|
Name |
Accession |
Description |
Interval |
E-value |
| LCB5 |
COG1597 |
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ... |
1-291 |
6.93e-95 |
|
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 441205 [Multi-domain] Cd Length: 295 Bit Score: 283.67 E-value: 6.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKKAIFIINLISGTSDKAAIPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVH 80
Cdd:COG1597 1 AMMRALLIVNPASGRGRAARLLERLVAALRAAGLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 81 SNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDAFISLKFAEAGKR--GPLTY 158
Cdd:COG1597 81 TGPPLGILPLGTGNDFARALGIPLDPEAALEALLTGRTRRIDLGRVNGRYFLNVAGIGFDAEVVERANRALKRrlGKLAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 159 IENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIMEPFGLIDAPQISIEMFNK 238
Cdd:COG1597 161 VLAALRALLRYRPFRLRIELDGEEIEGEALLVAVGNGPYYGGGLRLAPDASLDDGLLDVVVVRPLSRLRLLRLLPRLLRG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495178532 239 TLDkNNSKIKTFRCKKLCVHRHSPGAIHYDGDPVMTGADIDVELKPKGIKIVV 291
Cdd:COG1597 241 RHL-RHPGVRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLV 292
|
|
| PRK00861 |
PRK00861 |
putative lipid kinase; Reviewed |
1-296 |
4.22e-38 |
|
putative lipid kinase; Reviewed
Pssm-ID: 234850 [Multi-domain] Cd Length: 300 Bit Score: 137.83 E-value: 4.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKKAIFIINLISGTSDKAAIPELIEQLLDkEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVH 80
Cdd:PRK00861 1 MTRSACLIFNPVAGQGNPEVDLALIRAILE-PEMDLDIYLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 81 SNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDA-FISLKFAEAGKR-GPLTY 158
Cdd:PRK00861 80 TDIPLGIIPRGTANAFAAALGIPDTIEEACRTILQGKTRRVDVAYCNGQPMILLAGIGFEAeTVEEADREAKNRfGILAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 159 IENVLREGLKYEPETYTVMADDETSLHKAFLISCANAsqygnnayiAPQASM----------SDGLMDVIIMEPFGLIDA 228
Cdd:PRK00861 160 ILSGLQQLRELESFEVEIETEDQIITTNAVAVTVANA---------APPTSVlaqgpgavipDDGLLDVTIVAPKNLAEA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495178532 229 PQISIEMFNKTLDKNNSK---IKTFRCKKLCVHRHSPGAIHYDGDpVMTGADIDVELKPKGIKIVVNSQAD 296
Cdd:PRK00861 231 VAASYHLLQTALQGNPAErddIGYLRAKQVKITTDPPQKVVIDGE-VVGTTPIEIECLPRSLKVFAPLQAE 300
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
4-124 |
2.89e-36 |
|
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.
Pssm-ID: 425868 [Multi-domain] Cd Length: 125 Bit Score: 127.32 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 4 KAIFIINLISGTSDKAAIPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHSNT 83
Cdd:pfam00781 1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVEVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLAT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495178532 84 --ALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYG 124
Cdd:pfam00781 81 rpPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVG 123
|
|
| TIGR00147 |
TIGR00147 |
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ... |
3-291 |
3.08e-33 |
|
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 161732 [Multi-domain] Cd Length: 293 Bit Score: 124.54 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 3 KKAIFIINLISGTS-DKAAIPELIeQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAI--V 79
Cdd:TIGR00147 2 AEAPAILNPTAGKSnDNKPLREVI-MLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNALiqL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 80 HSNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIING-YPFFCTCGMGFDAFISLKFAEAGKR--GPL 156
Cdd:TIGR00147 81 DDIPALGILPLGTANDFARSLGIPEDLDKAAKLVIAGDARAIDMGQVNKqYCFINMAGGGFGTEITTETPEKLKAalGSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 157 TYIENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIMEPFGLIDApQISIEMF 236
Cdd:TIGR00147 161 SYILSGLMRMDTLQPFRCEIRGEGEHWQGEAVVFLVGNGRQAGGGQKLAPDASINDGLLDLRIFTNDNLLPA-LVLTLMS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 495178532 237 NKTLDKNNSKIKTFRCKKLCVHRHSPGAIHYDGDPvMTGADIDVELKPKGIKIVV 291
Cdd:TIGR00147 240 DEGKHTDNPNIIYGKASRIDIQTPHKITFNLDGEP-LGGTPFHIEILPAHLRCRL 293
|
|
| DAGKc |
smart00046 |
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ... |
6-114 |
2.64e-12 |
|
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.
Pssm-ID: 214487 [Multi-domain] Cd Length: 124 Bit Score: 63.08 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 6 IFIINLISGTSDkaaiPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHSN--- 82
Cdd:smart00046 1 LVFVNPKSGGGK----GEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRElpl 76
|
90 100 110
....*....|....*....|....*....|....
gi 495178532 83 --TALGIIPCGSGNGLARHLQLPINVKKSIEILN 114
Cdd:smart00046 77 pePPVAVLPLGTGNDLARSLGWGGGYDGEKLLKT 110
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
11-78 |
5.15e-03 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 38.29 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495178532 11 LISG-TSDKAAIPELIEQLlDKEKFEYEIAItqYAGHASE-----IASKAKDANVDLVVAVGGdGTVNEVARAI 78
Cdd:cd08550 27 IIGGkTALEAVGEKLEKSL-EEAGIDYEVEV--FGGECTEenierLAEKAKEEGADVIIGIGG-GKVLDTAKAV 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LCB5 |
COG1597 |
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ... |
1-291 |
6.93e-95 |
|
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 441205 [Multi-domain] Cd Length: 295 Bit Score: 283.67 E-value: 6.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKKAIFIINLISGTSDKAAIPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVH 80
Cdd:COG1597 1 AMMRALLIVNPASGRGRAARLLERLVAALRAAGLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 81 SNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDAFISLKFAEAGKR--GPLTY 158
Cdd:COG1597 81 TGPPLGILPLGTGNDFARALGIPLDPEAALEALLTGRTRRIDLGRVNGRYFLNVAGIGFDAEVVERANRALKRrlGKLAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 159 IENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIMEPFGLIDAPQISIEMFNK 238
Cdd:COG1597 161 VLAALRALLRYRPFRLRIELDGEEIEGEALLVAVGNGPYYGGGLRLAPDASLDDGLLDVVVVRPLSRLRLLRLLPRLLRG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495178532 239 TLDkNNSKIKTFRCKKLCVHRHSPGAIHYDGDPVMTGADIDVELKPKGIKIVV 291
Cdd:COG1597 241 RHL-RHPGVRYFRAREVEIESDRPLPVQLDGEPLGLATPLEFEVLPGALRVLV 292
|
|
| PRK00861 |
PRK00861 |
putative lipid kinase; Reviewed |
1-296 |
4.22e-38 |
|
putative lipid kinase; Reviewed
Pssm-ID: 234850 [Multi-domain] Cd Length: 300 Bit Score: 137.83 E-value: 4.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKKAIFIINLISGTSDKAAIPELIEQLLDkEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVH 80
Cdd:PRK00861 1 MTRSACLIFNPVAGQGNPEVDLALIRAILE-PEMDLDIYLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 81 SNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDA-FISLKFAEAGKR-GPLTY 158
Cdd:PRK00861 80 TDIPLGIIPRGTANAFAAALGIPDTIEEACRTILQGKTRRVDVAYCNGQPMILLAGIGFEAeTVEEADREAKNRfGILAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 159 IENVLREGLKYEPETYTVMADDETSLHKAFLISCANAsqygnnayiAPQASM----------SDGLMDVIIMEPFGLIDA 228
Cdd:PRK00861 160 ILSGLQQLRELESFEVEIETEDQIITTNAVAVTVANA---------APPTSVlaqgpgavipDDGLLDVTIVAPKNLAEA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495178532 229 PQISIEMFNKTLDKNNSK---IKTFRCKKLCVHRHSPGAIHYDGDpVMTGADIDVELKPKGIKIVVNSQAD 296
Cdd:PRK00861 231 VAASYHLLQTALQGNPAErddIGYLRAKQVKITTDPPQKVVIDGE-VVGTTPIEIECLPRSLKVFAPLQAE 300
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
4-124 |
2.89e-36 |
|
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.
Pssm-ID: 425868 [Multi-domain] Cd Length: 125 Bit Score: 127.32 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 4 KAIFIINLISGTSDKAAIPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHSNT 83
Cdd:pfam00781 1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVEVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLAT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495178532 84 --ALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYG 124
Cdd:pfam00781 81 rpPLGIIPLGTGNDFARALGIPGDPEEALEAILKGQTRPVDVG 123
|
|
| TIGR00147 |
TIGR00147 |
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ... |
3-291 |
3.08e-33 |
|
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 161732 [Multi-domain] Cd Length: 293 Bit Score: 124.54 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 3 KKAIFIINLISGTS-DKAAIPELIeQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAI--V 79
Cdd:TIGR00147 2 AEAPAILNPTAGKSnDNKPLREVI-MLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNALiqL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 80 HSNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIING-YPFFCTCGMGFDAFISLKFAEAGKR--GPL 156
Cdd:TIGR00147 81 DDIPALGILPLGTANDFARSLGIPEDLDKAAKLVIAGDARAIDMGQVNKqYCFINMAGGGFGTEITTETPEKLKAalGSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 157 TYIENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIMEPFGLIDApQISIEMF 236
Cdd:TIGR00147 161 SYILSGLMRMDTLQPFRCEIRGEGEHWQGEAVVFLVGNGRQAGGGQKLAPDASINDGLLDLRIFTNDNLLPA-LVLTLMS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 495178532 237 NKTLDKNNSKIKTFRCKKLCVHRHSPGAIHYDGDPvMTGADIDVELKPKGIKIVV 291
Cdd:TIGR00147 240 DEGKHTDNPNIIYGKASRIDIQTPHKITFNLDGEP-LGGTPFHIEILPAHLRCRL 293
|
|
| PRK12361 |
PRK12361 |
hypothetical protein; Provisional |
2-296 |
9.01e-29 |
|
hypothetical protein; Provisional
Pssm-ID: 183473 [Multi-domain] Cd Length: 547 Bit Score: 116.26 E-value: 9.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 2 KKKAIFIINLISGTSDKAAIPELIEQLLdKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHS 81
Cdd:PRK12361 242 HKRAWLIANPVSGGGKWQEYGEQIQREL-KAYFDLTVKLTTPEISAEALAKQARKAGADIVIACGGDGTVTEVASELVNT 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 82 NTALGIIPCGSGNGLARHL----QLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDAfislKFAEAGKR---- 153
Cdd:PRK12361 321 DITLGIIPLGTANALSHALfglgSKLIPVEQACDNIIQGHTQRIDTARCNDRLMLLLVGIGFEQ----KMIESADRerkn 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 154 --GPLTYIENVLREGLKYEPETYTVMADDETSLH---KAFLIscANASQY------GNNayiAPQasMSDGLMDVIIMEP 222
Cdd:PRK12361 397 alGQLAYLDGLWRAVNENETLTLTVTLDDAEPQTistHSLVV--ANAAPFtsllaqGGG---EPN--MTDGLLDITWLDS 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495178532 223 FGLIDAPQISI-EMFNKTLDKN--NSKIKTFRCKKlcVHRHSPGAIHY--DGDpVMTGADIDVELKPKGIKIVVNSQAD 296
Cdd:PRK12361 470 GGEPGEQLLSLaELALSGLGKEpeANKVHHAHAKK--VTISSQKPIKYviDGE-LFEDEDLTIEVQPASLKVFVPYQEI 545
|
|
| PRK13057 |
PRK13057 |
lipid kinase; |
23-221 |
1.19e-23 |
|
lipid kinase;
Pssm-ID: 183857 [Multi-domain] Cd Length: 287 Bit Score: 98.45 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 23 ELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDAnVDLVVAVGGDGTVNEVARAIVHSNTALGIIPCGSGNGLARHLQL 102
Cdd:PRK13057 16 AAARAALEAAGLELVEPPAEDPDDLSEVIEAYADG-VDLVIVGGGDGTLNAAAPALVETGLPLGILPLGTANDLARTLGI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 103 PINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDAFISLKF-AEAGKR-GPLTYIENVLREGLKYEPETYTVMADD 180
Cdd:PRK13057 95 PLDLEAAARVIATGQVRRIDLGWVNGHYFFNVASLGLSAELARRLtKELKRRwGTLGYAIAALRVLRRSRPFTAEIEHDG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495178532 181 ETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIME 221
Cdd:PRK13057 175 RTERVKTLQVAVGNGRYYGGGMTVAHDATIDDGRLDLYSLE 215
|
|
| PRK13059 |
PRK13059 |
putative lipid kinase; Reviewed |
3-291 |
4.69e-21 |
|
putative lipid kinase; Reviewed
Pssm-ID: 183858 Cd Length: 295 Bit Score: 91.64 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 3 KKAIFIINLISGTSdkaAIPELIEQLLDKEKfEYEIAITQY---AGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIV 79
Cdd:PRK13059 2 KKVKFIYNPYSGEN---AIISELDKVIRIHQ-EKGYLVVPYrisLEYDLKNAFKDIDESYKYILIAGGDGTVDNVVNAMK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 80 HSNTAL--GIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMGFDAFISLKFAEAGKR--GP 155
Cdd:PRK13059 78 KLNIDLpiGILPVGTANDFAKFLGMPTDIGEACEQILKSKPKKVDLGKINDKYFINVASTGLFTDVSQKTDVNLKNtiGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 156 LTYIENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGN--NAYiapQASMSDGLMDVIIMEPFGLIDAPQISI 233
Cdd:PRK13059 158 LAYYLKGLEELPNFRKLKVKVTSEEVNFDGDMYLMLVFNGQTAGNfnLAY---KAEVDDGLLDVIIIKACPIIDLIPLFI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 234 EMFNKTLDKNNSKIKTFRCKKLCVHRHSPGAIHYDGDpvmTGAD--IDVELKPKGIKIVV 291
Cdd:PRK13059 235 KVLKGEHLEDVNGLIYFKTDKLEIESNEEIVTDIDGE---RGPDfpLNIECIKGGLKVLG 291
|
|
| PRK13054 |
PRK13054 |
lipid kinase; Reviewed |
1-290 |
3.27e-20 |
|
lipid kinase; Reviewed
Pssm-ID: 237281 [Multi-domain] Cd Length: 300 Bit Score: 89.16 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKKAIFIINlisgtSDKAAIPELIE--QLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAI 78
Cdd:PRK13054 2 TFPKSLLILN-----GKSAGNEELREavGLLREEGHTLHVRVTWEKGDAARYVEEALALGVATVIAGGGDGTINEVATAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 79 VH----SNTALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTcgM---GFDAFISLKFAEAG 151
Cdd:PRK13054 77 AQlegdARPALGILPLGTANDFATAAGIPLEPDKALKLAIEGRAQPIDLARVNDRTYFIN--MatgGFGTRVTTETPEKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 152 KR--GPLTYIENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIMEPFGlIDAP 229
Cdd:PRK13054 155 KAalGGVAYLIHGLMRMDTLKPDRCEIRGPDFHWQGDALVIGIGNGRQAGGGQQLCPEALINDGLLDLRILPAPQ-ELLP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495178532 230 QISIEMFNKTLDKNNskIKTFRCKKLCVHRHSPGAIHYDGDPVmTGADIDVELKPKGIKIV 290
Cdd:PRK13054 234 TLLSTLTGGSEDNPN--IIRARLPWLEIQAPHELTFNLDGEPL-SGRHFRIEVLPAALRCR 291
|
|
| PRK13337 |
PRK13337 |
putative lipid kinase; Reviewed |
3-221 |
3.29e-17 |
|
putative lipid kinase; Reviewed
Pssm-ID: 183982 [Multi-domain] Cd Length: 304 Bit Score: 80.86 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 3 KKAIFIINLISGTSD-KAAIPELIEQLldkEKFEYEIAI--TQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIV 79
Cdd:PRK13337 2 KRARIIYNPTSGRELfKKNLPDVLQKL---EQAGYETSAhaTTGPGDATLAAERAVERKFDLVIAAGGDGTLNEVVNGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 80 -HSN-TALGIIPCGSGNGLARHLQLPINVKKSIEILNTFEVRDLDYGIINGYPFFCTCGMG------FDAFISLKFAeag 151
Cdd:PRK13337 79 eKENrPKLGIIPVGTTNDFARALHVPRDIEKAADVIIEGHTVPVDIGKANNRYFINIAGGGrlteltYEVPSKLKTM--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495178532 152 kRGPLTYienvLREGLKYEPETYTV---------MADDETSLhkaFLISCANAsqYGNNAYIAPQASMSDGLMDVIIME 221
Cdd:PRK13337 156 -LGQLAY----YLKGIEMLPSLKATdvrieydgkLFQGEIML---FLLGLTNS--VGGFEKLAPDASLDDGYFDLIIVK 224
|
|
| PRK11914 |
PRK11914 |
diacylglycerol kinase; Reviewed |
44-295 |
3.41e-17 |
|
diacylglycerol kinase; Reviewed
Pssm-ID: 237021 [Multi-domain] Cd Length: 306 Bit Score: 80.99 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 44 AGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHSNTALGIIPCGSGNGLARHLQLPI-NVKKSIEILNTFEVRDLD 122
Cdd:PRK11914 50 AHDARHLVAAALAKGTDALVVVGGDGVISNALQVLAGTDIPLGIIPAGTGNDHAREFGIPTgDPEAAADVIVDGWTETVD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 123 YGIINGYP-----FFCTCGMGFDAFISlkfaEAGKR-----GPLTYIENVLREGLKYEPETYTVMADD-ETSLHKAFLIS 191
Cdd:PRK11914 130 LGRIQDDDgivkwFGTVAATGFDSLVT----DRANRmrwphGRMRYNLAMLAELSKLRPLPFRLVLDGtEEIVTDLTLAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 192 CANASQYGNNAYIAPQASMSDGLMDVIIMEpfgliDAPQISIEMFNKTLDK----NNSKIKTFRCKKlcVHRHSPGAIHY 267
Cdd:PRK11914 206 FGNTRSYGGGMLICPNADHTDGLLDITMVQ-----SASRTRLLRLFPTVFKgthvELDEVSTARAKT--VHVECPGINAY 278
|
250 260
....*....|....*....|....*....
gi 495178532 268 -DGDPVMTgADIDVELKPKGIKIVVNSQA 295
Cdd:PRK11914 279 aDGDFACP-LPAEISAVPGALQILRPRPG 306
|
|
| PRK13055 |
PRK13055 |
putative lipid kinase; Reviewed |
1-323 |
3.07e-16 |
|
putative lipid kinase; Reviewed
Pssm-ID: 237282 [Multi-domain] Cd Length: 334 Bit Score: 78.49 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKKAIFIINLISGtsdKAAIPELIEQLLDK-EKFEYE---IAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVAR 76
Cdd:PRK13055 1 MQKRARLIYNPTSG---QEIMKKNVADILDIlEQAGYEtsaFQTTPEPNSAKNEAKRAAEAGFDLIIAAGGDGTINEVVN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 77 AI--VHSNTALGIIPCGSGNGLARHLQLP-INVKKSIEILNTFEVRDLDYGIINGYPFFctcgmgfdafisLKFAEAGKR 153
Cdd:PRK13055 78 GIapLEKRPKMAIIPAGTTNDYARALKIPrDNPVEAAKVILKNQTIKMDIGRANEDKYF------------INIAAGGSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 154 GPLTYI--ENV---------LREGLKYEPETYTVMA----DDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVI 218
Cdd:PRK13055 146 TELTYSvpSQLksmfgylayLAKGAELLPRVSPVPVrityDEGVFEGKISMFFLALTNSVGGFEQIVPDAKLDDGKFTLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 219 IMEPFGLIDAPQISIEMFNKTLDKNNSKIKTFRCKKLCVHRHSPGA--IHYDGDpvmTGADIDVELK--PKGIKIVVNSQ 294
Cdd:PRK13055 226 IVKTANLFELLHLMALILNGGKHIDDPRVIYIKTSKLTIEPLGDDRlmVNLDGE---YGGDAPMTFEnlKQHIEFFANTD 302
|
330 340 350
....*....|....*....|....*....|.
gi 495178532 295 A--DRNLRKPNALQNAATELFNEINIIREEI 323
Cdd:PRK13055 303 EisDDALTDELEIEEIAKKFAEEVEDLEQED 333
|
|
| YegS_C |
pfam19279 |
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ... |
153-222 |
1.08e-12 |
|
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal domain found in the YegS protein. It is related to the beta sandwich domain of NAD kinases. The structure of YegS reveals a two-domain protein with the active site crevice found between the two domains. The C-terminal domain contains 13 beta-strands and two alpha-helices. The likely substrate for YegS is phosphatidylglycerol.
Pssm-ID: 437111 Cd Length: 158 Bit Score: 64.91 E-value: 1.08e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 153 RGPLTYIENVLREGLKYEPETYTVMADDETSLHKAFLISCANASQYGNNAYIAPQASMSDGLMDVIIMEP 222
Cdd:pfam19279 22 PGALSYPAAALRALATFRPLRYRVTVDGEVREFSAALVAVANSGYYGGGMRIAPDARVDDGLLDVVVIEA 91
|
|
| DAGKc |
smart00046 |
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ... |
6-114 |
2.64e-12 |
|
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.
Pssm-ID: 214487 [Multi-domain] Cd Length: 124 Bit Score: 63.08 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 6 IFIINLISGTSDkaaiPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHSN--- 82
Cdd:smart00046 1 LVFVNPKSGGGK----GEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRElpl 76
|
90 100 110
....*....|....*....|....*....|....
gi 495178532 83 --TALGIIPCGSGNGLARHLQLPINVKKSIEILN 114
Cdd:smart00046 77 pePPVAVLPLGTGNDLARSLGWGGGYDGEKLLKT 110
|
|
| PLN02958 |
PLN02958 |
diacylglycerol kinase/D-erythro-sphingosine kinase |
3-100 |
1.91e-05 |
|
diacylglycerol kinase/D-erythro-sphingosine kinase
Pssm-ID: 215517 [Multi-domain] Cd Length: 481 Bit Score: 46.01 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 3 KKAIFIINLISGTSDKAAI-PELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANVDLVVAVGGDGTVNEVARAIVHS 81
Cdd:PLN02958 112 KRLLVFVNPFGGKKSASKIfFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSKYDGIVCVSGDGILVEVVNGLLER 191
|
90 100
....*....|....*....|....*.
gi 495178532 82 ---NTA----LGIIPCGSGNGLARHL 100
Cdd:PLN02958 192 edwKTAiklpIGMVPAGTGNGMAKSL 217
|
|
| NadK |
COG0061 |
NAD kinase [Coenzyme transport and metabolism]; |
1-87 |
8.34e-05 |
|
NAD kinase [Coenzyme transport and metabolism];
Pssm-ID: 439831 [Multi-domain] Cd Length: 279 Bit Score: 43.59 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 1 MKKkaifiINLISGTSDKAAIP--ELIEQLLDKEKFEYEIAiTQYAGHASEIASKAKDAnvDLVVAVGGDGTVNEVARAI 78
Cdd:COG0061 1 MKR-----IAIVAKPGKPEALEaaEELAELLEERGIEVVLD-EDTAVPGVPLEELGEEA--DLVIVLGGDGTLLRAARLL 72
|
90
....*....|
gi 495178532 79 VHSNTA-LGI 87
Cdd:COG0061 73 APLGIPiLGI 82
|
|
| COG3199 |
COG3199 |
NAD kinase [Nucleotide transport and metabolism]; |
26-87 |
1.34e-04 |
|
NAD kinase [Nucleotide transport and metabolism];
Pssm-ID: 442432 [Multi-domain] Cd Length: 367 Bit Score: 43.33 E-value: 1.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495178532 26 EQLLDKEKFEYEIAITQYAGHAS-----EIASKAKDANVDLVVAVGGDGTVNEVARAIVHSNTALGI 87
Cdd:COG3199 68 EDVLRELGFEVEVLYDMPPVTTTaedtrRAARAMLEAGVDLIVFLGGDGTARDVAKAVGDSVPVLGI 134
|
|
| PLN02204 |
PLN02204 |
diacylglycerol kinase |
3-81 |
2.98e-04 |
|
diacylglycerol kinase
Pssm-ID: 215126 [Multi-domain] Cd Length: 601 Bit Score: 42.56 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 3 KKAIFIINLISGTSDKAAIPELIEQLLDKEKFEYEIAITQYAGHASEIASKAKDANV---DLVVAVGGDGTVNEVARAIV 79
Cdd:PLN02204 160 KNLLVFVHPLSGKGSGSRTWETVSPIFIRAKVKTKVIVTERAGHAFDVMASISNKELksyDGVIAVGGDGFFNEILNGYL 239
|
..
gi 495178532 80 HS 81
Cdd:PLN02204 240 LS 241
|
|
| ppnK |
PRK01231 |
NAD(+) kinase; |
9-87 |
4.27e-04 |
|
NAD(+) kinase;
Pssm-ID: 179257 [Multi-domain] Cd Length: 295 Bit Score: 41.48 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178532 9 INLIsGTSDKAAIPELIEQLLDKEK-------FEYEIAITqYAGHASEIASKAKDANV-DLVVAVGGDGTVNEVARAIVH 80
Cdd:PRK01231 7 IGLI-GRLGSSSVVETLRRLKDFLLdrgleviLDEETAEV-LPGHGLQTVSRKLLGEVcDLVIVVGGDGSLLGAARALAR 84
|
....*...
gi 495178532 81 SNTA-LGI 87
Cdd:PRK01231 85 HNVPvLGI 92
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
11-78 |
5.15e-03 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 38.29 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495178532 11 LISG-TSDKAAIPELIEQLlDKEKFEYEIAItqYAGHASE-----IASKAKDANVDLVVAVGGdGTVNEVARAI 78
Cdd:cd08550 27 IIGGkTALEAVGEKLEKSL-EEAGIDYEVEV--FGGECTEenierLAEKAKEEGADVIIGIGG-GKVLDTAKAV 96
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
18-78 |
6.01e-03 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 38.20 E-value: 6.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495178532 18 KAAIPELIEQLLDKEKFEYEIaITQYAGHAS-----EIASKAKDANVDLVVAVGGdGTVNEVARAI 78
Cdd:cd08551 36 KAGLLDKVLESLKAAGIEVEV-FDDVEPNPTvetveAAAELAREEGADLVIAVGG-GSVLDTAKAI 99
|
|
| |
