|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
1-333 |
0e+00 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 664.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 1 MARFSFPCFPNFGGFNQHRMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPL 80
Cdd:PLN02731 1 MARFSFPCFPNFGGFNQHRMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 81 KSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYD 160
Cdd:PLN02731 81 KSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 161 SLGDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHH 240
Cdd:PLN02731 161 SLGDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 241 WQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQPPPQVNNGEEEDGGFMGLHLVDNP 320
Cdd:PLN02731 241 WQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQPPPQVNNGEEEDGGFMGLHLVDNP 320
|
330
....*....|...
gi 145331736 321 TMRREEDVETGRG 333
Cdd:PLN02731 321 TMRREEDVETGRG 333
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
74-262 |
1.47e-86 |
|
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: 258.69 E-value: 1.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 74 TDLSYPLKSN-TVPIWSVPVYAMLLPL-VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRC 151
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLlVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 152 FPDGKALYDSL--GDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALV 229
Cdd:cd03390 81 FPDGGTPSDTLvgIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 145331736 230 GISRVDDYWHHWQDVFAGGLLGLAISTICYLQF 262
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
122-263 |
4.27e-22 |
|
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: 89.79 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 122 LLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLgdvichgdksvirEGHKSFPSGHTSWSFSGLGFLSLYLS 201
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP-------------GLGYSFPSGHSATAFALALLLALLLR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145331736 202 GKIqafdgkgHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFF 263
Cdd:pfam01569 69 RLR-------KIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
127-259 |
3.80e-18 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 78.93 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 127 LVTAVLTDAIKNAVGRPRPDFFWRCfpdgkalydslgDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLsgkiqa 206
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIG------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL------ 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 145331736 207 fdgKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICY 259
Cdd:smart00014 67 ---PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
45-262 |
7.38e-15 |
|
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: 71.99 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 45 WIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLY 124
Cdd:COG0671 1 LLLALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 125 SVLVTAVLTDAIKNAVGRPRPDffwrcfpdgkalydslgdVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLsgki 204
Cdd:COG0671 81 LLLLLLLLLLLLKYLFGRPRPF------------------VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL---- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145331736 205 qafdgkghvAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQF 262
Cdd:COG0671 139 ---------PRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
1-333 |
0e+00 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 664.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 1 MARFSFPCFPNFGGFNQHRMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPL 80
Cdd:PLN02731 1 MARFSFPCFPNFGGFNQHRMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 81 KSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYD 160
Cdd:PLN02731 81 KSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 161 SLGDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHH 240
Cdd:PLN02731 161 SLGDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 241 WQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQPPPQVNNGEEEDGGFMGLHLVDNP 320
Cdd:PLN02731 241 WQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQPPPQVNNGEEEDGGFMGLHLVDNP 320
|
330
....*....|...
gi 145331736 321 TMRREEDVETGRG 333
Cdd:PLN02731 321 TMRREEDVETGRG 333
|
|
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
20-291 |
7.16e-171 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 477.11 E-value: 7.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 20 MREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPL 99
Cdd:PLN02250 1 MPEIQLGAHTIRSHGVKVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 100 VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSL-GDVICHGDKSVIREGH 178
Cdd:PLN02250 81 AVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVtTDVLCTGAKSVIKEGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 179 KSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTIC 258
Cdd:PLN02250 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFC 240
|
250 260 270
....*....|....*....|....*....|....*
gi 145331736 259 YLQFFPPPYHTEGWGPYAYFQVLEAAR--VQGAAN 291
Cdd:PLN02250 241 YLQFFPPPYDIDGWGPHAYFQMLAESRngAQSSNG 275
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
19-282 |
1.35e-142 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 405.98 E-value: 1.35e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 19 RMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLP 98
Cdd:PLN02715 25 RIQEIDLGVHTIKSHGGRVASKHKHDWIILVILIAIEIGLNLISPFYRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 99 LVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLGDVICHGDKSVIREGH 178
Cdd:PLN02715 105 IILFVCFYLKRRCVYDLHHSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDALGGVICHGKAAEVKEGH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 179 KSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTIC 258
Cdd:PLN02715 185 KSFPSGHTSWSFAGLTFLSLYLSGKIKAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFC 264
|
250 260
....*....|....*....|....
gi 145331736 259 YLQFFPPPYHTEGWGPYAYFQVLE 282
Cdd:PLN02715 265 YRQFYPNPYHEEGWGPYAYFKAAQ 288
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
74-262 |
1.47e-86 |
|
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: 258.69 E-value: 1.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 74 TDLSYPLKSN-TVPIWSVPVYAMLLPL-VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRC 151
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLlVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 152 FPDGKALYDSL--GDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALV 229
Cdd:cd03390 81 FPDGGTPSDTLvgIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 145331736 230 GISRVDDYWHHWQDVFAGGLLGLAISTICYLQF 262
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
123-255 |
1.57e-31 |
|
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: 115.81 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 123 LYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLG------DVICHGDKSVIREGHKSFPSGHTSWSFSGLGFL 196
Cdd:cd03384 10 LFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNYTDLTCSLDhqyiadCTCCTGDPDLIREARLSFPSGHASLSMYAAVFL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 145331736 197 SLYLSGKIQAFDGKghVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAIS 255
Cdd:cd03384 90 ALYLQARLKLRGSR--LLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIA 146
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
115-259 |
3.01e-26 |
|
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: 101.00 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 115 LHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGkalydslgdvichgDKSVIREGHKSFPSGHTSWSFSGLG 194
Cdd:cd01610 1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG--------------DPLLLTEGGYSFPSGHAAFAFALAL 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145331736 195 FLSLYLsgkiqafdgKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICY 259
Cdd:cd01610 67 FLALLL---------PRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
122-263 |
4.27e-22 |
|
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: 89.79 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 122 LLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLgdvichgdksvirEGHKSFPSGHTSWSFSGLGFLSLYLS 201
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP-------------GLGYSFPSGHSATAFALALLLALLLR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145331736 202 GKIqafdgkgHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFF 263
Cdd:pfam01569 69 RLR-------KIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
127-259 |
3.80e-18 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 78.93 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 127 LVTAVLTDAIKNAVGRPRPDFFWRCfpdgkalydslgDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLsgkiqa 206
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIG------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL------ 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 145331736 207 fdgKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICY 259
Cdd:smart00014 67 ---PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
91-263 |
6.32e-16 |
|
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: 74.57 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 91 PVYAMLLPLVIFIFIYFRRRdvydlHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKalydslgdvichgd 170
Cdd:cd03392 41 PAVLLIIVLLLALLLLLKRR-----RRAALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVPEGGY-------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 171 ksvireghkSFPSGHTSWSFSGLGFLSLYLSGKIqafdgKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLL 250
Cdd:cd03392 102 ---------SFPSGHAMGATVLYGFLAYLLARRL-----PRRRVRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLL 167
|
170
....*....|...
gi 145331736 251 GLAISTICYLQFF 263
Cdd:cd03392 168 GLAWLALLILLYR 180
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
45-262 |
7.38e-15 |
|
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: 71.99 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 45 WIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLY 124
Cdd:COG0671 1 LLLALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 125 SVLVTAVLTDAIKNAVGRPRPDffwrcfpdgkalydslgdVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLsgki 204
Cdd:COG0671 81 LLLLLLLLLLLLKYLFGRPRPF------------------VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL---- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145331736 205 qafdgkghvAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQF 262
Cdd:COG0671 139 ---------PRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALL 187
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
122-259 |
6.29e-13 |
|
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: 64.27 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 122 LLYSVLVTAVLTDAIKNAVGRPRPDffwrcfpdgkalydslgdvichGDksviREGHKSFPSGHTSWSFSGLGFLSlYLS 201
Cdd:cd03394 8 LAEAAALTAAVTEGLKFAVGRARPD----------------------GS----NNGYRSFPSGHTASAFAAATFLQ-YRY 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 145331736 202 GKIQAFdgkghvaklciviLPL-LFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICY 259
Cdd:cd03394 61 GWRWYG-------------IPAyALASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
86-262 |
1.95e-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: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 86 PIWSVPVYAMLLPLVIFIFIYFRRrdvydLHHAVLGLLySVLVTAVLTD-----AIKNAVGRPRPdffwrCFPDGKALYD 160
Cdd:cd03395 27 PFLTGKKLSVPIFLLLALFILFRK-----GPIGLLILL-LVLLAVGFADqlasgFLKPLVARLRP-----CNALDGVRLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 161 SLGDvichgdksviREGHKSFPSGHTSWSFSGLGFLSLYlsgkiqafdgkgHVAKLCIVILpLLFAALVGISRVDDYWHH 240
Cdd:cd03395 96 VLGD----------QGGSYSFASSHAANSFALALFIWLF------------FRRGLFSPVL-LLWALLVGYSRVYVGVHY 152
|
170 180
....*....|....*....|..
gi 145331736 241 WQDVFAGGLLGLAISTICYLQF 262
Cdd:cd03395 153 PGDVIAGALIGIISGLLFYLLF 174
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
92-262 |
1.18e-07 |
|
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: 51.17 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 92 VYAMLLPLVIFIFIYFR------RRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFwrcFPDGkalydSLGDV 165
Cdd:cd03389 38 LIPSLLLFLLFRFGDLRglsapsRARFPKAAWAGLFLFATVALSGILVNLLKFIIGRARPKLL---FDDG-----LYGFD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 166 ICHGDksvirEGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFdgkghvaklcivilpLLFAALVGISRVDDYWHHWQDVF 245
Cdd:cd03389 110 PFHAD-----YAFTSFPSGHSATAGAAAAALALLFPRYRWAF---------------ILLALLIAFSRVIVGAHYPSDVI 169
|
170
....*....|....*..
gi 145331736 246 AGGLLGLAISTICYLQF 262
Cdd:cd03389 170 AGSLLGAVTALALYQRF 186
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
119-252 |
9.32e-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: 48.08 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 119 VLGLLYSVLVTAVLtdaiKNAVGRPRPdffwrcfpdgkaLYDSLGDVICHG-DksviregHKSFPSGHTSWSFSGLGFLS 197
Cdd:cd03391 53 LLGLLLDIITVAIL----KALVRRRRP------------AYNSPDMLDYVAvD-------KYSFPSGHASRAAFVARFLL 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 145331736 198 LYLsgkiqafdgkghVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGL 252
Cdd:cd03391 110 NHL------------VLAVPLRVLLVLWATVVGISRVLLGRHHVLDVLAGAFLGY 152
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
100-259 |
5.70e-05 |
|
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: 43.44 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 100 VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAI---KNAVGRPRP----DFfwrcfpDGKALYDSLGDVICHGDKs 172
Cdd:cd03396 47 VLLLALALLFFRRKRLRRRRRALLLLILVIGLGLLVVailKSHWGRPRPwdltEF------GGDAPYTPLFSGPSNGCG- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 173 vireGHKSFPSGHTSWSFSglgFLSLYLSGKIQAFDGkghvAKLCIVILpLLFAALVGISRVDDYWHHWQDVFAGGLLGL 252
Cdd:cd03396 120 ----KGCSFPSGHASAGFA---LLALYFLFRRRRPRL----ARLVLAAG-LALGALMGLARMARGAHFLSDVLWSLLLVW 187
|
....*..
gi 145331736 253 AISTICY 259
Cdd:cd03396 188 LIALLLY 194
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
93-259 |
6.30e-05 |
|
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: 42.65 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 93 YAMLLPLVIFIFIY---FRRRDVYDLHhAVLGLLYSVLVTAVLtdaiKNAVGRPRPDFFwrcfpdgkalydslgdvichg 169
Cdd:cd03382 20 YLSLLPVAILVGYAtliLFRRELEAIY-LFIGLLANEALNYVL----KRIIKEPRPCSG--------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 170 dKSVIREGHkSFPSGH--TSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILpllfAALVGISRVDDYWHHWQDVFAG 247
Cdd:cd03382 74 -AYFVRSGY-GMPSSHsqFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLL----ALLVSYSRVYLGYHTVSQVVVG 147
|
170
....*....|..
gi 145331736 248 GLLGLAISTICY 259
Cdd:cd03382 148 AIVGILLGILWF 159
|
|
| PAP2_diacylglycerolkinase |
cd03383 |
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ... |
182-262 |
5.64e-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: 38.85 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 182 PSGHTSWSFSGLGFLSLYLSGKIqafdgkghvaklcIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQ 261
Cdd:cd03383 42 PSGHAAIAFSIATAISLITNNPI-------------ISILSVLLAVMVAHSRVEMKIHTMWEVVVGAILGALITLLIFKI 108
|
.
gi 145331736 262 F 262
Cdd:cd03383 109 F 109
|
|
| PAP2_like_1 |
cd03380 |
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ... |
127-254 |
9.65e-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: 36.64 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331736 127 LVTAVLTDAI------KNAVGRPRPdFFWrcfpdgkalYDSLGDVIChgDKSVIREGHKSFPSGHTswSFSGLGFLSL-Y 199
Cdd:cd03380 97 LLARALTDAGiatwdaKYHYNRPRP-FVA---------IRLQWLPIC--TPEEGTPKHPSYPSGHA--TFGGAAALVLaE 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 145331736 200 LSGkiQAFDgkghvaklcivilPLL-FAALVGISRVddyWH--HWQ-DVFAGGLLGLAI 254
Cdd:cd03380 163 LFP--ERAA-------------ELLaRAAEAGNSRV---VAgvHWPsDVEAGRILGEAI 203
|
|
| |
