|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
1-290 |
0e+00 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 591.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 1 MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPF 80
Cdd:PLN02250 1 MPEIQLGAHTIRSHGVKVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 81 AVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFHNVTKNVLCTGAKDVVKEGH 160
Cdd:PLN02250 81 AVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTTDVLCTGAKSVIKEGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFC 240
Cdd:PLN02250 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFC 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 28393050 241 YLQFFPPPYDPDGWGPHAYFQMLADSRNDVQDSAGMNHLSVRQTELESVR 290
Cdd:PLN02250 241 YLQFFPPPYDIDGWGPHAYFQMLAESRNGAQSSNGINHLSVQQTELESVY 290
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
55-244 |
2.26e-88 |
|
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: 261.39 E-value: 2.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 55 TDLRYPLQDN-TIPFWAVPLIAVVLPFAVICVYY-FIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRC 132
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISlFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 133 FPDGIGIFH-NVTKNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALV 211
Cdd:cd03390 81 FPDGGTPSDtLVGIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 28393050 212 GVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQF 244
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
103-245 |
4.98e-23 |
|
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: 91.33 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 103 LLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDgigifhnvtknvlcTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYL 182
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL--------------VPAPSTLPGLGYSFPSGHSATAFALALLLALLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28393050 183 sgkirvfDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQFF 245
Cdd:pfam01569 68 -------RRLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
108-241 |
9.70e-18 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 77.00 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 108 LITGVITDAIKDAVGRPRPDFFWRCfpdgigifhnvtkNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLsgkir 187
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIG-------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL----- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 28393050 188 vfdqRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCY 241
Cdd:smart00014 67 ----PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
66-244 |
1.97e-13 |
|
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: 67.37 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 66 IPFWAVPLIAVVLPFAVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDffwrcfpdgigifhnvtk 145
Cdd:COG0671 41 LALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF------------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 146 nVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLsgkirvfdqrghvAKLCIVILPLLVAALVGVSRVDDYWHHWQD 225
Cdd:COG0671 103 -VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL-------------PRRWLAALLLALALLVGLSRVYLGVHYPSD 168
|
170
....*....|....*....
gi 28393050 226 VFGGAIIGLTVATFCYLQF 244
Cdd:COG0671 169 VLAGALLGLAIALLLLALL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
1-290 |
0e+00 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 591.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 1 MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPF 80
Cdd:PLN02250 1 MPEIQLGAHTIRSHGVKVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 81 AVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFHNVTKNVLCTGAKDVVKEGH 160
Cdd:PLN02250 81 AVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTTDVLCTGAKSVIKEGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFC 240
Cdd:PLN02250 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFC 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 28393050 241 YLQFFPPPYDPDGWGPHAYFQMLADSRNDVQDSAGMNHLSVRQTELESVR 290
Cdd:PLN02250 241 YLQFFPPPYDIDGWGPHAYFQMLAESRNGAQSSNGINHLSVQQTELESVY 290
|
|
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
1-267 |
7.62e-133 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 379.76 E-value: 7.62e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 1 MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPF 80
Cdd:PLN02731 20 MREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 81 AVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFHNVtKNVLCTGAKDVVKEGH 160
Cdd:PLN02731 100 VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSL-GDVICHGDKSVIREGH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFC 240
Cdd:PLN02731 179 KSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTIC 258
|
250 260
....*....|....*....|....*..
gi 28393050 241 YLQFFPPPYDPDGWGPHAYFQMLADSR 267
Cdd:PLN02731 259 YLQFFPPPYHTEGWGPYAYFQVLEAAR 285
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
1-288 |
1.08e-124 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 358.98 E-value: 1.08e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 1 MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPF 80
Cdd:PLN02715 26 IQEIDLGVHTIKSHGGRVASKHKHDWIILVILIAIEIGLNLISPFYRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 81 AVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFhNVTKNVLCTGAKDVVKEGH 160
Cdd:PLN02715 106 ILFVCFYLKRRCVYDLHHSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELY-DALGGVICHGKAAEVKEGH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFC 240
Cdd:PLN02715 185 KSFPSGHTSWSFAGLTFLSLYLSGKIKAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFC 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 28393050 241 YLQFFPPPYDPDGWGPHAYFQMLADSRNDVQDSAGMNHLSVRQTELES 288
Cdd:PLN02715 265 YRQFYPNPYHEEGWGPYAYFKAAQERGVPVASSQNGDALRAMSLQMDS 312
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
55-244 |
2.26e-88 |
|
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: 261.39 E-value: 2.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 55 TDLRYPLQDN-TIPFWAVPLIAVVLPFAVICVYY-FIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRC 132
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISlFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 133 FPDGIGIFH-NVTKNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALV 211
Cdd:cd03390 81 FPDGGTPSDtLVGIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 28393050 212 GVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQF 244
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
104-239 |
1.05e-33 |
|
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: 120.04 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 104 LFSVLITGVITDAIKDAVGRPRPDFFWRCFPD----GIGIFHNVTKN-VLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFL 178
Cdd:cd03384 10 LFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNytdlTCSLDHQYIADcTCCTGDPDLIREARLSFPSGHASLSMYAAVFL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28393050 179 SLYLSGkiRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATF 239
Cdd:cd03384 90 ALYLQA--RLKLRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALF 148
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
96-241 |
6.03e-27 |
|
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: 101.77 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 96 LHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGigifhnvtknvlctgAKDVVKEGHKSFPSGHTSWSFAGL 175
Cdd:cd01610 1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG---------------DPLLLTEGGYSFPSGHAAFAFALA 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28393050 176 GFLSLYLsgkirvfdqRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCY 241
Cdd:cd01610 66 LFLALLL---------PRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
103-245 |
4.98e-23 |
|
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: 91.33 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 103 LLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDgigifhnvtknvlcTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYL 182
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL--------------VPAPSTLPGLGYSFPSGHSATAFALALLLALLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28393050 183 sgkirvfDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQFF 245
Cdd:pfam01569 68 -------RRLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
108-241 |
9.70e-18 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 77.00 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 108 LITGVITDAIKDAVGRPRPDFFWRCfpdgigifhnvtkNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLsgkir 187
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIG-------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL----- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 28393050 188 vfdqRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCY 241
Cdd:smart00014 67 ----PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
74-245 |
9.75e-15 |
|
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: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 74 IAVVLPFAVICVYYFIRNDVYdlhhAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIgifhnvtknvlctgak 153
Cdd:cd03392 42 AVLLIIVLLLALLLLLKRRRR----AALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVPEGGY---------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 154 dvvkeghkSFPSGHTSWSFAGLGFLSLYLSGKIrvfdqRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIG 233
Cdd:cd03392 102 --------SFPSGHAMGATVLYGFLAYLLARRL-----PRRRVRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLLG 168
|
170
....*....|..
gi 28393050 234 LTVATFCYLQFF 245
Cdd:cd03392 169 LAWLALLILLYR 180
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
103-241 |
2.15e-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: 67.74 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 103 LLFSVLITGVITDAIKDAVGRPRPDffwrcfpdgigifhnvtknvlctGAKDvvkeGHKSFPSGHTSWSFAGLGFLSlYL 182
Cdd:cd03394 8 LAEAAALTAAVTEGLKFAVGRARPD-----------------------GSNN----GYRSFPSGHTASAFAAATFLQ-YR 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 183 SGKIRVFdqrghvaklciviLPL-LVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCY 241
Cdd:cd03394 60 YGWRWYG-------------IPAyALASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
66-244 |
1.97e-13 |
|
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: 67.37 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 66 IPFWAVPLIAVVLPFAVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDffwrcfpdgigifhnvtk 145
Cdd:COG0671 41 LALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF------------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 146 nVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLsgkirvfdqrghvAKLCIVILPLLVAALVGVSRVDDYWHHWQD 225
Cdd:COG0671 103 -VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL-------------PRRWLAALLLALALLVGLSRVYLGVHYPSD 168
|
170
....*....|....*....
gi 28393050 226 VFGGAIIGLTVATFCYLQF 244
Cdd:COG0671 169 VLAGALLGLAIALLLLALL 187
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
55-244 |
1.57e-09 |
|
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: 56.12 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 55 TDLRYPLQDNTIPFWAVPLIAVVLPFAVICVYYFIRNDVYDLhhAILGLLFSVLIT-GVITDAIKDAVGRPRPdffwrCF 133
Cdd:cd03395 15 GTLVHPLLDDLMPFLTGKKLSVPIFLLLALFILFRKGPIGLL--ILLLVLLAVGFAdQLASGFLKPLVARLRP-----CN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 134 PDGIGIFHNVtknvlctgakdVVKEGHKSFPSGHTSWSFAGLGFLSLYlsgkirvfdqrgHVAKLCIVILpLLVAALVGV 213
Cdd:cd03395 88 ALDGVRLVVL-----------GDQGGSYSFASSHAANSFALALFIWLF------------FRRGLFSPVL-LLWALLVGY 143
|
170 180 190
....*....|....*....|....*....|.
gi 28393050 214 SRVDDYWHHWQDVFGGAIIGLTVATFCYLQF 244
Cdd:cd03395 144 SRVYVGVHYPGDVIAGALIGIISGLLFYLLF 174
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
103-244 |
2.92e-09 |
|
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: 55.40 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 103 LLFSVLITGVITDAIKDAVGRPRPDFFwrcFPDGIGIFHNVTKNVLCTgakdvvkeghkSFPSGHTSWSFAGLGFLSLyl 182
Cdd:cd03389 74 LFATVALSGILVNLLKFIIGRARPKLL---FDDGLYGFDPFHADYAFT-----------SFPSGHSATAGAAAAALAL-- 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28393050 183 sgkirVFDQRGHVAklcivilpLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQF 244
Cdd:cd03389 138 -----LFPRYRWAF--------ILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQRF 186
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
100-234 |
4.80e-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: 45.77 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 100 ILGLLFSVLITGVItdaiKDAVGRPRPdffwrcfpdgigiFHNVTKNVLCTGAKdvvkegHKSFPSGHTSWSFAGLGFLS 179
Cdd:cd03391 53 LLGLLLDIITVAIL----KALVRRRRP-------------AYNSPDMLDYVAVD------KYSFPSGHASRAAFVARFLL 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 28393050 180 LYLsgkirvfdqrghVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGL 234
Cdd:cd03391 110 NHL------------VLAVPLRVLLVLWATVVGISRVLLGRHHVLDVLAGAFLGY 152
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
163-241 |
1.10e-04 |
|
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: 41.88 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 163 FPSGH--TSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIvilpLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFC 240
Cdd:cd03382 83 MPSSHsqFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGL----LLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILW 158
|
.
gi 28393050 241 Y 241
Cdd:cd03382 159 F 159
|
|
| PAP2_like_3 |
cd03393 |
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
76-237 |
1.93e-03 |
|
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: 37.35 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 76 VVLPFAVICVyyfirnDVYDLHHAILGLLFSvlitGVITDAIKDAVGRPRPDFfwrcfPDGIGIFHNVTknvlctgakdv 155
Cdd:cd03393 1 IVLSLIYWLV------DKRLGRYLGLALCAS----GYLNAALKEVFKIPRPFT-----YDGIQAIYEES----------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 156 vkEGHKSFPSGHTSWSFAGLGFLSLylsgkirvfdqrgHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLT 235
Cdd:cd03393 55 --AGGYGFPSGHAQTSATFWGSLML-------------HVRKKWFTLIGVVLVVLISFSRLYLGVHWPSDVIGGVLIGLL 119
|
..
gi 28393050 236 VA 237
Cdd:cd03393 120 VL 121
|
|
| PAP2_like_1 |
cd03380 |
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ... |
58-237 |
2.78e-03 |
|
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: 38.18 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 58 RYPLQDNTIPFWAVPLIAVVLpfavicvYYFIRNDVYDLH------HAILGLLFSVLIT--GVITDAIKDAVGRPRPdFF 129
Cdd:cd03380 52 RTTAQTALAAFDADGGDPPPH-------YANAFSIALGTPglseerTPRLYALLARALTdaGIATWDAKYHYNRPRP-FV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 130 WRCFPDgigifhnvtkNVLCTGakDVVKEGHKSFPSGHTSWSFAGLGFLSlYLSGkirvfDQRGHVAKLcivilpllvAA 209
Cdd:cd03380 124 AIRLQW----------LPICTP--EEGTPKHPSYPSGHATFGGAAALVLA-ELFP-----ERAAELLAR---------AA 176
|
170 180 190
....*....|....*....|....*....|.
gi 28393050 210 LVGVSRVddyWH--HWQ-DVFGGAIIGLTVA 237
Cdd:cd03380 177 EAGNSRV---VAgvHWPsDVEAGRILGEAIA 204
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
66-216 |
3.09e-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: 38.05 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 66 IPFWAVPLIAVVLPFAVICVYYFIRNDVydLHHAILGLLFSVLITGVITDAI---KDAVGRPRP----DF-----FWRCF 133
Cdd:cd03396 34 LHLGGRLLSIALAVLLLALALLFFRRKR--LRRRRRALLLLILVIGLGLLVVailKSHWGRPRPwdltEFggdapYTPLF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28393050 134 PDGIGIFHnvtknvlctgakdvvkeGHKSFPSGHTSWSFAglgFLSLYLSGKIRvfdqRGHVAKLCIVILpLLVAALVGV 213
Cdd:cd03396 112 SGPSNGCG-----------------KGCSFPSGHASAGFA---LLALYFLFRRR----RPRLARLVLAAG-LALGALMGL 166
|
...
gi 28393050 214 SRV 216
Cdd:cd03396 167 ARM 169
|
|
| |
