|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
18-262 |
4.00e-126 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 362.32 E-value: 4.00e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 18 RVARSHAWDWVALLLLVAVDVLLNVIEPFHRFVGAGMMADLRYPMKGNTVPVWAVPIIAVIGPVTIFAVVYIRRRNAYDL 97
Cdd:PLN02250 17 KVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPFAVILVYYFIRRDVYDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 98 HHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDGEAVYNNITTGVVCHGDPSVIKEGYKSFPSGHTSWSFAGLG 177
Cdd:PLN02250 97 HHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 178 FLSWYLAGKMTAFDRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQFFPAPSDEKGFWP 257
Cdd:PLN02250 177 FLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPPPYDIDGWGP 256
|
....*
gi 670389720 258 HAHLR 262
Cdd:PLN02250 257 HAYFQ 261
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
58-245 |
1.13e-74 |
|
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: 227.10 E-value: 1.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 58 LRYPMKGN-TVPVWAVPIIAVIGPVTIFAVVYIR-RRNAYDLHHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFP 135
Cdd:cd03390 3 ISYPFAESeTVPTWLLVIISVGIPLLVIILISLFfRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARCFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 136 DGEAVYNNITTGVVC-HGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYLAGKMTAFDRRGHVAKLCVVLLPLLVAALVAV 214
Cdd:cd03390 83 DGGTPSDTLVGIDICcTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILVAV 162
|
170 180 190
....*....|....*....|....*....|.
gi 670389720 215 SRVDDYWHHWQDVCTGGVLGLVVASVCYLQF 245
Cdd:cd03390 163 SRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
104-246 |
2.61e-15 |
|
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: 70.91 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 104 ILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDgeavynnittgvvcHGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYL 183
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL--------------VPAPSTLPGLGYSFPSGHSATAFALALLLALLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670389720 184 AgkmtafdRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQFF 246
Cdd:pfam01569 68 R-------RLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
105-242 |
4.26e-11 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 58.90 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 105 LFAVLITGVLTDAIKDAVGRPRPnfywrcfpdgeavYNNITTGVVCHGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYLa 184
Cdd:smart00014 1 ALLAVVSQLFNGVIKNYFGRPRP-------------FFLSIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 670389720 185 gkmtafdrRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCY 242
Cdd:smart00014 67 --------PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
69-245 |
4.50e-07 |
|
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: 49.27 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 69 VWAVPIIAVIGPVTIFAVVYIRRRNAYDLHHAILGILFAVLITGVLTDAIKDAVGRPRPNfywrcfpdgeavynnittgV 148
Cdd:COG0671 43 LLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF-------------------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 149 VCHGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYLagkmtafdRRGHVAKLCvvllpLLVAALVAVSRVDDYWHHWQDVC 228
Cdd:COG0671 104 VPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL--------PRRWLAALL-----LALALLVGLSRVYLGVHYPSDVL 170
|
170
....*....|....*..
gi 670389720 229 TGGVLGLVVASVCYLQF 245
Cdd:COG0671 171 AGALLGLAIALLLLALL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
18-262 |
4.00e-126 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 362.32 E-value: 4.00e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 18 RVARSHAWDWVALLLLVAVDVLLNVIEPFHRFVGAGMMADLRYPMKGNTVPVWAVPIIAVIGPVTIFAVVYIRRRNAYDL 97
Cdd:PLN02250 17 KVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPFAVILVYYFIRRDVYDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 98 HHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDGEAVYNNITTGVVCHGDPSVIKEGYKSFPSGHTSWSFAGLG 177
Cdd:PLN02250 97 HHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 178 FLSWYLAGKMTAFDRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQFFPAPSDEKGFWP 257
Cdd:PLN02250 177 FLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPPPYDIDGWGP 256
|
....*
gi 670389720 258 HAHLR 262
Cdd:PLN02250 257 HAYFQ 261
|
|
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
19-262 |
8.84e-105 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 308.88 E-value: 8.84e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 19 VARSHAWDWVALLLLVAVDVLLNVIEPFHRFVGAGMMADLRYPMKGNTVPVWAVPIIAVIGPVTIFAVVYIRRRNAYDLH 98
Cdd:PLN02731 37 VARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 99 HAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDGEAVYNNITTgVVCHGDPSVIKEGYKSFPSGHTSWSFAGLGF 178
Cdd:PLN02731 117 HAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLGD-VICHGDKSVIREGHKSFPSGHTSWSFSGLGF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 179 LSWYLAGKMTAFDRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQFFPAPSDEKGFWPH 258
Cdd:PLN02731 196 LSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPY 275
|
....
gi 670389720 259 AHLR 262
Cdd:PLN02731 276 AYFQ 279
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
18-262 |
3.55e-99 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 294.27 E-value: 3.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 18 RVARSHAWDWVALLLLVAVDVLLNVIEPFHRFVGAGMMADLRYPMKGNTVPVWAVPIIAVIGPVTIFAVVYIRRRNAYDL 97
Cdd:PLN02715 42 RVASKHKHDWIILVILIAIEIGLNLISPFYRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLPIILFVCFYLKRRCVYDL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 98 HHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDGEAVYNNItTGVVCHGDPSVIKEGYKSFPSGHTSWSFAGLG 177
Cdd:PLN02715 122 HHSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDAL-GGVICHGKAAEVKEGHKSFPSGHTSWSFAGLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 178 FLSWYLAGKMTAFDRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQFFPAPSDEKGFWP 257
Cdd:PLN02715 201 FLSLYLSGKIKAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCYRQFYPNPYHEEGWGP 280
|
....*
gi 670389720 258 HAHLR 262
Cdd:PLN02715 281 YAYFK 285
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
58-245 |
1.13e-74 |
|
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: 227.10 E-value: 1.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 58 LRYPMKGN-TVPVWAVPIIAVIGPVTIFAVVYIR-RRNAYDLHHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFP 135
Cdd:cd03390 3 ISYPFAESeTVPTWLLVIISVGIPLLVIILISLFfRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARCFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 136 DGEAVYNNITTGVVC-HGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYLAGKMTAFDRRGHVAKLCVVLLPLLVAALVAV 214
Cdd:cd03390 83 DGGTPSDTLVGIDICcTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILVAV 162
|
170 180 190
....*....|....*....|....*....|.
gi 670389720 215 SRVDDYWHHWQDVCTGGVLGLVVASVCYLQF 245
Cdd:cd03390 163 SRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
105-238 |
1.94e-26 |
|
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: 101.55 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 105 LFAVLITGVLTDAIKDAVGRPRPNFYWRCFPD-----GEAVYNNITTGVVCHGDPSVIKEGYKSFPSGHTSWSFAGLGFL 179
Cdd:cd03384 10 LFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNytdltCSLDHQYIADCTCCTGDPDLIREARLSFPSGHASLSMYAAVFL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 670389720 180 SWYLAGKMTafDRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVA 238
Cdd:cd03384 90 ALYLQARLK--LRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIA 146
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
97-242 |
7.13e-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: 77.89 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 97 LHHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDGeavynnittgvvchgDPSVIKEGYKSFPSGHTSWSFAGL 176
Cdd:cd01610 1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG---------------DPLLLTEGGYSFPSGHAAFAFALA 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670389720 177 GFLSWYLagkmtafdrRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCY 242
Cdd:cd01610 66 LFLALLL---------PRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
104-246 |
2.61e-15 |
|
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: 70.91 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 104 ILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDgeavynnittgvvcHGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYL 183
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL--------------VPAPSTLPGLGYSFPSGHSATAFALALLLALLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670389720 184 AgkmtafdRRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQFF 246
Cdd:pfam01569 68 R-------RLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
105-242 |
4.26e-11 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 58.90 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 105 LFAVLITGVLTDAIKDAVGRPRPnfywrcfpdgeavYNNITTGVVCHGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYLa 184
Cdd:smart00014 1 ALLAVVSQLFNGVIKNYFGRPRP-------------FFLSIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 670389720 185 gkmtafdrRGHVAKLCVVLLPLLVAALVAVSRVDDYWHHWQDVCTGGVLGLVVASVCY 242
Cdd:smart00014 67 --------PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
75-246 |
1.30e-08 |
|
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: 53.77 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 75 IAVIGPVTIFAVVYIRRRNAYdlhHAILGILFAVLITGVLTDAIKDAVGRPRPNFYWRCFPDGeavynnittgvvchgdp 154
Cdd:cd03392 41 PAVLLIIVLLLALLLLLKRRR---RAALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVPEGG----------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 155 svikegyKSFPSGHTSWSFAGLGFLSWYLAGKMTAFDRRGHVAKLCvvllpLLVAALVAVSRVDDYWHHWQDVCTGGVLG 234
Cdd:cd03392 101 -------YSFPSGHAMGATVLYGFLAYLLARRLPRRRVRILLLILA-----AILILLVGLSRLYLGVHYPSDVLAGWLLG 168
|
170
....*....|..
gi 670389720 235 LVVASVCYLQFF 246
Cdd:cd03392 169 LAWLALLILLYR 180
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
105-238 |
2.84e-07 |
|
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: 48.10 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 105 LFAVLITGVLTDAIKDAVGRPRPNFYWRcfpdgeavynnittgvvchgdpsvikeGYKSFPSGHTSWSFAGLGFLSW--- 181
Cdd:cd03394 9 AEAAALTAAVTEGLKFAVGRARPDGSNN---------------------------GYRSFPSGHTASAFAAATFLQYryg 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 670389720 182 --------YLAGKMTAFdrrghvaklcvvllpllvaalvavSRVDDYWHHWQDVCTGGVLGLVVA 238
Cdd:cd03394 62 wrwygipaYALASLVGA------------------------SRVVANRHWLSDVLAGAAIGILVG 102
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
69-245 |
4.50e-07 |
|
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: 49.27 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 69 VWAVPIIAVIGPVTIFAVVYIRRRNAYDLHHAILGILFAVLITGVLTDAIKDAVGRPRPNfywrcfpdgeavynnittgV 148
Cdd:COG0671 43 LLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF-------------------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 149 VCHGDPSVIKEGYKSFPSGHTSWSFAGLGFLSWYLagkmtafdRRGHVAKLCvvllpLLVAALVAVSRVDDYWHHWQDVC 228
Cdd:COG0671 104 VPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL--------PRRWLAALL-----LALALLVGLSRVYLGVHYPSDVL 170
|
170
....*....|....*..
gi 670389720 229 TGGVLGLVVASVCYLQF 245
Cdd:COG0671 171 AGALLGLAIALLLLALL 187
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
104-245 |
4.26e-06 |
|
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: 46.16 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 104 ILFAVLITGVLTDAIKDAVGRPRPNFYwrcFPDGeavynnittgvvCHG-DPSVIKEGYKSFPSGH--TSWSFAG-LGFL 179
Cdd:cd03389 74 LFATVALSGILVNLLKFIIGRARPKLL---FDDG------------LYGfDPFHADYAFTSFPSGHsaTAGAAAAaLALL 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670389720 180 swylagkmtaFDRRGHVAKLCVVLLpllvaalvAVSRVDDYWHHWQDVCTGGVLGLVVASVCYLQF 245
Cdd:cd03389 139 ----------FPRYRWAFILLALLI--------AFSRVIVGAHYPSDVIAGSLLGAVTALALYQRF 186
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
65-179 |
8.34e-03 |
|
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: 36.89 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670389720 65 NTVPVWAVPIIAVIGPVTIFAVVYIRRRnaydlhhaILGILFAVLITGVLTDAI-KDAVGRPRPNFYwrcfpdgeAVYNN 143
Cdd:cd03396 40 LLSIALAVLLLALALLFFRRKRLRRRRR--------ALLLLILVIGLGLLVVAIlKSHWGRPRPWDL--------TEFGG 103
|
90 100 110
....*....|....*....|....*....|....*...
gi 670389720 144 ITTGVVCHGDPSVIKEGYKSFPSGHTS--WSFAGLGFL 179
Cdd:cd03396 104 DAPYTPLFSGPSNGCGKGCSFPSGHASagFALLALYFL 141
|
|
| |
