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Conserved domains on  [gi|1834134240]
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Chain A, Choline kinase

Protein Classification

ethanolamine kinase( domain architecture ID 10142388)

ethanolamine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn)

CATH:  1.10.510.10
EC:  2.7.1.82
Gene Ontology:  GO:0004305|GO:0006646|GO:0005524
PubMed:  16244704

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
53-432 2.11e-110

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: 327.62  E-value: 2.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  53 IHLQKVSGALTNAVFFVSFNPAPNPTspsesplltptippsdpshpppltpeqyphTLLFRVYGPSSDALISRSEELRIL 132
Cdd:cd05157     1 IKVKRITGGITNALYKVTYPSGDTPK------------------------------TVLVRIYGPGTELLIDRDRELRIL 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 133 HVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLRrlgYEQGRATEPALWICLKEWS 212
Cdd:cd05157    51 QLLS-RAGIGPKLYGRFENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPL---GEIEGKKKPILWTTIRKWL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 213 EAAEDVISSLTAlggtLEAWVERFSLHRIREEVTIYRNFVESQsgKGNGVVFAHNDTQYGNLLRldvelppnTPEHCRYI 292
Cdd:cd05157   127 DLAPEVFEDEKN----KEKKLEKVDLERLRKELEWLEKWLESL--EKSPIVFCHNDLLYGNILY--------NEDDDSVT 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 293 VIDFEYASPNPRGYDIANHFHEWRANYHHPTHShsliphfPYPTPIQREDFYRSYLSVEVDGRNGEEVVgkrkdvpADKV 372
Cdd:cd05157   193 FIDFEYAGPNPRAFDIANHFCEWAGFYCVLDYS-------RYPTKEEQRNFLRAYLESLDGLPGGEEVS-------EEEV 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 373 AALEHEVRIWSPGCSINWALWGLVQAEEQvcalatkkegyVPEFDYLSYAAERLEMFRDE 432
Cdd:cd05157   259 EKLYNEVNLFRLASHLFWGLWALIQAAIS-----------SIDFDYLGYAKERLDEYWGD 307
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
53-432 2.11e-110

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: 327.62  E-value: 2.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  53 IHLQKVSGALTNAVFFVSFNPAPNPTspsesplltptippsdpshpppltpeqyphTLLFRVYGPSSDALISRSEELRIL 132
Cdd:cd05157     1 IKVKRITGGITNALYKVTYPSGDTPK------------------------------TVLVRIYGPGTELLIDRDRELRIL 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 133 HVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLRrlgYEQGRATEPALWICLKEWS 212
Cdd:cd05157    51 QLLS-RAGIGPKLYGRFENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPL---GEIEGKKKPILWTTIRKWL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 213 EAAEDVISSLTAlggtLEAWVERFSLHRIREEVTIYRNFVESQsgKGNGVVFAHNDTQYGNLLRldvelppnTPEHCRYI 292
Cdd:cd05157   127 DLAPEVFEDEKN----KEKKLEKVDLERLRKELEWLEKWLESL--EKSPIVFCHNDLLYGNILY--------NEDDDSVT 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 293 VIDFEYASPNPRGYDIANHFHEWRANYHHPTHShsliphfPYPTPIQREDFYRSYLSVEVDGRNGEEVVgkrkdvpADKV 372
Cdd:cd05157   193 FIDFEYAGPNPRAFDIANHFCEWAGFYCVLDYS-------RYPTKEEQRNFLRAYLESLDGLPGGEEVS-------EEEV 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 373 AALEHEVRIWSPGCSINWALWGLVQAEEQvcalatkkegyVPEFDYLSYAAERLEMFRDE 432
Cdd:cd05157   259 EKLYNEVNLFRLASHLFWGLWALIQAAIS-----------SIDFDYLGYAKERLDEYWGD 307
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
110-326 5.51e-64

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: 205.20  E-value: 5.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 110 LLFRVYGPSSDALISRSEELRILHVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDL 189
Cdd:pfam01633   5 VLLRIYGPGTELLINREDEIVNFALLS-ERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 190 RRLGyeqgratEPALWICLKEWSEAAEDVISSLTAlggTLEAWVERFSLHRIREEVTIYRNFVESqsgKGNGVVFAHNDT 269
Cdd:pfam01633  84 PGKK-------SPSLWKTMRKWLSLLKNLGAPESV---NKSEQLKSINLEDLEKEINKLEKWLEL---LDSPIVFCHNDL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834134240 270 QYGNLLrldvelppNTPEHCRYIVIDFEYASPNPRGYDIANHFHEWRANYHHPTHSH 326
Cdd:pfam01633 151 QSGNIL--------LLNETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPTPFF 199
PLN02236 PLN02236
choline kinase
107-427 6.24e-55

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 186.02  E-value: 6.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 107 PHTLLFRVYGPSSDALISRSEELRILHVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHS 186
Cdd:PLN02236   65 GRKVLVRIYGEGVELFFDRDDEIRTFECMS-RHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 187 VDLrrlgyeQGrATEPALWICLKEWSEAAEDVISSLTAlggtleawvERFSLHRIREEVtiyrNFVESQ-SGKGNGVVFA 265
Cdd:PLN02236  144 LDM------PG-PKNVLLWDRLRNWLKEAKNLCSPEEA---------KEFRLDSLEDEI----NLLEKElSGDDQEIGFC 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 266 HNDTQYGNLLrLDvelppntpEHCRYI-VIDFEYASPNPRGYDIANHFHEWRANYHHPThshsliPHF----PYPTPIQR 340
Cdd:PLN02236  204 HNDLQYGNIM-ID--------EETRAItIIDYEYASYNPVAYDIANHFCEMAADYHSET------PHIldysKYPGEEER 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 341 EDFYRSYLSVEvdgrnGEEvvgkrkdVPADKVAALEHEVRIWSPGCSINWALWGLVQaeeqvcalatkkeGYVP--EFDY 418
Cdd:PLN02236  269 RRFIRTYLSSS-----GEE-------PSDEEVEQLLDDVEKYTLASHLFWGLWGIIS-------------GHVNkiDFDY 323

                  ....*....
gi 1834134240 419 LSYAAERLE 427
Cdd:PLN02236  324 MEYARQRFE 332
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
238-403 3.61e-09

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 55.56  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 238 LHRIREEVTIYRNFVESQSGKgngVVFAHNDTQYGNLLRldvelppnTPEHcRYIVIDFEYASPNPRGYDIANHFHEWRa 317
Cdd:COG0510    28 LPELLRRLEELERALAARPLP---LVLCHGDLHPGNFLV--------TDDG-RLYLIDWEYAGLGDPAFDLAALLVEYG- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 318 nyhhpthshsliphfpyPTPIQREDFYRSYLSVEVDgrngeevvgkrkdvpadkvAALEHEVRIWSPGCSINWALWGLVQ 397
Cdd:COG0510    95 -----------------LSPEQAEELLEAYGFGRPT-------------------EELLRRLRAYRALADLLWALWALVR 138

                  ....*.
gi 1834134240 398 AEEQVC 403
Cdd:COG0510   139 AAQEAN 144
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
53-432 2.11e-110

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: 327.62  E-value: 2.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  53 IHLQKVSGALTNAVFFVSFNPAPNPTspsesplltptippsdpshpppltpeqyphTLLFRVYGPSSDALISRSEELRIL 132
Cdd:cd05157     1 IKVKRITGGITNALYKVTYPSGDTPK------------------------------TVLVRIYGPGTELLIDRDRELRIL 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 133 HVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLRrlgYEQGRATEPALWICLKEWS 212
Cdd:cd05157    51 QLLS-RAGIGPKLYGRFENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPL---GEIEGKKKPILWTTIRKWL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 213 EAAEDVISSLTAlggtLEAWVERFSLHRIREEVTIYRNFVESQsgKGNGVVFAHNDTQYGNLLRldvelppnTPEHCRYI 292
Cdd:cd05157   127 DLAPEVFEDEKN----KEKKLEKVDLERLRKELEWLEKWLESL--EKSPIVFCHNDLLYGNILY--------NEDDDSVT 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 293 VIDFEYASPNPRGYDIANHFHEWRANYHHPTHShsliphfPYPTPIQREDFYRSYLSVEVDGRNGEEVVgkrkdvpADKV 372
Cdd:cd05157   193 FIDFEYAGPNPRAFDIANHFCEWAGFYCVLDYS-------RYPTKEEQRNFLRAYLESLDGLPGGEEVS-------EEEV 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 373 AALEHEVRIWSPGCSINWALWGLVQAEEQvcalatkkegyVPEFDYLSYAAERLEMFRDE 432
Cdd:cd05157   259 EKLYNEVNLFRLASHLFWGLWALIQAAIS-----------SIDFDYLGYAKERLDEYWGD 307
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
110-326 5.51e-64

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: 205.20  E-value: 5.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 110 LLFRVYGPSSDALISRSEELRILHVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDL 189
Cdd:pfam01633   5 VLLRIYGPGTELLINREDEIVNFALLS-ERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 190 RRLGyeqgratEPALWICLKEWSEAAEDVISSLTAlggTLEAWVERFSLHRIREEVTIYRNFVESqsgKGNGVVFAHNDT 269
Cdd:pfam01633  84 PGKK-------SPSLWKTMRKWLSLLKNLGAPESV---NKSEQLKSINLEDLEKEINKLEKWLEL---LDSPIVFCHNDL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834134240 270 QYGNLLrldvelppNTPEHCRYIVIDFEYASPNPRGYDIANHFHEWRANYHHPTHSH 326
Cdd:pfam01633 151 QSGNIL--------LLNETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPTPFF 199
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
53-429 2.29e-57

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: 191.69  E-value: 2.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  53 IHLQKVSGALTNAVFFVSfNPAPNPTSPSEsplltptippsdpshpppltpeqyPHTLLFRVYGPSSDALISRSEELRIL 132
Cdd:cd05156     1 FGIKTITGGLSNLLYLCS-LPDGVVPVGGE------------------------PRKVLLRIYGQILQAEESLVTESVIF 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 133 HVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLrRLGYEQGRatepaLWICLKEWs 212
Cdd:cd05156    56 ALLS-ERGLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEM-PISKEPKW-----LFDTMERW- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 213 eaaedvISSLTALGGTLEAWVERFSLHRIR-----EEVTIYRNFVESQSGKgngVVFAHNDTQYGNLLRLDVELPPNTPE 287
Cdd:cd05156   128 ------LKEALSILFTDEPTKPSKQLELLLsydlaKELGWLRSLLESTPSP---VVFCHNDLQEGNILLLNGPENSEDDK 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 288 hcrYIVIDFEYASPNPRGYDIANHFHEWRANYHHPTHshsliPHFP-----YPTPIQREDFYRSYLSvevdgrngEEVVG 362
Cdd:cd05156   199 ---LVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEP-----PYFKinpenYPTREQQLHFIRAYLD--------EQYKD 262
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 363 KRKDVPADKVAALEH---EVRIWSPGCSINWALWGLVQAEEQVCalatkkegyvpEFDYLSYAAERLEMF 429
Cdd:cd05156   263 KTNDLTEERSKEEEKlllEVNRFALASHFFWGLWSIVQAKISSI-----------EFGYLEYAQARLDAY 321
PLN02236 PLN02236
choline kinase
107-427 6.24e-55

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 186.02  E-value: 6.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 107 PHTLLFRVYGPSSDALISRSEELRILHVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHS 186
Cdd:PLN02236   65 GRKVLVRIYGEGVELFFDRDDEIRTFECMS-RHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 187 VDLrrlgyeQGrATEPALWICLKEWSEAAEDVISSLTAlggtleawvERFSLHRIREEVtiyrNFVESQ-SGKGNGVVFA 265
Cdd:PLN02236  144 LDM------PG-PKNVLLWDRLRNWLKEAKNLCSPEEA---------KEFRLDSLEDEI----NLLEKElSGDDQEIGFC 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 266 HNDTQYGNLLrLDvelppntpEHCRYI-VIDFEYASPNPRGYDIANHFHEWRANYHHPThshsliPHF----PYPTPIQR 340
Cdd:PLN02236  204 HNDLQYGNIM-ID--------EETRAItIIDYEYASYNPVAYDIANHFCEMAADYHSET------PHIldysKYPGEEER 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 341 EDFYRSYLSVEvdgrnGEEvvgkrkdVPADKVAALEHEVRIWSPGCSINWALWGLVQaeeqvcalatkkeGYVP--EFDY 418
Cdd:PLN02236  269 RRFIRTYLSSS-----GEE-------PSDEEVEQLLDDVEKYTLASHLFWGLWGIIS-------------GHVNkiDFDY 323

                  ....*....
gi 1834134240 419 LSYAAERLE 427
Cdd:PLN02236  324 MEYARQRFE 332
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
53-395 1.04e-42

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: 150.11  E-value: 1.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  53 IHLQKVSGALTNAVFFVSfNPAPNPTSPsesplltptippsdpshpppltpeqyPHTLLFRVYGPSSDALISRSEELRIL 132
Cdd:cd14021     1 ILVIRILSGLTNQVYKVS-LKDESDSLE--------------------------PKKVLFRIYGKYLSTLYDREKESEVF 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 133 HVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSvdlrrlgyeqgRATEPalwiclkews 212
Cdd:cd14021    54 KILS-EQGLGPKLIYKFDGGRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHK-----------IKTPP---------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 213 eaaedvissltalggtleawverfslhrireevtiyrnfvesqsgkgngVVFAHNDTQYGNLLrldvelppNTPEHCRYI 292
Cdd:cd14021   112 -------------------------------------------------VVFCHNDLQENNIL--------LTNDQDGLR 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 293 VIDFEYASPNPRGYDIANHFHEWRANYHHPthshslIPHFP------YPTPIQREDFYRSYLSvevdgrngeEVVGKRKD 366
Cdd:cd14021   135 LIDFEYSGFNYRGYDIANFFNESMIDYDHP------EPPYFkiykenYISEEEKRLFVSVYLS---------EYLEKNVL 199
                         330       340       350
                  ....*....|....*....|....*....|
gi 1834134240 367 VPADK-VAALEHEVRIWSPGCSINWALWGL 395
Cdd:cd14021   200 PSLDKlVEQFLQEVEIFTLGSHLYWGLWSI 229
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
113-436 5.96e-42

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 151.04  E-value: 5.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 113 RVYGPSSDALISRSEELRILHVLSTQyGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLrrl 192
Cdd:PLN02421   48 RLFGPNTDYVIDRERELQAIKYLSAA-GFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEI--- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 193 gyeQGrATEPALWICLKEWSEAAEDVISSLTALGGTLEAwverFSLHRIREEVTIYRNFVESQSGKgngVVFAHNDTQYG 272
Cdd:PLN02421  124 ---PG-SKEPQLWNDIFKFYEKASTVKFEDPEKQKKYET----ISFEELRDEIVELKEITDSLKAP---VVFAHNDLLSG 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 273 NLLRldvelppNTPEHCRYIvIDFEYASPNPRGYDIANHFHEWrANYHhptHSHSLiphfpYPTPIQREDFYRSYLSVEv 352
Cdd:PLN02421  193 NLML-------NEDEGKLYF-IDFEYGSYSYRGYDIGNHFNEY-AGFD---CDYSL-----YPSKEEQYHFFRHYLRPD- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 353 dgrngeevvgKRKDVPADKVAALEHEVRIWSPGCSINWALWGLVQAEeqvcalatkkegYVP-EFDYLSYAAERLEMFRD 431
Cdd:PLN02421  255 ----------DPEEVSDAELEELFVETNFYALASHLYWAIWAIVQAK------------MSPiDFDYLGYFFLRYKEYKR 312

                  ....*
gi 1834134240 432 EAKKL 436
Cdd:PLN02421  313 QKEKL 317
PTZ00296 PTZ00296
choline kinase; Provisional
40-436 5.89e-31

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 123.46  E-value: 5.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  40 VPRWSSplLTPTNIHLQKVSGALTNAVFFVSFNPApnptspsesplltptippsdpshppplTPEQYPHT---LLFRVYG 116
Cdd:PTZ00296   97 VPEWRR--FTEDDVRVNQILSGLTNQLFEVSLKEE---------------------------TANNYPSIrrrVLFRIYG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 117 PSSDALISRSEELRILHVLStQYGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDlRRLGYEQ 196
Cdd:PTZ00296  148 KDVDELYNPISEFEVYKTMS-KYRIAPQLLNTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLS-RKRHLPE 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 197 GRATEPALWICLKEWSEAAEDVissltalggtleAWVERFSLH--RIREEVTIYRNFVESQS---GKGNGVVFAHNDTQY 271
Cdd:PTZ00296  226 HWDRTPCIFKMMEKWKNQLSKY------------KNIEKYQRDihKYIKESEKFIKFMKVYSksdNLANDIVFCHNDLQE 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 272 GNLLrldvelppNTPEHCRYivIDFEYASPNPRGYDIANHFHEWRANYHHPTHSHSLIPHFPYPTPIQREDFYRSYLSve 351
Cdd:PTZ00296  294 NNII--------NTNKCLRL--IDFEYSGYNFLATDIANFFIETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYLS-- 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 352 vdgrngeEVVGKRKDVPADK-VAALEHEVRIWSPGCSINWALWGLVQAEEqvcalaTKKEGyvpEFDYLSYAAERLEMFR 430
Cdd:PTZ00296  362 -------NYLDKSLVVPNPKiIDQILEAVEVQALGAHLLWGFWSIIRGYQ------TKSYN---EFDFFLYAKERFKMYD 425

                  ....*.
gi 1834134240 431 DEAKKL 436
Cdd:PTZ00296  426 EQKEYL 431
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
53-316 6.96e-17

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: 77.21  E-value: 6.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  53 IHLQKVSGALTNAVFFVSFNPapnptspsesplltptippsdpshpppltpEQYphtlLFRVYGPSSDALISRSEELRIL 132
Cdd:cd05151     1 ITIEPLKGGLTNKNYLVEVAG------------------------------KKY----VLRIPGAGTELLIDRENEKANS 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 133 HVLStQYGIGPRVFG--TFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLRRLgyeqgratepalwiclke 210
Cdd:cd05151    47 KAAA-ELGIAPEVIYfdPETGVKITEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLEDL------------------ 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 211 wseaaedvissltalggtleawverfslhrireevtiyrnfvesqsgkgngvVFAHNDTQYGNLLRLDVELppntpehcr 290
Cdd:cd05151   108 ----------------------------------------------------VLCHNDLVPGNFLLDDDRL--------- 126
                         250       260
                  ....*....|....*....|....*.
gi 1834134240 291 YIvIDFEYASPNPRGYDIANHFHEWR 316
Cdd:cd05151   127 YL-IDWEYAGMNDPLFDLAALFSENN 151
PTZ00384 PTZ00384
choline kinase; Provisional
39-400 1.28e-10

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 62.87  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240  39 HVPRWSSplLTPTNIHLQKVSGALTNAVFFVSFNPAPNPTSPSESPLLTPTIPPSDPSHPPPLtpeQYphtllfrvygps 118
Cdd:PTZ00384   41 HVPFWNN--VNPEFIEIKKMNNGITNQVYQATLVDGDKDRYPIKSVCIKKSSTYNSLVIDNDL---QY------------ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 119 sdalisrseelRILHVLSTQyGIGPRVFGTFTNGRVEEFFPSRALTAQELRDPIISRGIARRMRELHSVDLRRLGYEQGR 198
Cdd:PTZ00384  104 -----------NIAKLLGDN-NFGPKIIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHKRVTELVPKEWDR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 199 AtePALWICLKEWSEAAEDVISSLTaLGGTLEAWVERFSLHRireevTIYRNFVESQSGKGNGVVFAHNDTQYGNLLRLD 278
Cdd:PTZ00384  172 T--PMFLTKISTWSQHVERIIKKYN-LDFDYNELVQNYELFK-----KILNNHLNTSNSITNSVLFCHNDLFFTNILDFN 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 279 velppntpeHCRYIvIDFEYASPNPRGYDIANHFHEWRANYHHPTHsHSLIPHFPYPTPIQREDFYRS-YLSvEVDGRNg 357
Cdd:PTZ00384  244 ---------QGIYF-IDFDFAGFNYVGWEIANFFVKLYIVYDPPTP-PYFNSDDSLALSEEMKTIFVSvYLS-QLLGKN- 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1834134240 358 eevVGKRKDVPADKVAALEhevrIWSPGCSINWALWGLVQAEE 400
Cdd:PTZ00384  311 ---VLPSDDLVKEFLQSLE----IHTLGVNLFWTYWGIVMNDK 346
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
238-403 3.61e-09

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 55.56  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 238 LHRIREEVTIYRNFVESQSGKgngVVFAHNDTQYGNLLRldvelppnTPEHcRYIVIDFEYASPNPRGYDIANHFHEWRa 317
Cdd:COG0510    28 LPELLRRLEELERALAARPLP---LVLCHGDLHPGNFLV--------TDDG-RLYLIDWEYAGLGDPAFDLAALLVEYG- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 318 nyhhpthshsliphfpyPTPIQREDFYRSYLSVEVDgrngeevvgkrkdvpadkvAALEHEVRIWSPGCSINWALWGLVQ 397
Cdd:COG0510    95 -----------------LSPEQAEELLEAYGFGRPT-------------------EELLRRLRAYRALADLLWALWALVR 138

                  ....*.
gi 1834134240 398 AEEQVC 403
Cdd:COG0510   139 AAQEAN 144
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
106-316 5.98e-06

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 47.80  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 106 YPHTLLFRVYGPSSDALISRSEELRILHVLSTQYGIG-PRVFGTFTNGRVE-------EFFPSRALTAQ-ELRDPIISRG 176
Cdd:COG3173    41 TGDRLVLRRPPRGLASAHDVRREARVLRALAPRLGVPvPRPLALGEDGEVIgapfyvmEWVEGETLEDAlPDLSPAERRA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 177 IARRM----RELHSVDLRRLGYEQGRAtePALWICLKEWSEAAEDVISSLTALGGTLEAWVERFSLHRIREEvtiyrnfv 252
Cdd:COG3173   121 LARALgeflAALHAVDPAAAGLADGRP--EGLERQLARWRAQLRRALARTDDLPALRERLAAWLAANLPEWG-------- 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834134240 253 esqsgkgnGVVFAHNDTQYGNLLRldvelppnTPEHCRYI-VIDFEYASPNPRGYDIANHFHEWR 316
Cdd:COG3173   191 --------PPVLVHGDLRPGNLLV--------DPDDGRLTaVIDWELATLGDPAADLAYLLLYWR 239
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
262-316 2.76e-03

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: 38.44  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1834134240 262 VVFAHNDTQYGNLLrLDvelppNTPEHCRyiVIDFEYASPNPRGYDIANHFHEWR 316
Cdd:cd05120   111 SVLTHGDLHPGNIL-VK-----PDGKLSG--IIDWEFAGYGPPAFDYAAALRDWT 157
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
109-318 5.79e-03

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: 38.25  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 109 TLLFRVYgPSSDALISRSEELRILHVLSTQyGIG--PRVFGTFTNGRVEEFfPSRALT---AQELRDPIISRGIARRMRE 183
Cdd:pfam01636  22 RYVLRLP-PPGRAAEELRRELALLRHLAAA-GVPpvPRVLAGCTDAELLGL-PFLLMEylpGEVLARPLLPEERGALLEA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834134240 184 LHSV--DLRRLGYEQGR-ATEPALWicLKEWSEAAEDVISSLTALGGTLEAWVERFSLHRIREEVTIYRNFVesqsgkgn 260
Cdd:pfam01636  99 LGRAlaRLHAVDPAALPlAGRLARL--LELLRQLEAALARLLAAELLDRLEELEERLLAALLALLPAELPPV-------- 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834134240 261 gvvFAHNDTQYGNLLRldvelppNTPEHCRYiVIDFEYASPNPRGYDIANHFHEWRAN 318
Cdd:pfam01636 169 ---LVHGDLHPGNLLV-------DPGGRVSG-VIDFEDAGLGDPAYDLAILLNSWGRE 215
 
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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