMDYSKYPGVEE 269
Cdd:pfam01633 163 RLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPTPfFKCDYSLYPTREE 211
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
41-341 9.05e-80

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: 246.77  E-value: 9.05e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  41 LQVIPLKGAMTNEVFQIKWP---TREKGPSRKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFL 117
Cdd:cd05156   1 FGIKTITGGLSNLLYLCSLPdgvVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 118 HARTLSACDLRDPEISGRIATRMKEFHGLEMP-GAKKALLWDRLRNWLTACKRLASPEEAKSFRL-------DVMEMEIN 189
Cdd:cd05156  81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPiSKEPKWLFDTMERWLKEALSILFTDEPTKPSKqlelllsYDLAKELG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 190 MLEKSLFDNDENIGFCHNDLQYGNIMMDE-----ETKAITIIDYEYSCYNPVAYDIANHFCEMAADY-HTETPHI-MDYS 262
Cdd:cd05156 161 WLRSLLESTPSPVVFCHNDLQEGNILLLNgpensEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYtVPEPPYFkINPE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 263 KYPGVEERQRFLKTYMS-YSDEKPSDTM------VKKLLEDVEKYTLASHLIWGLWGIISEHVNEIDFDYMEYARQRFEQ 335
Cdd:cd05156 241 NYPTREQQLHFIRAYLDeQYKDKTNDLTeerskeEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                ....*.
gi 22330627 336 YWLTKP 341
Cdd:cd05156 321 YFKQKE 326
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
43-313 2.21e-68

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: 214.05  E-value: 2.21e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  43 VIPLKGAMTNEVFQIK-WPTREKGPSRKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHART 121
Cdd:cd14021   3 VIRILSGLTNQVYKVSlKDESDSLEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 122 LSACDLRDPEISGRIATRMKEFHGLEMPgakkallwdrlrnwltackrlaspeeaksfrldvmemeinmlekslfdndeN 201
Cdd:cd14021  83 LTTDELRNPSVLTSIAKLLAKFHKIKTP---------------------------------------------------P 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 202 IGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIANHFCEMAADYHTETPH--IMDYSKYPGVEERQRFLKTYMS 279
Cdd:cd14021 112 VVFCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHPEPPyfKIYKENYISEEEKRLFVSVYLS 191
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 22330627 280 YSDEK----PSDTMVKKLLEDVEKYTLASHLIWGLWGI 313
Cdd:cd14021 192 EYLEKnvlpSLDKLVEQFLQEVEIFTLGSHLYWGLWSI 229
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
26-344 5.04e-64

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 206.51  E-value: 5.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   26 QAIASEWEDVIDSKaLQVIPLKGAMTNEVFQIKwPTREKGPSRKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLL 105
Cdd:PLN02421   3 KALFKGWSDLDDSD-FSVERISGGITNLLLKVS-VKEENGNEVSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  106 GRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLEMPGAKKALLWDRLRNWLTACKRLA--SPEEAKSFR--- 180
Cdd:PLN02421  81 GVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQLWNDIFKFYEKASTVKfeDPEKQKKYEtis 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  181 LDVMEMEINMLeKSLFDN-DENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIANHFCEMAAdyhtetpHIM 259
Cdd:PLN02421 161 FEELRDEIVEL-KEITDSlKAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAG-------FDC 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  260 DYSKYPGVEERQRFLKTYMSYSD-EKPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEIDFDYMEYARQRFEQYWL 338
Cdd:PLN02421 233 DYSLYPSKEEQYHFFRHYLRPDDpEEVSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKR 312

                 ....*.
gi 22330627  339 TKPRLL 344
Cdd:PLN02421 313 QKEKLL 318
PTZ00296 PTZ00296
choline kinase; Provisional
50-345 1.09e-49

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 172.00  E-value: 1.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   50 MTNEVFQ--IKWPTREKGPS--RKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSAC 125
Cdd:PTZ00296 117 LTNQLFEvsLKEETANNYPSirRRVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSGGRIEEWLYGDPLRID 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  126 DLRDPEISGRIATRMKEFHGL----EMPGA--KKALLWDRLRNWLTACKRLASPE-EAKSFRLDVMEMEINMLEKSLFDN 198
Cdd:PTZ00296 197 DLKNPSILIGIANVLGKFHTLsrkrHLPEHwdRTPCIFKMMEKWKNQLSKYKNIEkYQRDIHKYIKESEKFIKFMKVYSK 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  199 DENIG----FCHNDLQYGNIMmdEETKAITIIDYEYSCYNPVAYDIANHFCEMAADYhTETPH---IMDYSKYPGVEERQ 271
Cdd:PTZ00296 277 SDNLAndivFCHNDLQENNII--NTNKCLRLIDFEYSGYNFLATDIANFFIETTIDY-SVSHYpffAIDKKKYISYENRK 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  272 RFLKTYMSYSDEKP----SDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNEI--DFDYMEYARQRFEQYWLTKPRLLA 345
Cdd:PTZ00296 354 LFITAYLSNYLDKSlvvpNPKIIDQILEAVEVQALGAHLLWGFWSIIRGYQTKSynEFDFFLYAKERFKMYDEQKEYLIS 433
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
43-247 2.04e-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: 105.33  E-value: 2.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  43 VIPLKGAMTNEVFQIKWPtrekgpSRKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGN--GRIEEFLHAR 120
Cdd:cd05151   3 IEPLKGGLTNKNYLVEVA------GKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPEtgVKITEFIEGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 121 TLSACDLRDPEISGRIATRMKEFHGLEMPgakkallwdrlrnwltackrlaspeeaksfrldvmemeinmlekslfdnde 200
Cdd:cd05151  77 TLLTNDFSDPENLERIAALLRKLHSSPLE--------------------------------------------------- 105
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 22330627 201 NIGFCHNDLQYGNIMMDEETkaITIIDYEYSCYNPVAYDIANHFCEM 247
Cdd:cd05151 106 DLVLCHNDLVPGNFLLDDDR--LYLIDWEYAGMNDPLFDLAALFSEN 150
PTZ00384 PTZ00384
choline kinase; Provisional
32-343 5.85e-27

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 109.48  E-value: 5.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   32 WEDVIDSKaLQVIPLKGAMTNEVFQIKW--PTREKGPSRKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFG 109
Cdd:PTZ00384  45 WNNVNPEF-IEIKKMNNGITNQVYQATLvdGDKDRYPIKSVCIKKSSTYNSLVIDNDLQYNIAKLLGDNNFGPKIIGRFG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  110 NGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLEMPGAKKAllWDRLRNWLTACKRLASPEE--AKSFRL--DVME 185
Cdd:PTZ00384 124 DFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHKRVTELVPKE--WDRTPMFLTKISTWSQHVEriIKKYNLdfDYNE 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  186 MEINM-LEKSLFDNDEN--------IGFCHNDLQYGNIMmdEETKAITIIDYEYSCYNPVAYDIANHFCEMAADYHTETP 256
Cdd:PTZ00384 202 LVQNYeLFKKILNNHLNtsnsitnsVLFCHNDLFFTNIL--DFNQGIYFIDFDFAGFNYVGWEIANFFVKLYIVYDPPTP 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  257 HIMDYSKYPGVEERQR--FLKTYMSY---SDEKPSDTMVKKLLEDVEKYTLASHLIWGLWGII--SEHVNEIDFDYMEYA 329
Cdd:PTZ00384 280 PYFNSDDSLALSEEMKtiFVSVYLSQllgKNVLPSDDLVKEFLQSLEIHTLGVNLFWTYWGIVmnDKPKNELSKPVKFEA 359
                        330
                 ....*....|....
gi 22330627  330 RQRFeQYWLTKPRL 343
Cdd:PTZ00384 360 YAKF-QYNLFKNNL 372
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
168-334 2.37e-16

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 75.20  E-value: 2.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 168 KRLASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETKaITIIDYEYSCYNPVAYDIANHFCEM 247
Cdd:COG0510  15 ARLERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGR-LYLIDWEYAGLGDPAFDLAALLVEY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 248 AADYhtetphimdyskypgvEERQRFLKTYMSysdEKPSDTMVKKLLEdvekYTLASHLIWGLWGIISEHvNEIDFDYME 327
Cdd:COG0510  94 GLSP----------------EQAEELLEAYGF---GRPTEELLRRLRA----YRALADLLWALWALVRAA-QEANGDLLK 149

                ....*..
gi 22330627 328 YARQRFE 334
Cdd:COG0510 150 YLLRRLE 156
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
45-247 2.73e-12

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: 63.86  E-value: 2.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  45 PLKGAMTNEVFQIkwptrekGPSRKVLVRIYGEgvEIFFDREDEIRTFEFMSKHG--HGPLLLGRF----GNGRIEEFLH 118
Cdd:cd05120   5 LIKEGGDNKVYLL-------GDPREYVLKIGPP--RLKKDLEKEAAMLQLLAGKLslPVPKVYGFGesdgWEYLLMERIE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 119 ARTLSACDLRDPE-----ISGRIATRMKEFHGLEMPGakkallwdrlrnwltackrlaspeeaksfrldvmemeinmlek 193
Cdd:cd05120  76 GETLSEVWPRLSEeekekIADQLAEILAALHRIDSSV------------------------------------------- 112
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 22330627 194 slfdndenigFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIANHFCEM 247
Cdd:cd05120 113 ----------LTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
43-246 1.44e-11

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: 63.67  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627    43 VIPLKGAMTNEVFQIKWPTREkgpsrkVLVRIYgEGVEIFFDREDEIRTFEFMSKHGHGP---LLLGRFGNGRIE----- 114
Cdd:pfam01636   2 LRPISSGASNRTYLVTTGDGR------YVLRLP-PPGRAAEELRRELALLRHLAAAGVPPvprVLAGCTDAELLGlpfll 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   115 -EFLHARTLSacDLRDPEISGRIATRM----KEFHGLemPGAKKALLWDRLRN-----WLTACKRLASPEEAKSFRLDVM 184
Cdd:pfam01636  75 mEYLPGEVLA--RPLLPEERGALLEALgralARLHAV--DPAALPLAGRLARLlellrQLEAALARLLAAELLDRLEELE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330627   185 EMEINMLEKSLfDNDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIA---NHFCE 246
Cdd:pfam01636 151 ERLLAALLALL-PAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAillNSWGR 214
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
23-337 9.16e-09

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: 55.70  E-value: 9.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  23 EALQAIASEWeDVIDSKALQVIplkGAMTNEVFQIkwpTREKGpsRKVLVRIYgegvEIFFDREDEIRTF-EFMSK-HGH 100
Cdd:COG2334   1 DELAAALERY-GLGPLSSLKPL---NSGENRNYRV---ETEDG--RRYVLKLY----RPGRWSPEEIPFElALLAHlAAA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 101 G-----PL------LLGRFGNG--RIEEFLHARTLsacDLRDPEISGRIATRMKEFH----GLEMPGAKKALLWDRLRNW 163
Cdd:COG2334  68 GlpvpaPVptrdgeTLLELEGRpaALFPFLPGRSP---EEPSPEQLEELGRLLARLHralaDFPRPNARDLAWWDELLER 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 164 LTAcKRLASPEEAksfrlDVMEMEINMLEKSL--FDNDENIGFCHNDLQYGNIMMDEEtKAITIIDYEYSCYNPVAYDIA 241
Cdd:COG2334 145 LLG-PLLPDPEDR-----ALLEELLDRLEARLapLLGALPRGVIHGDLHPDNVLFDGD-GVSGLIDFDDAGYGPRLYDLA 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 242 nhfceMAADYHTETPHIMDYskypgveeRQRFLKTYMSYSDEKPSDtmvKKLLEDVEKYTLASHLIWGLWgiiseHVNEI 321
Cdd:COG2334 218 -----IALNGWADGPLDPAR--------LAALLEGYRAVRPLTEAE---LAALPPLLRLRALRFLAWRLR-----RVRAK 276
                       330
                ....*....|....*.
gi 22330627 322 DFDYMEYARQRFEQYW 337
Cdd:COG2334 277 DPAFERYLRRQIALAW 292
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
203-245 7.21e-07

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: 49.95  E-value: 7.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 22330627 203 GFCHNDLQYGNIMMDEEtKAITIIDYEYSCYNPVAYDIA---NHFC 245
Cdd:cd05153 180 GVIHADLFRDNVLFDGD-RLSGIIDFYDACYDPLLYDLAialNDWC 224
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
181-242 1.26e-05

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 46.43  E-value: 1.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330627 181 LDVMEMEINMLEKS-----LFDNDENIGFCHNDLQYGNIMMDEETKAItIIDYEYSCYNPVAYDIAN 242
Cdd:COG5881 175 LEQAEKALELLEKSayyklVKEAKKEGGFCHHDYAYHNILIDEDGKIY-IIDFDYCIYDLPVHDLAK 240
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
18-243 1.45e-05

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 45.88  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  18 PREVKEALQAIASEWEDVIDskalqVIPLKGAMTNEVFQIKWPTRekgpsrkVLVRIYGEGVEIFFDREDEIRTFEFMSK 97
Cdd:COG3173   5 EAALRALLAAQLPGLAGLPE-----VEPLSGGWSNLTYRLDTGDR-------LVLRRPPRGLASAHDVRREARVLRALAP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627  98 HGHGP----LLLGRFGNGR-----IEEFLHARTLSAC-DLRDPEISGRIATRM----KEFHGLEMPGA-----KKALLWD 158
Cdd:COG3173  73 RLGVPvprpLALGEDGEVIgapfyVMEWVEGETLEDAlPDLSPAERRALARALgeflAALHAVDPAAAgladgRPEGLER 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 159 RLRNWLtacKRLASPEEAKSFRLDVMEMEINMLEKSLfDNDENIGFCHNDLQYGNIMMDEETKAIT-IIDYEYSCYNPVA 237
Cdd:COG3173 153 QLARWR---AQLRRALARTDDLPALRERLAAWLAANL-PEWGPPVLVHGDLRPGNLLVDPDDGRLTaVIDWELATLGDPA 228

                ....*.
gi 22330627 238 YDIANH 243
Cdd:COG3173 229 ADLAYL 234
MthN COG4857
5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and ...
206-242 4.13e-04

5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and metabolism];


Pssm-ID: 443885  Cd Length: 404  Bit Score: 41.75  E-value: 4.13e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 22330627 206 HNDLQYGNIMM-DEETKaitIIDYEYSCYNPVAYDIAN 242
Cdd:COG4857 227 HGDLHTGSIFVnEDSTK---VIDPEFAFYGPIGFDIGN 261
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
125-242 6.69e-04

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: 41.11  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627   125 CDLRDPEISGRIATRMKEFH----GLEMP-GAKKALLWDRLRNW-------LTACKRLASPEEAKS----FRLDVMEMEI 188
Cdd:TIGR02906  82 CDFNNPIDLKKAAKGLALFHhaskGYVPPdGSKIRSKLGKWPKQfekrlkeLERFKKIALEKKYKDefdkLYLKEVDYFL 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330627   189 NMLEKSLF------------DNDENIGFCHNDLQYGNIMMDEEtkAITIIDYEYSCYNPVAYDIAN 242
Cdd:TIGR02906 162 ERGKKALEllnkskyydlckEAKKIRGFCHQDYAYHNILLKDN--EVYVIDFDYCTIDLPVRDLRK 225
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
145-277 1.10e-03

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: 39.91  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330627 145 GLEMPGAKKALLWDRLRNWLtacKRLaspEEAKSFRLDVMEMEINMLEKSLFDNDEnIGFCHNDLQYGNIMMDEETKAIT 224
Cdd:cd05154 127 GLADLGRPEGYLERQVDRWR---RQL---EAAATDPPPALEEALRWLRANLPADGR-PVLVHGDFRLGNLLFDPDGRVTA 199
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 22330627 225 IIDYEYSCY-NPVAyDIANhFCeMAADYHTETPHIMDYSKYPGVEERQRFLKTY 277
Cdd:cd05154 200 VLDWELATLgDPLE-DLAW-LL-ARWWRPGDPPGLAAPTRLPGFPSREELLARY 250
 
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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