|
Name |
Accession |
Description |
Interval |
E-value |
| PAP2_SPPase1 |
cd03388 |
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ... |
126-275 |
3.34e-76 |
|
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: 234.43 E-value: 3.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 126 WPLYCLFCFGTELGNELFYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVKLEVF-YNSEYSM 204
Cdd:cd03388 1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSsAALEYGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13540569 205 PSTHAMSGTAIPISMVLLTYGRWQYPLIYGLILIPCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:cd03388 81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
|
|
| PLN02525 |
PLN02525 |
phosphatidic acid phosphatase family protein |
143-435 |
4.21e-24 |
|
phosphatidic acid phosphatase family protein
Pssm-ID: 215288 Cd Length: 352 Bit Score: 102.51 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 143 FYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPV-----VKLEVFYNSEYSMPSTHAMSGTAIPI 217
Cdd:PLN02525 20 FYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVrrvtaTKDEEENAMEYGLPSSHTLNTVCLSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 218 SMV--LLTYGRWQYPLI--YGLILIpcwCSLVCL---SRIYMGMHSILDIIAGFLYTILILAVFYPFVDLIDNF-----N 285
Cdd:PLN02525 100 YLLhyVLSYLQNVDASVifAGLALF---CLLVALvgfGRLYLGMHSPIDIIAGLAIGLVILAFWLTVDEYVDAFitsgqN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 286 QTHKYAPFIIIGLhlalgiFSFTLDTWST-SRGDTAEILGSGAGIACGSHVTYNMGlvldPSLDTLPLAGPPITVTLFgk 364
Cdd:PLN02525 177 VTPFWAALSFLLL------FAYPTPEFPTpSFEYHTAFNGVAFGIVAGVQQTYSQF----HHEAAPRIFSPQLPIAAF-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 365 aILRILIGMVFVLIIRDVMK---KITIPLACKIFNIPC------------------DDIRKAR------------QHMEV 411
Cdd:PLN02525 245 -LGRVAVGIPTILAVKFCSKalaKWLLPVVCNALGIPIrstsyvpslkgsvsgkksDEPKQSVgylqklcffssqDSFDV 323
|
330 340
....*....|....*....|....
gi 13540569 412 ELPYRYITYGMVGFSITFFVPYIF 435
Cdd:PLN02525 324 DTGIRFLQYAGLAWSVVDLVPSIF 347
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
142-275 |
1.73e-14 |
|
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: 71.61 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 142 LFYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVL 221
Cdd:COG0671 57 LLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLAL 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 13540569 222 LTYGRWQYPLIYGLILipcwcsLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:COG0671 137 LLPRRWLAALLLALAL------LVGLSRVYLGVHYPSDVLAGALLGLAIALLLL 184
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
163-278 |
3.47e-14 |
|
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: 68.99 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 163 LVVIWVLVMYLGQCTKDIIRWPRPA-----SPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLIL 237
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 13540569 238 IPCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFYPFV 278
Cdd:pfam01569 82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLV 122
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
168-275 |
2.31e-13 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 66.22 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 168 VLVMYLGQCTKDIIRW----PRP------ASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLIL 237
Cdd:smart00014 1 ALLAVVSQLFNGVIKNyfgrPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 13540569 238 IpcWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:smart00014 81 L--LALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PAP2_SPPase1 |
cd03388 |
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ... |
126-275 |
3.34e-76 |
|
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: 234.43 E-value: 3.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 126 WPLYCLFCFGTELGNELFYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVKLEVF-YNSEYSM 204
Cdd:cd03388 1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSsAALEYGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13540569 205 PSTHAMSGTAIPISMVLLTYGRWQYPLIYGLILIPCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:cd03388 81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
|
|
| PLN02525 |
PLN02525 |
phosphatidic acid phosphatase family protein |
143-435 |
4.21e-24 |
|
phosphatidic acid phosphatase family protein
Pssm-ID: 215288 Cd Length: 352 Bit Score: 102.51 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 143 FYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPV-----VKLEVFYNSEYSMPSTHAMSGTAIPI 217
Cdd:PLN02525 20 FYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVrrvtaTKDEEENAMEYGLPSSHTLNTVCLSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 218 SMV--LLTYGRWQYPLI--YGLILIpcwCSLVCL---SRIYMGMHSILDIIAGFLYTILILAVFYPFVDLIDNF-----N 285
Cdd:PLN02525 100 YLLhyVLSYLQNVDASVifAGLALF---CLLVALvgfGRLYLGMHSPIDIIAGLAIGLVILAFWLTVDEYVDAFitsgqN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 286 QTHKYAPFIIIGLhlalgiFSFTLDTWST-SRGDTAEILGSGAGIACGSHVTYNMGlvldPSLDTLPLAGPPITVTLFgk 364
Cdd:PLN02525 177 VTPFWAALSFLLL------FAYPTPEFPTpSFEYHTAFNGVAFGIVAGVQQTYSQF----HHEAAPRIFSPQLPIAAF-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 365 aILRILIGMVFVLIIRDVMK---KITIPLACKIFNIPC------------------DDIRKAR------------QHMEV 411
Cdd:PLN02525 245 -LGRVAVGIPTILAVKFCSKalaKWLLPVVCNALGIPIrstsyvpslkgsvsgkksDEPKQSVgylqklcffssqDSFDV 323
|
330 340
....*....|....*....|....
gi 13540569 412 ELPYRYITYGMVGFSITFFVPYIF 435
Cdd:PLN02525 324 DTGIRFLQYAGLAWSVVDLVPSIF 347
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
163-275 |
2.55e-18 |
|
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: 80.58 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 163 LVVIWVLVMYLGQCTKDIIRWPRPASPPVVK----LEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLILI 238
Cdd:cd01610 8 LLLALLAGLLLTGVLKYLFGRPRPYFLLRCGpdgdPLLLTEGGYSFPSGHAAFAFALALFLALLLPRRLLRLLLGLLLLL 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 13540569 239 pcWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:cd01610 88 --LALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
142-275 |
1.73e-14 |
|
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: 71.61 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 142 LFYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVL 221
Cdd:COG0671 57 LLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLAL 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 13540569 222 LTYGRWQYPLIYGLILipcwcsLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:COG0671 137 LLPRRWLAALLLALAL------LVGLSRVYLGVHYPSDVLAGALLGLAIALLLL 184
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
163-278 |
3.47e-14 |
|
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: 68.99 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 163 LVVIWVLVMYLGQCTKDIIRWPRPA-----SPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLIL 237
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 13540569 238 IPCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFYPFV 278
Cdd:pfam01569 82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLV 122
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
168-275 |
2.31e-13 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 66.22 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 168 VLVMYLGQCTKDIIRW----PRP------ASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLIL 237
Cdd:smart00014 1 ALLAVVSQLFNGVIKNyfgrPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 13540569 238 IpcWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:smart00014 81 L--LALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
120-281 |
5.49e-11 |
|
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: 61.09 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 120 LARVSNWPLYCLFCFGTELGNELFYILFFPFWIWNLdPLVGRRLVVIWVLVMYLG-----QCTKDIIRWPRPASPPVVKL 194
Cdd:cd03392 20 LRSLRTPLLTAFMTAITFLGSPAVLLIIVLLLALLL-LLKRRRRAALFLLLALLGggalnTLLKLLVQRPRPPLHLLVPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 195 EVfynseYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLILIPC--WCSLVCLSRIYMGMHSILDIIAGFLYTILILA 272
Cdd:cd03392 99 GG-----YSFPSGHAMGATVLYGFLAYLLARRLPRRRVRILLLILAaiLILLVGLSRLYLGVHYPSDVLAGWLLGLAWLA 173
|
....*....
gi 13540569 273 VFYPFVDLI 281
Cdd:cd03392 174 LLILLYRRL 182
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
142-275 |
8.30e-10 |
|
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: 57.66 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 142 LFYILFFPFWIWNLDPLVgRRLVVIWVLVMYLGQCT----KDIIRWPRPASPPVVKLEVFYNSE---YSMPSTHAMSGTA 214
Cdd:cd03395 38 IFLLLALFILFRKGPIGL-LILLLVLLAVGFADQLAsgflKPLVARLRPCNALDGVRLVVLGDQggsYSFASSHAANSFA 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13540569 215 IPISMVLLTYGRWQYPLIYglilipCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFY 275
Cdd:cd03395 117 LALFIWLFFRRGLFSPVLL------LWALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFY 171
|
|
| PAP2_like_3 |
cd03393 |
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
146-271 |
1.50e-09 |
|
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: 55.84 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 146 LFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVkLEVFYNSE--YSMPSTHAMSGTAIPISMVLLT 223
Cdd:cd03393 1 IVLSLIYWLVDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYDGI-QAIYEESAggYGFPSGHAQTSATFWGSLMLHV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 13540569 224 YGRWQYplIYGLILIpcwcSLVCLSRIYMGMHSILDIIAGFLYTILIL 271
Cdd:cd03393 80 RKKWFT--LIGVVLV----VLISFSRLYLGVHWPSDVIGGVLIGLLVL 121
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
120-275 |
3.69e-08 |
|
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a membrane-associated protein located in the endoplasmic reticulum and hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate. The enzyme is necessary for maintaining proper levels of dolichol-linked oligosaccharides and protein N-glycosylation, and might play a role in re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during protein N-glycosylation reactions.
Pssm-ID: 239477 Cd Length: 159 Bit Score: 52.66 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 120 LARVSNWPLYCLFCFGTelgnelfyilffpfWIwnldpLVGRRLVVIWVLvmyLGQCT--------KDIIRWPRPASPpv 191
Cdd:cd03382 18 LAYLSLLPVAILVGYAT--------------LI-----LFRRELEAIYLF---IGLLAnealnyvlKRIIKEPRPCSG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 192 vklEVFYNSEYSMPSTHA--MSGTAIPISMVLLTYGRWQYPLIYGLILIPC---WCSLVCLSRIYMGMHSILDIIAGFLY 266
Cdd:cd03382 74 ---AYFVRSGYGMPSSHSqfMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGlllLALLVSYSRVYLGYHTVSQVVVGAIV 150
|
....*....
gi 13540569 267 TILiLAVFY 275
Cdd:cd03382 151 GIL-LGILW 158
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
145-269 |
4.62e-06 |
|
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: 46.54 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 145 ILFFPFWI---WNLDPLVGRRLVVIWVLVMYLGQCT----KDIIRWPRPASPPVVKLEVFYNSEYSMPSTHAmsGTAIPI 217
Cdd:cd03391 27 IPWLAGTIsclWISSSPAGQEVLVNLLLGLLLDIITvailKALVRRRRPAYNSPDMLDYVAVDKYSFPSGHA--SRAAFV 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 13540569 218 SMVLLTYGRWQYPLIYGLILipcWCSLVCLSRIYMGMHSILDIIAGFLYTIL 269
Cdd:cd03391 105 ARFLLNHLVLAVPLRVLLVL---WATVVGISRVLLGRHHVLDVLAGAFLGYL 153
|
|
| PAP2_BcrC_like |
cd03385 |
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ... |
150-276 |
1.83e-04 |
|
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: 41.47 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540569 150 FWIWNLDPlvgRRLVVIWVLV-----MYLGQCTKDIIRWPRPASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLlty 224
Cdd:cd03385 23 LWLWGGEK---QRKVVLFATIavavaLLINYIIGLLYFHPRPFVVGLGHNLLPHAADSSFPSDHTTLFFSIAFSLLL--- 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 13540569 225 grWQYPLIYGLILIpcWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFYP 276
Cdd:cd03385 97 --RRRKWAGWILLI--LALLVAWSRIYLGVHYPLDMLGAALVAVLSALLVFQ 144
|
|
| PAP2_diacylglycerolkinase |
cd03383 |
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ... |
204-274 |
1.48e-03 |
|
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: 38.08 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13540569 204 MPSTHAMSGTAIPISMVLLTygrwQYPLIygLILIPCWCSLVCLSRIYMGMHSILDIIA----GFLYTILILAVF 274
Cdd:cd03383 41 MPSGHAAIAFSIATAISLIT----NNPII--SILSVLLAVMVAHSRVEMKIHTMWEVVVgailGALITLLIFKIF 109
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| PRK09597 |
PRK09597 |
lipid A 1-phosphatase LpxE; |
198-274 |
2.78e-03 |
|
lipid A 1-phosphatase LpxE;
Pssm-ID: 181978 Cd Length: 190 Bit Score: 38.72 E-value: 2.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13540569 198 YNSEYSMPSTHA-MSGTAIPISMVlltygrwQYPLIYGLILIPCwCSLVCLSRIYMGMHSILDIIAGFLYTILILAVF 274
Cdd:PRK09597 115 YGGNFNMPSGHSsMVGLAVAFLMR-------RYSFKKYWWLLPL-IPLTMLARIYLDMHTIGAVLAGLGVGMLCVSLF 184
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| PAP2_Aur1_like |
cd03386 |
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ... |
204-278 |
3.61e-03 |
|
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.
Pssm-ID: 239481 Cd Length: 186 Bit Score: 38.45 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13540569 204 MPSTHamSGTAIPISMVLLTYGRWQYPLIYGLilipcWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFYPFV 278
Cdd:cd03386 119 FPSLH--VAWAVLAALFLWRHRRRLLRWLAVL-----WPLLIWLSTLYLGNHYFIDLVGGIALALLSFYLARRVR 186
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