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Conserved domains on  [gi|122484148|sp|Q251V5|]
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RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Short=CMK; AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase

Protein Classification

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase( domain architecture ID 11449259)

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol in isoprenoid biosynthesis

CATH:  3.30.230.10
EC:  2.7.1.148
PubMed:  12878729
SCOP:  4000959|4000643

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IspE COG1947
4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]; ...
6-284 5.59e-104

4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]; 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


:

Pssm-ID: 441550 [Multi-domain]  Cd Length: 281  Bit Score: 304.35  E-value: 5.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   6 VEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAE-GGIQCSCGEWS---GPENLAYRAAEAFLSGLGSS 81
Cdd:COG1947    2 LTVKAPAKINLFLHVTGRRPDGYHELETVFQFIDLGDTLTIEPADdGSISLTGPGAGvptDEDNLVYRAARLLQEATGIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  82 QGIHIDIEKNIPVQaglgggsadaaaalqalNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAP 161
Cdd:COG1947   82 PGVDIHLEKRIPVGaglgggssdaaatlralNRLWGLGLSREELAELAAKLGADVPFFLYGGTALAEGRGEKLTPLPPLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 162 KINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAEsLIPLLYNDLEPASMKLLPEIAWVKEELMKQnGC 241
Cdd:COG1947  162 ELWLVLVKPGVGVSTAEVYRALDLTRDTPPPDIDALLAALAAGDAA-LAALLRNDLEPVAFKLYPEIAEVLEALLEA-GA 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 122484148 242 LGALMSGSGSAVFGIVQTEEQAEKIAAIWRERnYHVWVTHTME 284
Cdd:COG1947  240 LAARMSGSGSTVFGLFEDEEAAEAAAAALPAR-GGVFVARTLN 281
 
Name Accession Description Interval E-value
IspE COG1947
4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]; ...
6-284 5.59e-104

4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]; 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441550 [Multi-domain]  Cd Length: 281  Bit Score: 304.35  E-value: 5.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   6 VEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAE-GGIQCSCGEWS---GPENLAYRAAEAFLSGLGSS 81
Cdd:COG1947    2 LTVKAPAKINLFLHVTGRRPDGYHELETVFQFIDLGDTLTIEPADdGSISLTGPGAGvptDEDNLVYRAARLLQEATGIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  82 QGIHIDIEKNIPVQaglgggsadaaaalqalNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAP 161
Cdd:COG1947   82 PGVDIHLEKRIPVGaglgggssdaaatlralNRLWGLGLSREELAELAAKLGADVPFFLYGGTALAEGRGEKLTPLPPLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 162 KINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAEsLIPLLYNDLEPASMKLLPEIAWVKEELMKQnGC 241
Cdd:COG1947  162 ELWLVLVKPGVGVSTAEVYRALDLTRDTPPPDIDALLAALAAGDAA-LAALLRNDLEPVAFKLYPEIAEVLEALLEA-GA 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 122484148 242 LGALMSGSGSAVFGIVQTEEQAEKIAAIWRERnYHVWVTHTME 284
Cdd:COG1947  240 LAARMSGSGSTVFGLFEDEEAAEAAAAALPAR-GGVFVARTLN 281
ispE TIGR00154
4-diphosphocytidyl-2C-methyl-D-erythritol kinase; Members of this family of GHMP kinases were ...
10-287 2.15e-57

4-diphosphocytidyl-2C-methyl-D-erythritol kinase; Members of this family of GHMP kinases were previously designated as conserved hypothetical protein YchB or as isopentenyl monophosphate kinase. It is now known, in tomato and E. coli, to encode 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, an enzyme of the deoxyxylulose phosphate pathway of terpenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 188029 [Multi-domain]  Cd Length: 294  Bit Score: 186.18  E-value: 2.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   10 AYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTL-AEGGIQCSCGEWSGP--ENLAYRAA----EAFLSGLGSSQ 82
Cdd:TIGR00154   7 APAKINLFLYILGKRPDGYHELQMLMQFIDLGDKIIISVrSDDDIRLLKGDFDVPleENLAYRAAqllkNFANSKIKSLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   83 GIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAPK 162
Cdd:TIGR00154  87 GVNIEITKNIPMAAGLGGGSSDAAAVLVGLNQLWNLGLSLEELAELGATLGADVPFFVSGGTAFATGRGEIITPFEDPPE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  163 INLVLIKPDQGVNTAEAYRAFDQEGKfSHLDYAGWQEALASGRAESLIPLLYNDLEPASMKLLPEIAWVKEElMKQNGCL 242
Cdd:TIGR00154 167 KWVVIAKPHVSVSTPVVYQAYKLPRN-TPKRAKEWLKKISLECLQLLDSNGLNDLEKVALKRHTEVAQALNW-LLEYGLA 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 122484148  243 GALMSGSGSAVFGIVQTEEQAEKIAAIWRER----NYHVWVTHTMERGN 287
Cdd:TIGR00154 245 PERMSGSGPCVFALFDMESEAEQVLEQAPEWlngfVAKGYNVSPIGRAM 293
PRK14608 PRK14608
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
9-283 1.53e-50

4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional


Pssm-ID: 237765 [Multi-domain]  Cd Length: 290  Bit Score: 168.11  E-value: 1.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   9 FAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAE---------GGIQCScgewSGPENLAYRAAEAFLSGLG 79
Cdd:PRK14608  10 FAPAKINLALHVTGRRADGYHLLESLVAFADVGDRLTLEPAEalsltvsgpFAAGLG----DGDDNLVLRAARALRARVG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  80 -SSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLP 158
Cdd:PRK14608  86 pGLPPGAFHLEKNLPVAAGIGGGSADAAAALRLLARLWGLALDDERLAALALSLGADVPVCLDSRPLIMRGIGEELTPLP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 159 HAPKINLVLIKPDQGVNTAEAYRAFDqeGKFS---------HLDYAGWQEALASGRaeslipllyNDLEPASMKLLPEIA 229
Cdd:PRK14608 166 GLPSLPAVLVNPGVPVATPDVFRALG--LRDGpplpgapdpLASADALLAALAATR---------NDLEPPALALAPVIG 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 122484148 230 WVKEELMKQNGCLGALMSGSGSAVFGIVQTEEQAEKIAAIWRERNYHVWVTHTM 283
Cdd:PRK14608 235 EVLAALRAQPGALLARMSGSGATCFALFADEAAAEAAAAAIAAAHPGWWVKATR 288
GHMP_kinases_C pfam08544
GHMP kinases C terminal; This family includes homoserine kinases, galactokinases and ...
199-276 1.42e-07

GHMP kinases C terminal; This family includes homoserine kinases, galactokinases and mevalonate kinases.


Pssm-ID: 430063 [Multi-domain]  Cd Length: 85  Bit Score: 48.24  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  199 EALASGRAESLIPLLYN-----DLEPASMKLLPEIAWVKEELmKQNGcLGALMSGS--GSAVFGIVQTEEQAEKIAAIWR 271
Cdd:pfam08544   3 EALLRGDLEELGKLLTEsaeslEPLLVVGILPPELDELLEAL-LELG-LGAKLSGSggGPTVFALFKDEDDAEEVARALR 80

                  ....*
gi 122484148  272 ERNYH 276
Cdd:pfam08544  81 EAGKK 85
 
Name Accession Description Interval E-value
IspE COG1947
4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]; ...
6-284 5.59e-104

4-diphosphocytidyl-2C-methyl-D-erythritol kinase [Lipid transport and metabolism]; 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441550 [Multi-domain]  Cd Length: 281  Bit Score: 304.35  E-value: 5.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   6 VEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAE-GGIQCSCGEWS---GPENLAYRAAEAFLSGLGSS 81
Cdd:COG1947    2 LTVKAPAKINLFLHVTGRRPDGYHELETVFQFIDLGDTLTIEPADdGSISLTGPGAGvptDEDNLVYRAARLLQEATGIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  82 QGIHIDIEKNIPVQaglgggsadaaaalqalNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAP 161
Cdd:COG1947   82 PGVDIHLEKRIPVGaglgggssdaaatlralNRLWGLGLSREELAELAAKLGADVPFFLYGGTALAEGRGEKLTPLPPLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 162 KINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAEsLIPLLYNDLEPASMKLLPEIAWVKEELMKQnGC 241
Cdd:COG1947  162 ELWLVLVKPGVGVSTAEVYRALDLTRDTPPPDIDALLAALAAGDAA-LAALLRNDLEPVAFKLYPEIAEVLEALLEA-GA 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 122484148 242 LGALMSGSGSAVFGIVQTEEQAEKIAAIWRERnYHVWVTHTME 284
Cdd:COG1947  240 LAARMSGSGSTVFGLFEDEEAAEAAAAALPAR-GGVFVARTLN 281
ispE TIGR00154
4-diphosphocytidyl-2C-methyl-D-erythritol kinase; Members of this family of GHMP kinases were ...
10-287 2.15e-57

4-diphosphocytidyl-2C-methyl-D-erythritol kinase; Members of this family of GHMP kinases were previously designated as conserved hypothetical protein YchB or as isopentenyl monophosphate kinase. It is now known, in tomato and E. coli, to encode 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, an enzyme of the deoxyxylulose phosphate pathway of terpenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 188029 [Multi-domain]  Cd Length: 294  Bit Score: 186.18  E-value: 2.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   10 AYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTL-AEGGIQCSCGEWSGP--ENLAYRAA----EAFLSGLGSSQ 82
Cdd:TIGR00154   7 APAKINLFLYILGKRPDGYHELQMLMQFIDLGDKIIISVrSDDDIRLLKGDFDVPleENLAYRAAqllkNFANSKIKSLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   83 GIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAPK 162
Cdd:TIGR00154  87 GVNIEITKNIPMAAGLGGGSSDAAAVLVGLNQLWNLGLSLEELAELGATLGADVPFFVSGGTAFATGRGEIITPFEDPPE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  163 INLVLIKPDQGVNTAEAYRAFDQEGKfSHLDYAGWQEALASGRAESLIPLLYNDLEPASMKLLPEIAWVKEElMKQNGCL 242
Cdd:TIGR00154 167 KWVVIAKPHVSVSTPVVYQAYKLPRN-TPKRAKEWLKKISLECLQLLDSNGLNDLEKVALKRHTEVAQALNW-LLEYGLA 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 122484148  243 GALMSGSGSAVFGIVQTEEQAEKIAAIWRER----NYHVWVTHTMERGN 287
Cdd:TIGR00154 245 PERMSGSGPCVFALFDMESEAEQVLEQAPEWlngfVAKGYNVSPIGRAM 293
PRK14608 PRK14608
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
9-283 1.53e-50

4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional


Pssm-ID: 237765 [Multi-domain]  Cd Length: 290  Bit Score: 168.11  E-value: 1.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   9 FAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAE---------GGIQCScgewSGPENLAYRAAEAFLSGLG 79
Cdd:PRK14608  10 FAPAKINLALHVTGRRADGYHLLESLVAFADVGDRLTLEPAEalsltvsgpFAAGLG----DGDDNLVLRAARALRARVG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  80 -SSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLP 158
Cdd:PRK14608  86 pGLPPGAFHLEKNLPVAAGIGGGSADAAAALRLLARLWGLALDDERLAALALSLGADVPVCLDSRPLIMRGIGEELTPLP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 159 HAPKINLVLIKPDQGVNTAEAYRAFDqeGKFS---------HLDYAGWQEALASGRaeslipllyNDLEPASMKLLPEIA 229
Cdd:PRK14608 166 GLPSLPAVLVNPGVPVATPDVFRALG--LRDGpplpgapdpLASADALLAALAATR---------NDLEPPALALAPVIG 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 122484148 230 WVKEELMKQNGCLGALMSGSGSAVFGIVQTEEQAEKIAAIWRERNYHVWVTHTM 283
Cdd:PRK14608 235 EVLAALRAQPGALLARMSGSGATCFALFADEAAAEAAAAAIAAAHPGWWVKATR 288
PRK03188 PRK03188
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
6-268 2.44e-50

4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional


Pssm-ID: 235110 [Multi-domain]  Cd Length: 300  Bit Score: 167.76  E-value: 2.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   6 VEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAEG-GIQCScGEWS-----GPENLAYRAAEAFLSGLG 79
Cdd:PRK03188   1 VTVRAPAKVNLHLGVGPLRDDGYHELATVFQAVSLYDEVTVTAADVlSVEVS-GEGAdqvptDESNLAWRAAELLAEHVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  80 SSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPH 159
Cdd:PRK03188  80 RAPDVHLHIDKGIPVAGGMAGGSADAAAALVACDALWGLGLSRDELLELAAELGSDVPFALLGGTALGTGRGEQLAPVLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 160 APKINLVLIKPDQGVNTAEAYRAFDQ---EGKFSHLDYA-GWQEALASGRAESLIPLLYNDLEPASMKLLPEIAWVKeEL 235
Cdd:PRK03188 160 RGTFHWVLAFADGGLSTPAVFRELDRlreAGDPPRLGEPdPLLAALRAGDPAQLAPLLGNDLQAAALSLRPSLRRTL-RA 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 122484148 236 MKQNGCLGALMSGSGSAVFGIVQTEEQAEKIAA 268
Cdd:PRK03188 239 GEEAGALAGIVSGSGPTCAFLCADADSAVDVAA 271
PRK14611 PRK14611
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;
12-271 2.40e-41

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;


Pssm-ID: 184767 [Multi-domain]  Cd Length: 275  Bit Score: 144.13  E-value: 2.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  12 AKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAEG-GIQCSCGEWSGPENLAYRAAEAFLSGLGSSQGIHIDIEK 90
Cdd:PRK14611   8 AKVNLGLWILGKRPDGYHEIFTIYHTIDLYDRIYIKEHHTlEVKTSSPQIKEEENIVYKALRLFERYTGIDINYSIFIEK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  91 NIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAPKINLVLIKP 170
Cdd:PRK14611  88 NIPVGAGLGGGSSNAAVVLKYLNELLGNPLSEEELFELASSISADAPFFLKGGFALGRGIGDKLEFLEKPISREITLVYP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 171 DQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAESLIPLLYNDLEPASMKLLPEIawvkEELMKQNGCLG--ALMSG 248
Cdd:PRK14611 168 NIKSSTGRVYSKVTKQILTNKEDLNIIISLLREGEEKKIEEVIENTLGEIALELYPEI----KEVYRFLEYLGykPFVSG 243
                        250       260
                 ....*....|....*....|....*
gi 122484148 249 SGSAVFGIVQTEEQAEKIAAI--WR 271
Cdd:PRK14611 244 SGSSVYVFGKPSEEVKKAAAVrgWK 268
PRK14613 PRK14613
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;
8-266 2.19e-23

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;


Pssm-ID: 173077 [Multi-domain]  Cd Length: 297  Bit Score: 96.89  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   8 MFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAEGGI------------------QCS-CGEWSgpENLAY 68
Cdd:PRK14613   1 MISPAKINLGLEIPFKREDGFHEIRSVFLKISWGDDIEIEPAPNGVfelfstneiilekrklydQVSeRGDIK--QNILY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  69 RAAEAFLSGLGSSQGIHIDIEKNIPvqaGLGGGSADAAAALQALNKLF--KEPYTEEELKSFAAQLGADVAFCLKGGTQW 146
Cdd:PRK14613  79 KTFIKARSLFPELPGVKIHLTKRIS---PAGGLGGGSTNAASLLNFLFswRNFFTSDEMQVFAKEIGSDVPFFLGEGHAF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 147 ATGVGEELKGLPHAPKINLVLIKPdQGVNTAEAYRAFDQ--EGKFSHLDYAGWQEALAS----GRAESLIPLLYNDLEPA 220
Cdd:PRK14613 156 VTGKGEIMEEIEVHKGQGILALTP-QVMNTGEMYALLKKplQESASQKNGNTLSEDLISslkvGDWVSLQGRLENDFEPV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 122484148 221 SMKLLPEIAWVKEELMkQNGCLGALMSGSGSAVFGIVQTEEQAEKI 266
Cdd:PRK14613 235 AFQLHPELGVLKDKFL-EFGSSYCSLTGSGSSMYGLVQGLEIQEEL 279
ThrB COG0083
Homoserine kinase [Amino acid transport and metabolism]; Homoserine kinase is part of the ...
38-281 1.66e-20

Homoserine kinase [Amino acid transport and metabolism]; Homoserine kinase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 439853 [Multi-domain]  Cd Length: 302  Bit Score: 89.00  E-value: 1.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  38 IGIYDRIRVTLAEGG---IQCScGEWSG-----PENLAYRAAEAFLSGLGSS-QGIHIDIEKNIP--------------- 93
Cdd:COG0083   25 LSLYDEVEVERSDEPgleIEIE-GEGADelptdEDNLVYQAALALLEKLGKEpPGLRIEIEKGIPlgrglgssaaaivag 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  94 VqaglgggsadaaaalQALNKLFKEPYTEEELKSFAAQL-G-AD-VAFCLKGGTQWATGVGEELK--GLPHAPKINLVLI 168
Cdd:COG0083  104 L---------------VAANALLGLPLSKEELLELATEGeGhPDnVAPALLGGLVLSRSDGEPVRvvRLPVPPDLKAVVV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 169 KPDQGVNTAEAyRA-------FdQEGKF--SHLdyAGWQEALASGRAEsLIPLLYNDL--EPASMKLLPEIAWVKEELmK 237
Cdd:COG0083  169 IPDFELSTKEA-RAvlpkqvpL-KDAVFnsSRA--ALLVAALATGDYE-LLGRAMEDRlhEPYRAKLIPGFDEVKEAA-L 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 122484148 238 QNGCLGALMSGSGSAVFGIVqTEEQAEKIAAIWRER------NYHVWVTH 281
Cdd:COG0083  243 EAGALGAGISGAGPTVLALA-DDEEAEAVAEAMKAAfaeagiDARVYVLK 291
PRK01212 PRK01212
homoserine kinase; Provisional
37-275 2.41e-20

homoserine kinase; Provisional


Pssm-ID: 234920 [Multi-domain]  Cd Length: 301  Bit Score: 88.67  E-value: 2.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  37 SIGIYDRIRVTLAEGGIQCSC----GEWSG------PENLAYRAAEAFLSGLGSSQGIHIDIEKNIP------------- 93
Cdd:PRK01212  25 ALSLYDEVLVGDVVSVEAEFSieviGEGADklpldpEKNLVYQAALKFLEKLGKPPGLRIELEKNIPlgrglgssaasiv 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  94 ---VqaglgggsadaaaalqALNKLFKEPYTEEELKSFAAQLG--AD-VAFCLKGGTQWATGV-GEELKGLPHAPKINLV 166
Cdd:PRK01212 105 aglV----------------AANELAGLPLSKEELLQLATEGEghPDnVAPALLGGLVLALEEnGVISVKIPVFDDLKWV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 167 LIKPDQGVNTAEAYRAFDQegKFSHLDY-------AGWQEALASGRAEsLIPLLYNDL--EPASMKLLPEIAWVKEELmK 237
Cdd:PRK01212 169 VAIPNIELSTAEARAVLPK--QYSLKDAvfnssraALLVAALYTGDYE-LAGRAMKDVlhEPYRAKLIPGFAEVRQAA-L 244
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 122484148 238 QNGCLGALMSGSGSAVFGIVqTEEQAEKIAAiWRERNY 275
Cdd:PRK01212 245 EAGALGAGISGAGPTVFALC-DKEDAEKVAD-ALQKAF 280
thrB TIGR00191
homoserine kinase; Homoserine kinase is part of the threonine biosynthetic pathway.Homoserine ...
64-275 1.11e-16

homoserine kinase; Homoserine kinase is part of the threonine biosynthetic pathway.Homoserine kinase is a member of the GHMP kinases (Galactokinase, Homoserine kinase, Mevalonate kinase, Phosphomevalonate kinase) and shares with them an amino-terminal domain probably related to ATP binding.P.aeruginosa homoserine kinase seems not to be homologous (see PROSITE:PDOC0054) [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129295 [Multi-domain]  Cd Length: 302  Bit Score: 78.21  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   64 ENLAYRAAEAFLSGLG-SSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAA--QLGAD-VAFC 139
Cdd:TIGR00191  60 DNLIYQVAKRFLDQLGiRMPPVKVTLEKNIPLGRGLGSSAAAIVAALAAANELCGLPLSKERLLDYASelEGHPDnVAPA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  140 LKGGTQWATGVGEELKGL--PHAPKINLVLIKPDQGVNTAEA-------YRAFDQEGKFSHLdyAGWQEALASGRAEsLI 210
Cdd:TIGR00191 140 LLGGFQLAFVEDDKLEVLkiPIFSKLDWVLAIPNIEVSTAEAravlpkaYPRQDLVFNLSHL--AGLVHAIYQKKPD-LG 216
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122484148  211 PLLYNDL--EPASMKLLPEIAWVKEElMKQNGCLGALMSGSGSAVFGIVqTEEQAEKIAAIWRERNY 275
Cdd:TIGR00191 217 AIMMKDRihQPYRESLIPNLFKIKQA-ALEKGAYGITISGSGPTILAMA-DEEFAEQKEQDLLEVLH 281
PRK04181 PRK04181
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional
8-260 2.25e-15

4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Provisional


Pssm-ID: 235243  Cd Length: 257  Bit Score: 73.84  E-value: 2.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148   8 MFAYAKINLALAITGRRpDGYHELESVMQSI-GIYDRIRVTLAEGGIQCSCGEWSGP--ENLAYRAAEAfLSGLGSSQGI 84
Cdd:PRK04181   3 MKAYAKVNIFLKILGKR-GNYHELISRFVLVkDLFDEIEFVPKSAESFELIGNFDCPleENIIYKAYQE-LKNKGFSNEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  85 -------HIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKG-GTQWATGVGEELKG 156
Cdd:PRK04181  81 ieffkkkAIEVEKNIPTGAGLGGGSSDAATFLLMLNEILNLKLSLEELAEIGSKVGADVAFFISGyKSANVSGIGEIVEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 157 LPHAPkINLVLIKPDQGVNTAEAYRAFDQEG-KFSHLDYAG-WQ-----EALASGRAESLipllyNDL-EPAsMKLLPEI 228
Cdd:PRK04181 161 FEEEI-LNLEIFTPNIFCSTKAVYKAYREEFyDFISFNQAKeLLklsslELLKNFKNTEL-----NDLlAPA-LKLYPAL 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 122484148 229 awvKEELMKqngclGALMSGSGSAVFGIVQTE 260
Cdd:PRK04181 234 ---KDYLGE-----DWFFSGSGSSFFRVKRAQ 257
GHMP_kinases_C pfam08544
GHMP kinases C terminal; This family includes homoserine kinases, galactokinases and ...
199-276 1.42e-07

GHMP kinases C terminal; This family includes homoserine kinases, galactokinases and mevalonate kinases.


Pssm-ID: 430063 [Multi-domain]  Cd Length: 85  Bit Score: 48.24  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  199 EALASGRAESLIPLLYN-----DLEPASMKLLPEIAWVKEELmKQNGcLGALMSGS--GSAVFGIVQTEEQAEKIAAIWR 271
Cdd:pfam08544   3 EALLRGDLEELGKLLTEsaeslEPLLVVGILPPELDELLEAL-LELG-LGAKLSGSggGPTVFALFKDEDDAEEVARALR 80

                  ....*
gi 122484148  272 ERNYH 276
Cdd:pfam08544  81 EAGKK 85
PRK05905 PRK05905
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;
10-261 1.78e-07

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;


Pssm-ID: 235642  Cd Length: 258  Bit Score: 51.00  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  10 AYAKINLALAITGRRPD-GYHELESVMQSI-GIYDRIRVTLAEGGIQ-----CSCGEWSGPENLAYRAAEAFL-SGLGSS 81
Cdd:PRK05905   5 SYAKINLGLSIYKKCKKvTKHKLESIFILVeNVYDDIEIEKIEKNIDdihyfDETNEILVYSRLILVKTLEWLrDKYNIK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  82 QGIHIDIEKNIPVQAGLGGGSADAAAalqalnkLFKEPYTEEELKSF-----AAQLGADVAFCLKG-GTQWATGVGEELK 155
Cdd:PRK05905  85 NHFKIKIKKRIPIGSGLGSGSSNAAV-------LMKWILEFEGINEInykdvVNKLGSDIPFFLSGyKTAYISDYGSQVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 156 GLPHAPKINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALasgrAESLIPLLYNDLEPASMKLLPEIAWVKEEL 235
Cdd:PRK05905 158 DLIGQFKLTYKVIFMNVNVSTKKVFEKFDDNQHVIKNNFKTIIKNL----KENIVVNIHNDLQEPCFELYPNLLYKYNEL 233
                        250       260
                 ....*....|....*....|....*.
gi 122484148 236 MKQNgcLGALMSGSGSAVFGIVQTEE 261
Cdd:PRK05905 234 LNDG--FYTILSGAGSSFIVIKKINE 257
PLN02451 PLN02451
homoserine kinase
65-268 2.23e-04

homoserine kinase


Pssm-ID: 215248  Cd Length: 370  Bit Score: 42.09  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148  65 NLAYRAAEAFLSGLG-SSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEE-----LKSFAAQLG--AD- 135
Cdd:PLN02451 115 NCAGIAAIATMKLLGiRSVGLSLSLHKGLPLGSGLGSSAASAAAAAVAVNELFGSPLGKDDlvlagLESEAKVSGyhADn 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122484148 136 VAFCLKGGTQWATGVGE-ELKGLPHAPKINL--VLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQ-----EALASGRAE 207
Cdd:PLN02451 195 IAPALMGGFVLIRSYEPlHLIPLRFPSAKDLffVLVSPDFEAPTKKMRAALPKEIPMKHHVWNCSQaaalvAAILQGDAV 274
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122484148 208 SLIPLLYND--LEPASMKLLPEIAWVKEELMKQnGCLGALMSGSGSAVFGIVQTEEQAEKIAA 268
Cdd:PLN02451 275 LLGEALSSDkiVEPTRAPLIPGMEAVKKAALEA-GAYGCTISGAGPTAVAVIDDEEKGEEVGE 336
 
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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