|
Name |
Accession |
Description |
Interval |
E-value |
| LCB5 |
COG1597 |
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ... |
213-493 |
3.82e-59 |
|
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 441205 [Multi-domain] Cd Length: 295 Bit Score: 197.00 E-value: 3.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 213 VTLVVNPRSGGGRAGEVAEQVRTALPA----VTVVELGPDDDVAEAVRRAADS-AEVLAIAGGDGSVAAAAGVAVERDLP 287
Cdd:COG1597 5 ALLIVNPASGRGRAARLLERLVAALRAagleVEVLETESPGDATELAREAAAEgADLVVAAGGDGTVNEVANGLAGTGPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 288 LAVFPGGTLNHFAKDIGCDTT-AKTVRAIAEGSLSRVDVVQFNDEtTVVNTASVGAYPAFVRRRERLQHKVGKPVASVYA 366
Cdd:COG1597 85 LGILPLGTGNDFARALGIPLDpEAALEALLTGRTRRIDLGRVNGR-YFLNVAGIGFDAEVVERANRALKRRLGKLAYVLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 367 MLMTLRREQP--VRITYDDKTLQ--TSLFFLGNSAYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRLQ 442
Cdd:COG1597 164 ALRALLRYRPfrLRIELDGEEIEgeALLVAVGNGPYYGGGLRLAPDASLDDGLLDVVVVRPLSRLRLLRLLPRLLRGRHL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1038032569 443 RSRLYHELQVPQFRFTApDGPVPLARDGEVDSPCAEAEFTVRYRALQVFRP 493
Cdd:COG1597 244 RHPGVRYFRAREVEIES-DRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
|
|
| PRK13057 |
PRK13057 |
lipid kinase; |
215-496 |
2.09e-25 |
|
lipid kinase;
Pssm-ID: 183857 [Multi-domain] Cd Length: 287 Bit Score: 105.77 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 215 LVVNPRSGGGRAGevAEQVRTALPA--VTVVELGPDD--DVAEAVRRAADSAEVLAIAGGDGSVAAAAGVAVERDLPLAV 290
Cdd:PRK13057 2 LLVNRHARSGRAA--LAAARAALEAagLELVEPPAEDpdDLSEVIEAYADGVDLVIVGGGDGTLNAAAPALVETGLPLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 291 FPGGTLNHFAKDIGC-DTTAKTVRAIAEGSLSRVDVVQFNDEtTVVNTASVGAYPAFVRR-RERLQHKVGKpVASVYAML 368
Cdd:PRK13057 80 LPLGTANDLARTLGIpLDLEAAARVIATGQVRRIDLGWVNGH-YFFNVASLGLSAELARRlTKELKRRWGT-LGYAIAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 369 MTLRREQP--VRITYDD-----KTLQTSlffLGNSAYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRL 441
Cdd:PRK13057 158 RVLRRSRPftAEIEHDGrtervKTLQVA---VGNGRYYGGGMTVAHDATIDDGRLDLYSLEVAHWWRLLALLPALRRGRH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1038032569 442 QRSRLYHELQVPQFRFTApDGPVPLARDGEV--DSPcaeAEFTVRYRALQVFRPMPP 496
Cdd:PRK13057 235 GEWPDVRAFRTTELELRT-RKPRPINTDGELttYTP---AHFRVLPKALRVLAPPPA 287
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
28-186 |
1.09e-19 |
|
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 440435 [Multi-domain] Cd Length: 189 Bit Score: 87.02 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 28 AIAHSPSRLLDTTMPPLTRAADYSKLWLALAAVMAATGRASAQRAAARGVVSLALTSLVTNQVVKRIRPRARPDilQVPL 107
Cdd:COG0671 29 LLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF--VVPD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 108 LRRARRLPLSNSLPSGHSASAAAFATGVGLESP--LLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVVGAKL 185
Cdd:COG0671 107 LELLLGTAGGYSFPSGHAAAAFALALVLALLLPrrWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
|
.
gi 1038032569 186 V 186
Cdd:COG0671 187 L 187
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
77-181 |
4.83e-19 |
|
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.
Pssm-ID: 238813 [Multi-domain] Cd Length: 122 Bit Score: 82.89 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 77 VVSLALTSLVTNQVVKRIRPRARPD--ILQVPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP------LLGLPIAG 148
Cdd:cd01610 8 LLLALLAGLLLTGVLKYLFGRPRPYflLRCGPDGDPLLLTEGGYSFPSGHAAFAFALALFLALLLPrrllrlLLGLLLLL 87
|
90 100 110
....*....|....*....|....*....|...
gi 1038032569 149 LAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd01610 88 LALLVGLSRVYLGVHYPSDVLAGALLGILVALL 120
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
213-327 |
1.25e-15 |
|
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: 73.39 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 213 VTLVVNPRSGGGRAGEVAEQVRTALPA----VTVVELGPDDDVAEAVRRAA-DSAEVLAIAGGDG--SVAAAAGVAVERD 285
Cdd:pfam00781 2 LLVIVNPKSGGGKGKKLLRKVRPLLNKagveVELVLTEGPGDALELAREAAeDGYDRIVVAGGDGtvNEVLNGLAGLATR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1038032569 286 LPLAVFPGGTLNHFAKDIGCDTTAKT-VRAIAEGSLSRVDVVQ 327
Cdd:pfam00781 82 PPLGIIPLGTGNDFARALGIPGDPEEaLEAILKGQTRPVDVGK 124
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
78-181 |
3.77e-14 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 68.91 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 78 VSLALTSLVTNQVVKRIRPRARPDILQVPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP------LLGLPIAGLAG 151
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLParagrkLLIFLLLLLAL 84
|
90 100 110
....*....|....*....|....*....|
gi 1038032569 152 LVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:smart00014 85 VVGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
77-181 |
1.83e-13 |
|
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.
Pssm-ID: 426329 [Multi-domain] Cd Length: 124 Bit Score: 67.06 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 77 VVSLALTSLVTN---QVVKRIRPRARPDILQvPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP--------LLGLP 145
Cdd:pfam01569 3 LLALALAGLLSSvlkDYFGRPRPFFLLLEGG-LVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRrlrkivrvLLALL 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 1038032569 146 IAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:pfam01569 82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALL 117
|
|
| TIGR00147 |
TIGR00147 |
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ... |
250-490 |
1.09e-12 |
|
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: 68.68 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 250 DVAEAVRRAAD-SAEVLAIAGGDGS--VAAAAGVAVERDLPLAVFPGGTLNHFAKDIGC-DTTAKTVRAIAEGSLSRVDV 325
Cdd:TIGR00147 45 DAARYVEEARKfGVDTVIAGGGDGTinEVVNALIQLDDIPALGILPLGTANDFARSLGIpEDLDKAAKLVIAGDARAIDM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 326 VQFNDETTVVNTASVGaypaFVRRR-----ERLQHKVGKpVASVYAMLMTLRREQPVR--ITYDDKTLQTS--LFFLGNS 396
Cdd:TIGR00147 125 GQVNKQYCFINMAGGG----FGTEIttetpEKLKAALGS-LSYILSGLMRMDTLQPFRceIRGEGEHWQGEavVFLVGNG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 397 AYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRLQRSRLYHELQVPQFRFTAPDGpVPLARDGEVDSpC 476
Cdd:TIGR00147 200 RQAGGGQKLAPDASINDGLLDLRIFTNDNLLPALVLTLMSDEGKHTDNPNIIYGKASRIDIQTPHK-ITFNLDGEPLG-G 277
|
250
....*....|....
gi 1038032569 477 AEAEFTVRYRALQV 490
Cdd:TIGR00147 278 TPFHIEILPAHLRC 291
|
|
| DAGKc |
smart00046 |
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ... |
215-324 |
1.68e-08 |
|
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: 52.68 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 215 LVVNPRSGGGRAGEVAEQVRTALPAVTVVEL-GPDDDVAEAVRRAADSAEVLAIAGGDGSVAAAAGVAVERDL-----PL 288
Cdd:smart00046 2 VFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLtKKGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRELplpepPV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1038032569 289 AVFPGGTLNHFAKDIG----CDT--TAKTVRAIAEGSLSRVD 324
Cdd:smart00046 82 AVLPLGTGNDLARSLGwgggYDGekLLKTLRDALESDTVKLD 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LCB5 |
COG1597 |
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ... |
213-493 |
3.82e-59 |
|
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 441205 [Multi-domain] Cd Length: 295 Bit Score: 197.00 E-value: 3.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 213 VTLVVNPRSGGGRAGEVAEQVRTALPA----VTVVELGPDDDVAEAVRRAADS-AEVLAIAGGDGSVAAAAGVAVERDLP 287
Cdd:COG1597 5 ALLIVNPASGRGRAARLLERLVAALRAagleVEVLETESPGDATELAREAAAEgADLVVAAGGDGTVNEVANGLAGTGPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 288 LAVFPGGTLNHFAKDIGCDTT-AKTVRAIAEGSLSRVDVVQFNDEtTVVNTASVGAYPAFVRRRERLQHKVGKPVASVYA 366
Cdd:COG1597 85 LGILPLGTGNDFARALGIPLDpEAALEALLTGRTRRIDLGRVNGR-YFLNVAGIGFDAEVVERANRALKRRLGKLAYVLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 367 MLMTLRREQP--VRITYDDKTLQ--TSLFFLGNSAYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRLQ 442
Cdd:COG1597 164 ALRALLRYRPfrLRIELDGEEIEgeALLVAVGNGPYYGGGLRLAPDASLDDGLLDVVVVRPLSRLRLLRLLPRLLRGRHL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1038032569 443 RSRLYHELQVPQFRFTApDGPVPLARDGEVDSPCAEAEFTVRYRALQVFRP 493
Cdd:COG1597 244 RHPGVRYFRAREVEIES-DRPLPVQLDGEPLGLATPLEFEVLPGALRVLVP 293
|
|
| PRK13057 |
PRK13057 |
lipid kinase; |
215-496 |
2.09e-25 |
|
lipid kinase;
Pssm-ID: 183857 [Multi-domain] Cd Length: 287 Bit Score: 105.77 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 215 LVVNPRSGGGRAGevAEQVRTALPA--VTVVELGPDD--DVAEAVRRAADSAEVLAIAGGDGSVAAAAGVAVERDLPLAV 290
Cdd:PRK13057 2 LLVNRHARSGRAA--LAAARAALEAagLELVEPPAEDpdDLSEVIEAYADGVDLVIVGGGDGTLNAAAPALVETGLPLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 291 FPGGTLNHFAKDIGC-DTTAKTVRAIAEGSLSRVDVVQFNDEtTVVNTASVGAYPAFVRR-RERLQHKVGKpVASVYAML 368
Cdd:PRK13057 80 LPLGTANDLARTLGIpLDLEAAARVIATGQVRRIDLGWVNGH-YFFNVASLGLSAELARRlTKELKRRWGT-LGYAIAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 369 MTLRREQP--VRITYDD-----KTLQTSlffLGNSAYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRL 441
Cdd:PRK13057 158 RVLRRSRPftAEIEHDGrtervKTLQVA---VGNGRYYGGGMTVAHDATIDDGRLDLYSLEVAHWWRLLALLPALRRGRH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1038032569 442 QRSRLYHELQVPQFRFTApDGPVPLARDGEV--DSPcaeAEFTVRYRALQVFRPMPP 496
Cdd:PRK13057 235 GEWPDVRAFRTTELELRT-RKPRPINTDGELttYTP---AHFRVLPKALRVLAPPPA 287
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
28-186 |
1.09e-19 |
|
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 440435 [Multi-domain] Cd Length: 189 Bit Score: 87.02 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 28 AIAHSPSRLLDTTMPPLTRAADYSKLWLALAAVMAATGRASAQRAAARGVVSLALTSLVTNQVVKRIRPRARPDilQVPL 107
Cdd:COG0671 29 LLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF--VVPD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 108 LRRARRLPLSNSLPSGHSASAAAFATGVGLESP--LLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVVGAKL 185
Cdd:COG0671 107 LELLLGTAGGYSFPSGHAAAAFALALVLALLLPrrWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
|
.
gi 1038032569 186 V 186
Cdd:COG0671 187 L 187
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
77-181 |
4.83e-19 |
|
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.
Pssm-ID: 238813 [Multi-domain] Cd Length: 122 Bit Score: 82.89 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 77 VVSLALTSLVTNQVVKRIRPRARPD--ILQVPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP------LLGLPIAG 148
Cdd:cd01610 8 LLLALLAGLLLTGVLKYLFGRPRPYflLRCGPDGDPLLLTEGGYSFPSGHAAFAFALALFLALLLPrrllrlLLGLLLLL 87
|
90 100 110
....*....|....*....|....*....|...
gi 1038032569 149 LAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd01610 88 LALLVGLSRVYLGVHYPSDVLAGALLGILVALL 120
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
79-181 |
3.37e-17 |
|
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria.
Pssm-ID: 239483 Cd Length: 186 Bit Score: 79.67 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 79 SLALTSLVTNqVVKRIRPRARPDILQ---VPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESPLLGLPIAGLAGLVGL 155
Cdd:cd03389 77 TVALSGILVN-LLKFIIGRARPKLLFddgLYGFDPFHADYAFTSFPSGHSATAGAAAAALALLFPRYRWAFILLALLIAF 155
|
90 100
....*....|....*....|....*.
gi 1038032569 156 SRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd03389 156 SRVIVGAHYPSDVIAGSLLGAVTALA 181
|
|
| PRK00861 |
PRK00861 |
putative lipid kinase; Reviewed |
215-497 |
5.62e-16 |
|
putative lipid kinase; Reviewed
Pssm-ID: 234850 [Multi-domain] Cd Length: 300 Bit Score: 78.51 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 215 LVVNPRSGGGRAGEVAEQVRTAL-PAV------TVVELGPDDDVAEAVRRAADsaevLAIA-GGDGSVAAAAGVAVERDL 286
Cdd:PRK00861 7 LIFNPVAGQGNPEVDLALIRAILePEMdldiylTTPEIGADQLAQEAIERGAE----LIIAsGGDGTLSAVAGALIGTDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 287 PLAVFPGGTLNHFAKDIGC-DTTAKTVRAIAEGSLSRVDVVQFNDETTVVnTASVGAYPAFVRRRER-LQHKVGKpVASV 364
Cdd:PRK00861 83 PLGIIPRGTANAFAAALGIpDTIEEACRTILQGKTRRVDVAYCNGQPMIL-LAGIGFEAETVEEADReAKNRFGI-LAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 365 YAMLMTLRREQP--VRITYDDKTLQTSlfflgNSAYLPVGFAPAVR--------NRMDDGLLDVRILETGRPWSTLRILV 434
Cdd:PRK00861 161 LSGLQQLRELESfeVEIETEDQIITTN-----AVAVTVANAAPPTSvlaqgpgaVIPDDGLLDVTIVAPKNLAEAVAASY 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 435 ALLTGRLQRSRLYHE----LQVPQFRFTApDGPVPLARDGEVdspcAEA---EFTVRYRALQVFRPMPPE 497
Cdd:PRK00861 236 HLLQTALQGNPAERDdigyLRAKQVKITT-DPPQKVVIDGEV----VGTtpiEIECLPRSLKVFAPLQAE 300
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
213-327 |
1.25e-15 |
|
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: 73.39 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 213 VTLVVNPRSGGGRAGEVAEQVRTALPA----VTVVELGPDDDVAEAVRRAA-DSAEVLAIAGGDG--SVAAAAGVAVERD 285
Cdd:pfam00781 2 LLVIVNPKSGGGKGKKLLRKVRPLLNKagveVELVLTEGPGDALELAREAAeDGYDRIVVAGGDGtvNEVLNGLAGLATR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1038032569 286 LPLAVFPGGTLNHFAKDIGCDTTAKT-VRAIAEGSLSRVDVVQ 327
Cdd:pfam00781 82 PPLGIIPLGTGNDFARALGIPGDPEEaLEAILKGQTRPVDVGK 124
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
78-181 |
1.01e-14 |
|
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239488 [Multi-domain] Cd Length: 106 Bit Score: 70.05 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 78 VSLALTSLVTnQVVKRIRPRARPDilqvpllrraRRLPLSNSLPSGHSASAAAFATGVGLE--SPLLGLPIAGLAGLVGL 155
Cdd:cd03394 10 EAAALTAAVT-EGLKFAVGRARPD----------GSNNGYRSFPSGHTASAFAAATFLQYRygWRWYGIPAYALASLVGA 78
|
90 100
....*....|....*....|....*...
gi 1038032569 156 SRIATGAHYPGDVLAG--LGIGASIAVV 181
Cdd:cd03394 79 SRVVANRHWLSDVLAGaaIGILVGYLVT 106
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
78-181 |
3.77e-14 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 68.91 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 78 VSLALTSLVTNQVVKRIRPRARPDILQVPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP------LLGLPIAGLAG 151
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLParagrkLLIFLLLLLAL 84
|
90 100 110
....*....|....*....|....*....|
gi 1038032569 152 LVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:smart00014 85 VVGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
17-181 |
4.06e-14 |
|
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239486 Cd Length: 182 Bit Score: 70.72 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 17 GLGELDAEVFKAIAHSPSRLLDTTMPPLTRAADySKLWLALAAVMAATGRASAQRAAARGVVSLALTSLVTNQVVKRIRP 96
Cdd:cd03392 8 WLTAFDQSVLSLLRSLRTPLLTAFMTAITFLGS-PAVLLIIVLLLALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 97 RARPDILQVPLLRrarrlplSNSLPSGHSASAAAFATGVG------LESPLLGLPI----AGLAGLVGLSRIATGAHYPG 166
Cdd:cd03392 87 RPRPPLHLLVPEG-------GYSFPSGHAMGATVLYGFLAyllarrLPRRRVRILLlilaAILILLVGLSRLYLGVHYPS 159
|
170
....*....|....*
gi 1038032569 167 DVLAGLGIGASIAVV 181
Cdd:cd03392 160 DVLAGWLLGLAWLAL 174
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
77-181 |
1.83e-13 |
|
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.
Pssm-ID: 426329 [Multi-domain] Cd Length: 124 Bit Score: 67.06 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 77 VVSLALTSLVTN---QVVKRIRPRARPDILQvPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP--------LLGLP 145
Cdd:pfam01569 3 LLALALAGLLSSvlkDYFGRPRPFFLLLEGG-LVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRrlrkivrvLLALL 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 1038032569 146 IAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:pfam01569 82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALL 117
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
17-185 |
9.63e-13 |
|
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239489 Cd Length: 177 Bit Score: 66.52 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 17 GLGELDAEVFKAIAHSP-SRLLDTTMPPLTRAADYSKLWLALAAVMAATGRASAQRAAARGVVSLALTSLVTNQVVKRIR 95
Cdd:cd03395 1 LLEQIDVWLFLLLNGTLvHPLLDDLMPFLTGKKLSVPIFLLLALFILFRKGPIGLLILLLVLLAVGFADQLASGFLKPLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 96 PRARPDI-LQVPLLRRARRLPLSNSLPSGHSASAAAFATGVGLESP--LLGLPIAGLAGLVGLSRIATGAHYPGDVLAGL 172
Cdd:cd03395 81 ARLRPCNaLDGVRLVVLGDQGGSYSFASSHAANSFALALFIWLFFRrgLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGA 160
|
170
....*....|...
gi 1038032569 173 GIGASIAVVGAKL 185
Cdd:cd03395 161 LIGIISGLLFYLL 173
|
|
| TIGR00147 |
TIGR00147 |
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ... |
250-490 |
1.09e-12 |
|
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: 68.68 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 250 DVAEAVRRAAD-SAEVLAIAGGDGS--VAAAAGVAVERDLPLAVFPGGTLNHFAKDIGC-DTTAKTVRAIAEGSLSRVDV 325
Cdd:TIGR00147 45 DAARYVEEARKfGVDTVIAGGGDGTinEVVNALIQLDDIPALGILPLGTANDFARSLGIpEDLDKAAKLVIAGDARAIDM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 326 VQFNDETTVVNTASVGaypaFVRRR-----ERLQHKVGKpVASVYAMLMTLRREQPVR--ITYDDKTLQTS--LFFLGNS 396
Cdd:TIGR00147 125 GQVNKQYCFINMAGGG----FGTEIttetpEKLKAALGS-LSYILSGLMRMDTLQPFRceIRGEGEHWQGEavVFLVGNG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 397 AYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRLQRSRLYHELQVPQFRFTAPDGpVPLARDGEVDSpC 476
Cdd:TIGR00147 200 RQAGGGQKLAPDASINDGLLDLRIFTNDNLLPALVLTLMSDEGKHTDNPNIIYGKASRIDIQTPHK-ITFNLDGEPLG-G 277
|
250
....*....|....
gi 1038032569 477 AEAEFTVRYRALQV 490
Cdd:TIGR00147 278 TPFHIEILPAHLRC 291
|
|
| PRK12361 |
PRK12361 |
hypothetical protein; Provisional |
214-493 |
8.98e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 183473 [Multi-domain] Cd Length: 547 Bit Score: 64.26 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 214 TLVVNPRSGGGRAGEVAEQVRTALPA---VTVVELGPD---DDVAEAVRRAadSAEVLAIAGGDGSVAAAAGVAVERDLP 287
Cdd:PRK12361 246 WLIANPVSGGGKWQEYGEQIQRELKAyfdLTVKLTTPEisaEALAKQARKA--GADIVIACGGDGTVTEVASELVNTDIT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 288 LAVFPGGTLNHFAKDI-GCDTTAKTVR----AIAEGSLSRVDVVQFNDETTVVnTASVGAYPAFVRRRERLQHKVGKPVA 362
Cdd:PRK12361 324 LGIIPLGTANALSHALfGLGSKLIPVEqacdNIIQGHTQRIDTARCNDRLMLL-LVGIGFEQKMIESADRERKNALGQLA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 363 SVYAML--MTLRREQPVRITYDD---KTLQTSLFFLGNSAylPVGFAPAVRN---RMDDGLLDVRILE-TGRPWSTLRIL 433
Cdd:PRK12361 403 YLDGLWraVNENETLTLTVTLDDaepQTISTHSLVVANAA--PFTSLLAQGGgepNMTDGLLDITWLDsGGEPGEQLLSL 480
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1038032569 434 VAL----LTGRLQRSRLYHElQVPQFRFTApDGPVPLARDGEVDSPcAEAEFTVRYRALQVFRP 493
Cdd:PRK12361 481 AELalsgLGKEPEANKVHHA-HAKKVTISS-QKPIKYVIDGELFED-EDLTIEVQPASLKVFVP 541
|
|
| PRK13054 |
PRK13054 |
lipid kinase; Reviewed |
251-493 |
9.39e-09 |
|
lipid kinase; Reviewed
Pssm-ID: 237281 [Multi-domain] Cd Length: 300 Bit Score: 56.80 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 251 VAEAVrraADSAEVLAIAGGDGS----VAAAAGVAVERDLPLAVFPGGTLNHFAKDIGCDTT-AKTVRAIAEGSLSRVDV 325
Cdd:PRK13054 49 VEEAL---ALGVATVIAGGGDGTinevATALAQLEGDARPALGILPLGTANDFATAAGIPLEpDKALKLAIEGRAQPIDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 326 VQFNDETTVVNTASVGaypaF-----VRRRERLQHKVGKpVASVYAMLMTLRREQP--VRITYDDKTLQTSLFFL--GNS 396
Cdd:PRK13054 126 ARVNDRTYFINMATGG----FgtrvtTETPEKLKAALGG-VAYLIHGLMRMDTLKPdrCEIRGPDFHWQGDALVIgiGNG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 397 AYLPVGFAPAVRNRMDDGLLDVRILETgrPWSTLRILVALLTGRLQRSRLYHELQVPQFRFTAPDgPVPLARDGEvdsPC 476
Cdd:PRK13054 201 RQAGGGQQLCPEALINDGLLDLRILPA--PQELLPTLLSTLTGGSEDNPNIIRARLPWLEIQAPH-ELTFNLDGE---PL 274
|
250
....*....|....*....
gi 1038032569 477 AEAEF--TVRYRALQVFRP 493
Cdd:PRK13054 275 SGRHFriEVLPAALRCRLP 293
|
|
| PRK13059 |
PRK13059 |
putative lipid kinase; Reviewed |
250-442 |
1.50e-08 |
|
putative lipid kinase; Reviewed
Pssm-ID: 183858 Cd Length: 295 Bit Score: 56.20 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 250 DVAEAVRRAADSAEVLAIAGGDGSVAAAAGVAVER--DLPLAVFPGGTLNHFAKDIGCDTTAK-TVRAIAEGSLSRVDVV 326
Cdd:PRK13059 45 DLKNAFKDIDESYKYILIAGGDGTVDNVVNAMKKLniDLPIGILPVGTANDFAKFLGMPTDIGeACEQILKSKPKKVDLG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 327 QFNDEtTVVNTASVGAYPAFVRRRE-RLQHKVGKPVASVYAM--LMTLRReQPVRIT-----YDDKTLqTSLFFLGNSAy 398
Cdd:PRK13059 125 KINDK-YFINVASTGLFTDVSQKTDvNLKNTIGKLAYYLKGLeeLPNFRK-LKVKVTseevnFDGDMY-LMLVFNGQTA- 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1038032569 399 lpVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRLQ 442
Cdd:PRK13059 201 --GNFNLAYKAEVDDGLLDVIIIKACPIIDLIPLFIKVLKGEHL 242
|
|
| DAGKc |
smart00046 |
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ... |
215-324 |
1.68e-08 |
|
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: 52.68 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 215 LVVNPRSGGGRAGEVAEQVRTALPAVTVVEL-GPDDDVAEAVRRAADSAEVLAIAGGDGSVAAAAGVAVERDL-----PL 288
Cdd:smart00046 2 VFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLtKKGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKRELplpepPV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1038032569 289 AVFPGGTLNHFAKDIG----CDT--TAKTVRAIAEGSLSRVD 324
Cdd:smart00046 82 AVLPLGTGNDLARSLGwgggYDGekLLKTLRDALESDTVKLD 123
|
|
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
119-181 |
1.21e-07 |
|
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid phosphatases. Wunen is a drosophila protein expressed in the central nervous system, which provides repellent activity towards primordial germ cells (PGCs), controls the survival of PGCs and is essential in the migration process of these cells towards the somatic gonadal precursors.
Pssm-ID: 239479 Cd Length: 150 Bit Score: 51.09 E-value: 1.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1038032569 119 SLPSGHSASAAAFAT-------------GVGLESPLLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd03384 73 SFPSGHASLSMYAAVflalylqarlklrGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALF 148
|
|
| PRK13055 |
PRK13055 |
putative lipid kinase; Reviewed |
247-439 |
4.48e-07 |
|
putative lipid kinase; Reviewed
Pssm-ID: 237282 [Multi-domain] Cd Length: 334 Bit Score: 51.91 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 247 PDDDVAEAVRRAADSAEVLAIAGGDGSV--AAAAGVAVERDLPLAVFPGGTLNHFAK--DIGCDTTAKTVRAIAEGSLSR 322
Cdd:PRK13055 45 PNSAKNEAKRAAEAGFDLIIAAGGDGTIneVVNGIAPLEKRPKMAIIPAGTTNDYARalKIPRDNPVEAAKVILKNQTIK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 323 VDVVQFNDETTVVNTASVGaypafvrRRERLQHKVGKPVASVY---------AMLMTLRREQPVRITYDDKTL--QTSLF 391
Cdd:PRK13055 125 MDIGRANEDKYFINIAAGG-------SLTELTYSVPSQLKSMFgylaylakgAELLPRVSPVPVRITYDEGVFegKISMF 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1038032569 392 FLG--NSAYlpvGFAPAVRN-RMDDGLLDVRILETGRPWSTLRILVALLTG 439
Cdd:PRK13055 198 FLAltNSVG---GFEQIVPDaKLDDGKFTLIIVKTANLFELLHLMALILNG 245
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
119-175 |
8.97e-07 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to eukaryota, lacks functional characterization and may act as a membrane-associated phosphatidic acid phosphatase.
Pssm-ID: 239485 [Multi-domain] Cd Length: 159 Bit Score: 48.85 E-value: 8.97e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 119 SLPSGHSASAAAFATGVGLESPL---LGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIG 175
Cdd:cd03391 92 SFPSGHASRAAFVARFLLNHLVLavpLRVLLVLWATVVGISRVLLGRHHVLDVLAGAFLG 151
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
77-181 |
1.75e-06 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.
Pssm-ID: 239484 [Multi-domain] Cd Length: 193 Bit Score: 48.37 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 77 VVSLALTSLVTNqVVK----RIRP----RARPDILQVPLLRRARRLPLSN----------SLPSGHSASAAA---FAT-- 133
Cdd:cd03390 52 LLSVSLNGVITN-VLKnyagRPRPdflaRCFPDGGTPSDTLVGIDICCTGdpgvlkegrkSFPSGHSSFAFAglgFLSly 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1038032569 134 -----------GVGLESPLLGLPIAgLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd03390 131 lagklhifdprGSSWRLLLALLPLL-LAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYL 188
|
|
| PAP2_BcrC_like |
cd03385 |
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ... |
118-179 |
3.15e-06 |
|
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as bacitracin transport permeases, as it was suspected that they form the permease component of an ABC transporter system. It was shown, however, that BcrC from Bacillus subtilis posesses undecaprenyl pyrophosphate (UPP) phospatase activity, and it is hypothesized that it competes with bacitracin for UPP, increasing the cell's resistance to bacitracin.
Pssm-ID: 239480 Cd Length: 144 Bit Score: 46.87 E-value: 3.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1038032569 118 NSLPSGHSASAAAFATGVGL-ESPLLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIA 179
Cdd:cd03385 77 SSFPSDHTTLFFSIAFSLLLrRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSA 139
|
|
| PRK11914 |
PRK11914 |
diacylglycerol kinase; Reviewed |
213-439 |
7.16e-06 |
|
diacylglycerol kinase; Reviewed
Pssm-ID: 237021 [Multi-domain] Cd Length: 306 Bit Score: 47.86 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 213 VTLVVNPRSGGGRAGEVAEQVRTALPA--VTVVEL-GPD-DDVAEAVRRA-ADSAEVLAIAGGDGSVAAAAGVAVERDLP 287
Cdd:PRK11914 11 VTVLTNPLSGHGAAPHAAERAIARLHHrgVDVVEIvGTDaHDARHLVAAAlAKGTDALVVVGGDGVISNALQVLAGTDIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 288 LAVFPGGTLNHFAKDIGCDTTAKTVRA--IAEGSLSRVDVVQFNDETTVV---NTASVGAYPAFVRRRERLQHKVGKPVA 362
Cdd:PRK11914 91 LGIIPAGTGNDHAREFGIPTGDPEAAAdvIVDGWTETVDLGRIQDDDGIVkwfGTVAATGFDSLVTDRANRMRWPHGRMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 363 SVYAMLMTLR--REQPVRITYDDK---TLQTSLFFLGNSAYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALL 437
Cdd:PRK11914 171 YNLAMLAELSklRPLPFRLVLDGTeeiVTDLTLAAFGNTRSYGGGMLICPNADHTDGLLDITMVQSASRTRLLRLFPTVF 250
|
..
gi 1038032569 438 TG 439
Cdd:PRK11914 251 KG 252
|
|
| PAP2_like_1 |
cd03380 |
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ... |
119-180 |
1.20e-05 |
|
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases.
Pssm-ID: 239475 Cd Length: 209 Bit Score: 46.27 E-value: 1.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1038032569 119 SLPSGHSASAAAFATGVGLESPLLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAV 180
Cdd:cd03380 144 SYPSGHATFGGAAALVLAELFPERAAELLARAAEAGNSRVVAGVHWPSDVEAGRILGEAIAA 205
|
|
| PAP2_SPPase1 |
cd03388 |
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ... |
119-181 |
5.08e-05 |
|
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.
Pssm-ID: 239482 Cd Length: 151 Bit Score: 43.37 E-value: 5.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1038032569 119 SLPSGHSASAAAFA-------TGVGLESPLLGLPIAGL-AGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd03388 79 GFPSTHAMNATAISfylliylYDRYQYPFVLGLILALFySTLVCLSRIYMGMHSVLDVIAGSLIGVLILLF 149
|
|
| YegS_C |
pfam19279 |
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ... |
338-492 |
1.04e-04 |
|
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: 42.57 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 338 ASVGA-YPAFVRRRERLQHKVGKPVASVYAMLMTLRREQPV--RITYDD--KTLQTSLFFLGNSAYLPVGFAPAVRNRMD 412
Cdd:pfam19279 1 GSVYAgVDARVNRRANRSRLLPGALSYPAAALRALATFRPLryRVTVDGevREFSAALVAVANSGYYGGGMRIAPDARVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 413 DGLLDVRILETGRPWSTLRILVALLTGRLQRSRLYHELQVPQFRFTApDGPVPLARDGEVDSPcAEAEFTVRYRALQVFR 492
Cdd:pfam19279 81 DGLLDVVVIEAASRRTLLRLLPKVYDGRHVRLPQVEVLRGREVRIEA-DRPLPAGADGEVLGP-LPVRVEVLPGALRVLA 158
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
76-186 |
3.99e-04 |
|
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which mainly contains bacterial proteins, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239490 Cd Length: 197 Bit Score: 41.52 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 76 GVVSLAL-TSLVTNQVVKRIRPRARP-DILQ--------VPLLRRARRLPLSNSLPSGHSASAAAF------ATGVGLES 139
Cdd:cd03396 70 LLLILVIgLGLLVVAILKSHWGRPRPwDLTEfggdapytPLFSGPSNGCGKGCSFPSGHASAGFALlalyflFRRRRPRL 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1038032569 140 PLLGLPIA-GLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVVGAKLV 186
Cdd:cd03396 150 ARLVLAAGlALGALMGLARMARGAHFLSDVLWSLLLVWLIALLLYRLI 197
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
4-479 |
4.52e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.94 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 4 LRRRRSGLRQITQGLGEL-------------------------------DAEVFKAIAHSPSRLLDTTMPPLTRAADYSK 52
Cdd:COG3321 823 LRRGEDELAQLLTALAQLwvagvpvdwsalypgrgrrrvplptypfqreDAAAALLAAALAAALAAAAALGALLLAALAA 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 53 LWLALAAVMAATGRASAQRAAARGVVSLALTSLVTNQVVKRIRPRARPDILQVPLLRRARRLPLSNSLPSGHSASAAAFA 132
Cdd:COG3321 903 ALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAA 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 133 TGVGLESPLLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVVGAKLVPPIPSPPPQHVDALRVACLPRPDGAG 212
Cdd:COG3321 983 AAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALA 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 213 VtlvvnprsGGGRAGEVAEQVRTALPAVTVVELGPDDDVAEAVRRAADSAEVLAIAGGDGSVAAAAGVAVERDLPLAVFP 292
Cdd:COG3321 1063 L--------ALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAA 1134
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 293 GGTLNHFAKDIGCDTTAKTVRAIAEGSLSRVDVVQFNDETTVVNTASVGAYPAFVRRRERLQHKVGKPVASVYAMLMTLR 372
Cdd:COG3321 1135 AAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALA 1214
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 373 REQPVRITYDDKTLQTSLFFLGNSAYLPVGFAPAVRNRMDDGLLDVRILETGRPWSTLRILVALLTGRLQRSRLYHELQV 452
Cdd:COG3321 1215 ALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAA 1294
|
490 500
....*....|....*....|....*..
gi 1038032569 453 PQFRFTAPDGPVPLARDGEVDSPCAEA 479
Cdd:COG3321 1295 AAALAALLAAAAAAAAAAAAAAAAAAL 1321
|
|
| PAP2_diacylglycerolkinase |
cd03383 |
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ... |
120-180 |
6.34e-04 |
|
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like phosphatase domains appear fused to E. coli DAGK-like trans-membrane diacylglycerol kinase domains. The cellular function of these architectures remains to be determined.
Pssm-ID: 239478 [Multi-domain] Cd Length: 109 Bit Score: 39.23 E-value: 6.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1038032569 120 LPSGHSASAAAFATGVGL--ESPLLGLPIAGLAGLVGLSRIATGAHYPGDVLAG--LGIGASIAV 180
Cdd:cd03383 41 MPSGHAAIAFSIATAISLitNNPIISILSVLLAVMVAHSRVEMKIHTMWEVVVGaiLGALITLLI 105
|
|
| PAP2_like_3 |
cd03393 |
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
82-182 |
6.38e-04 |
|
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria and archaea, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239487 [Multi-domain] Cd Length: 125 Bit Score: 39.66 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 82 LTSLVTNQVVKRIRPRARPDILQVPLLRRARRLPlSNSLPSGHSASAAAFATGVGL--ESPLLGLPIAGLAGLVGLSRIA 159
Cdd:cd03393 23 CASGYLNAALKEVFKIPRPFTYDGIQAIYEESAG-GYGFPSGHAQTSATFWGSLMLhvRKKWFTLIGVVLVVLISFSRLY 101
|
90 100
....*....|....*....|...
gi 1038032569 160 TGAHYPGDVLAGLGIGASIAVVG 182
Cdd:cd03393 102 LGVHWPSDVIGGVLIGLLVLVLG 124
|
|
| PAP2_acid_phosphatase |
cd03397 |
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ... |
119-181 |
4.07e-03 |
|
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.
Pssm-ID: 239491 Cd Length: 232 Bit Score: 38.86 E-value: 4.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1038032569 119 SLPSGHSASAAAFATGVGLESPLLGLPIAGLAGLVGLSRIATGAHYPGDVLAGLGIGASIAVV 181
Cdd:cd03397 151 SYPSGHTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAA 213
|
|
| PAP2_haloperoxidase |
cd03398 |
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ... |
119-180 |
5.11e-03 |
|
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles.
Pssm-ID: 239492 Cd Length: 232 Bit Score: 38.56 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038032569 119 SLPSGHSASAAAFAT-----------GVGLESPLLGLPIAG----------LAGLVGLSRIATGAHYPGDVLAGLGIGAS 177
Cdd:cd03398 146 SYPSGHATFAGAAATvlkalfgsdkvPDTVSEPDEGGPSTGvtrvwaelneLADEVAISRVYAGVHFRSDDAAGAALGEQ 225
|
...
gi 1038032569 178 IAV 180
Cdd:cd03398 226 IGA 228
|
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