|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
1-309 |
0e+00 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 580.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 1 MPEIQLGAHTVKSHGVKVARTHMHDWLILLLLIVIEVILNVIEPFHRFVGEDMMTDLRYPLKDNTVPFWAVPILAILLPF 80
Cdd:PLN02250 1 MPEIQLGAHTIRSHGVKVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 81 IVIIVYYFIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDGKGVFDPVTKDVMCTGLKSVIKEGH 160
Cdd:PLN02250 81 AVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTTDVLCTGAKSVIKEGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 161 KSFPSGHTSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFC 240
Cdd:PLN02250 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFC 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1965349704 241 YLQFFPAPYEVDGWGPHAYFQMLAESQN-----ANPSNANVQQSDLEGGYMDSQHERELLRVNTNDSSPILEGT 309
Cdd:PLN02250 241 YLQFFPPPYDIDGWGPHAYFQMLAESRNgaqssNGINHLSVQQTELESVYIDSQHGMETSRVNTRDTSPILEGL 314
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
55-244 |
1.79e-90 |
|
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: 267.93 E-value: 1.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 55 TDLRYPLKDN-TVPFWAVPILAILLPFIVIIVYY-FIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRC 132
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISlFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 133 FPDGKGVFD-PVTKDVMCTGLKSVIKEGHKSFPSGHTSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIVFLPLLIAALV 211
Cdd:cd03390 81 FPDGGTPSDtLVGIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 1965349704 212 GISRVDDYWHHWQDVFAGGLLGITVSSFCYLQF 244
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
103-245 |
6.27e-24 |
|
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: 94.41 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 103 LLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDgkgVFDPVTKDvmctglksvikEGHKSFPSGHTSWSFAGLGFLALYL 182
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL---VPAPSTLP-----------GLGYSFPSGHSATAFALALLLALLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1965349704 183 sgkirvfDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCYLQFF 245
Cdd:pfam01569 68 -------RRLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
108-241 |
9.16e-22 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 88.17 E-value: 9.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 108 LITGVITDSIKNAVGRPRPDFFWRCfpdgkgvfdpvtkDVMCTGLKSVIKEGHKSFPSGHTSWSFAGLGFLALYLsgkir 187
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIG-------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL----- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1965349704 188 vfdrRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCY 241
Cdd:smart00014 67 ----PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
68-244 |
5.01e-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: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 68 FWAVPILAILLPFIVIIVYYFIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDffwrcfpdgkgvfdpvtkdV 147
Cdd:COG0671 43 LLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF-------------------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 148 MCTGLKSVIKEGHKSFPSGHTSWSFAGLGFLALYLsgkirvfdrrghvAKLCIVFLPLLIAALVGISRVDDYWHHWQDVF 227
Cdd:COG0671 104 VPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL-------------PRRWLAALLLALALLVGLSRVYLGVHYPSDVL 170
|
170
....*....|....*..
gi 1965349704 228 AGGLLGITVSSFCYLQF 244
Cdd:COG0671 171 AGALLGLAIALLLLALL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
1-309 |
0e+00 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 580.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 1 MPEIQLGAHTVKSHGVKVARTHMHDWLILLLLIVIEVILNVIEPFHRFVGEDMMTDLRYPLKDNTVPFWAVPILAILLPF 80
Cdd:PLN02250 1 MPEIQLGAHTIRSHGVKVARTHMHDWLILLLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPLQDNTIPFWAVPLIAILLPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 81 IVIIVYYFIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDGKGVFDPVTKDVMCTGLKSVIKEGH 160
Cdd:PLN02250 81 AVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTTDVLCTGAKSVIKEGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 161 KSFPSGHTSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFC 240
Cdd:PLN02250 161 KSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFC 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1965349704 241 YLQFFPAPYEVDGWGPHAYFQMLAESQN-----ANPSNANVQQSDLEGGYMDSQHERELLRVNTNDSSPILEGT 309
Cdd:PLN02250 241 YLQFFPPPYDIDGWGPHAYFQMLAESRNgaqssNGINHLSVQQTELESVYIDSQHGMETSRVNTRDTSPILEGL 314
|
|
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
1-286 |
1.34e-144 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 410.57 E-value: 1.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 1 MPEIQLGAHTVKSHGVKVARTHMHDWLILLLLIVIEVILNVIEPFHRFVGEDMMTDLRYPLKDNTVPFWAVPILAILLPF 80
Cdd:PLN02731 20 MREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 81 IVIIVYYFIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDGKGVFDPVtKDVMCTGLKSVIKEGH 160
Cdd:PLN02731 100 VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSL-GDVICHGDKSVIREGH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 161 KSFPSGHTSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFC 240
Cdd:PLN02731 179 KSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTIC 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1965349704 241 YLQFFPAPYEVDGWGPHAYFQMLAESQNANPSNANVQQS--------DLEGGYM 286
Cdd:PLN02731 259 YLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQPppqvnngeEEDGGFM 312
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
1-280 |
1.77e-130 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 374.39 E-value: 1.77e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 1 MPEIQLGAHTVKSHGVKVARTHMHDWLILLLLIVIEVILNVIEPFHRFVGEDMMTDLRYPLKDNTVPFWAVPILAILLPF 80
Cdd:PLN02715 26 IQEIDLGVHTIKSHGGRVASKHKHDWIILVILIAIEIGLNLISPFYRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 81 IVIIVYYFIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDGKGVFDPVtKDVMCTGLKSVIKEGH 160
Cdd:PLN02715 106 ILFVCFYLKRRCVYDLHHSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDAL-GGVICHGKAAEVKEGH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 161 KSFPSGHTSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFC 240
Cdd:PLN02715 185 KSFPSGHTSWSFAGLTFLSLYLSGKIKAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFC 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1965349704 241 YLQFFPAPYEVDGWGPHAYFQMLAE-------SQNANPSNANVQQSD 280
Cdd:PLN02715 265 YRQFYPNPYHEEGWGPYAYFKAAQErgvpvasSQNGDALRAMSLQMD 311
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
55-244 |
1.79e-90 |
|
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: 267.93 E-value: 1.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 55 TDLRYPLKDN-TVPFWAVPILAILLPFIVIIVYY-FIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRC 132
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISlFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 133 FPDGKGVFD-PVTKDVMCTGLKSVIKEGHKSFPSGHTSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIVFLPLLIAALV 211
Cdd:cd03390 81 FPDGGTPSDtLVGIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 1965349704 212 GISRVDDYWHHWQDVFAGGLLGITVSSFCYLQF 244
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
104-239 |
1.49e-35 |
|
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: 125.82 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 104 LFSVLITGVITDSIKNAVGRPRPDFFWRCFPD-----GKGVFDPVTKDVMCTGLKSVIKEGHKSFPSGHTSWSFAGLGFL 178
Cdd:cd03384 10 LFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNytdltCSLDHQYIADCTCCTGDPDLIREARLSFPSGHASLSMYAAVFL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1965349704 179 ALYLSGkiRVFDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSF 239
Cdd:cd03384 90 ALYLQA--RLKLRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALF 148
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
96-241 |
2.99e-28 |
|
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: 105.62 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 96 LHHAILGLLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDGKgvfdpvtkdvmctglKSVIKEGHKSFPSGHTSWSFAGL 175
Cdd:cd01610 1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGD---------------PLLLTEGGYSFPSGHAAFAFALA 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965349704 176 GFLALYLsgkirvfdrRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCY 241
Cdd:cd01610 66 LFLALLL---------PRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
103-245 |
6.27e-24 |
|
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: 94.41 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 103 LLFSVLITGVITDSIKNAVGRPRPDFFWRCFPDgkgVFDPVTKDvmctglksvikEGHKSFPSGHTSWSFAGLGFLALYL 182
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL---VPAPSTLP-----------GLGYSFPSGHSATAFALALLLALLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1965349704 183 sgkirvfDRRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCYLQFF 245
Cdd:pfam01569 68 -------RRLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
108-241 |
9.16e-22 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 88.17 E-value: 9.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 108 LITGVITDSIKNAVGRPRPDFFWRCfpdgkgvfdpvtkDVMCTGLKSVIKEGHKSFPSGHTSWSFAGLGFLALYLsgkir 187
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIG-------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL----- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1965349704 188 vfdrRGHVAKLCIVFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCY 241
Cdd:smart00014 67 ----PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
43-245 |
4.51e-17 |
|
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: 77.65 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 43 EPFHRFVGEDMMTDLRYPLKDNTvpFWAVPILAILLPFIVIIVYYFIRRdvydlHHAILGLLFSVLITGVITDSIKNAVG 122
Cdd:cd03392 14 QSVLSLLRSLRTPLLTAFMTAIT--FLGSPAVLLIIVLLLALLLLLKRR-----RRAALFLLLALLGGGALNTLLKLLVQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 123 RPRPDFFWRCFPDGKgvfdpvtkdvmctglksvikeghkSFPSGHTSWSFAGLGFLALYLSGKIrvfdrRGHVAKLCIVF 202
Cdd:cd03392 87 RPRPPLHLLVPEGGY------------------------SFPSGHAMGATVLYGFLAYLLARRL-----PRRRVRILLLI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1965349704 203 LPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCYLQFF 245
Cdd:cd03392 138 LAAILILLVGLSRLYLGVHYPSDVLAGWLLGLAWLALLILLYR 180
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
68-244 |
5.01e-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: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 68 FWAVPILAILLPFIVIIVYYFIRRDVYDLHHAILGLLFSVLITGVITDSIKNAVGRPRPDffwrcfpdgkgvfdpvtkdV 147
Cdd:COG0671 43 LLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPF-------------------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 148 MCTGLKSVIKEGHKSFPSGHTSWSFAGLGFLALYLsgkirvfdrrghvAKLCIVFLPLLIAALVGISRVDDYWHHWQDVF 227
Cdd:COG0671 104 VPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL-------------PRRWLAALLLALALLVGLSRVYLGVHYPSDVL 170
|
170
....*....|....*..
gi 1965349704 228 AGGLLGITVSSFCYLQF 244
Cdd:COG0671 171 AGALLGLAIALLLLALL 187
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
103-241 |
7.40e-15 |
|
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: 69.28 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 103 LLFSVLITGVITDSIKNAVGRPRPDffwrcfpdgkgvfdpvtkdvmctglksVIKEGHKSFPSGHTSWSFAGLGFLALyl 182
Cdd:cd03394 8 LAEAAALTAAVTEGLKFAVGRARPD---------------------------GSNNGYRSFPSGHTASAFAAATFLQY-- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 183 sgkirvfdRRGHVAklciVFLPL-LIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCY 241
Cdd:cd03394 59 --------RYGWRW----YGIPAyALASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
103-244 |
9.39e-13 |
|
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: 65.81 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 103 LLFSVLITGVITDSIKNAVGRPRPDFFwrcFPDGKGVFDPVTkdvmctglksvIKEGHKSFPSGHTSWSFAGLGFLALyl 182
Cdd:cd03389 74 LFATVALSGILVNLLKFIIGRARPKLL---FDDGLYGFDPFH-----------ADYAFTSFPSGHSATAGAAAAALAL-- 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965349704 183 sgkirVFDRRGhvaklcivFLPLLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCYLQF 244
Cdd:cd03389 138 -----LFPRYR--------WAFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQRF 186
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
100-234 |
7.47e-09 |
|
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: 53.86 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 100 ILGLLFSVLITGVItdsiKNAVGRPRPdffWRCFPDgkgVFDPVTKDvmctglksvikegHKSFPSGHTSWSFAGLGFLA 179
Cdd:cd03391 53 LLGLLLDIITVAIL----KALVRRRRP---AYNSPD---MLDYVAVD-------------KYSFPSGHASRAAFVARFLL 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1965349704 180 LYLSgkirvfdrrghvakLCIVFLPLLI--AALVGISRVDDYWHHWQDVFAGGLLGI 234
Cdd:cd03391 110 NHLV--------------LAVPLRVLLVlwATVVGISRVLLGRHHVLDVLAGAFLGY 152
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
55-242 |
1.30e-08 |
|
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: 53.42 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 55 TDLRYPLKDNTVPFWAVPilAILLPFIVIIVYYFIRRDVYDLHHAILGLLFSVLIT-GVITDSIKNAVGRPRPdffwrCF 133
Cdd:cd03395 15 GTLVHPLLDDLMPFLTGK--KLSVPIFLLLALFILFRKGPIGLLILLLVLLAVGFAdQLASGFLKPLVARLRP-----CN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 134 PDGKGVfdpvtkdvmctgLKSVIKEGHK-SFPSGHTSWSFAGLGFLALYlsgkirvfdrrgHVAKLCIVFLpLLIAALVG 212
Cdd:cd03395 88 ALDGVR------------LVVLGDQGGSySFASSHAANSFALALFIWLF------------FRRGLFSPVL-LLWALLVG 142
|
170 180 190
....*....|....*....|....*....|
gi 1965349704 213 ISRVDDYWHHWQDVFAGGLLGITVSSFCYL 242
Cdd:cd03395 143 YSRVYVGVHYPGDVIAGALIGIISGLLFYL 172
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
77-241 |
5.06e-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: 51.51 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 77 LLPFIVIIVYY---FIRRDVYDLHhAILGLLFSVLITGVItdsiKNAVGRPRPDFFWRCFPDGKGvfdpvtkdvmctglk 153
Cdd:cd03382 23 LLPVAILVGYAtliLFRRELEAIY-LFIGLLANEALNYVL----KRIIKEPRPCSGAYFVRSGYG--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 154 svikeghksFPSGH--TSWSFAGLGFLALYLSGKIRVFDRRGHVAKLCIvflpLLIAALVGISRVDDYWHHWQDVFAGGL 231
Cdd:cd03382 83 ---------MPSSHsqFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGL----LLLALLVSYSRVYLGYHTVSQVVVGAI 149
|
170
....*....|
gi 1965349704 232 LGITVSSFCY 241
Cdd:cd03382 150 VGILLGILWF 159
|
|
| PAP2_like_1 |
cd03380 |
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ... |
86-236 |
4.75e-05 |
|
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases.
Pssm-ID: 239475 Cd Length: 209 Bit Score: 43.58 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 86 YYFIRRDVYDLH------HAILGLLFSVLIT--GVITDSIKNAVGRPRPdFFWrcfpdgkgvfDPVTKDVMCTGlkSVIK 157
Cdd:cd03380 73 YANAFSIALGTPglseerTPRLYALLARALTdaGIATWDAKYHYNRPRP-FVA----------IRLQWLPICTP--EEGT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 158 EGHKSFPSGHTswSFAGLGFLAL-YLSGkirvfDRRGHVAKLcivflplliAALVGISRVddywH---HWQ-DVFAGGLL 232
Cdd:cd03380 140 PKHPSYPSGHA--TFGGAAALVLaELFP-----ERAAELLAR---------AAEAGNSRV----VagvHWPsDVEAGRIL 199
|
....
gi 1965349704 233 GITV 236
Cdd:cd03380 200 GEAI 203
|
|
| COG3907 |
COG3907 |
Membrane-associated enzyme, PAP2 (acid phosphatase) superfamily [General function prediction ... |
58-248 |
1.78e-04 |
|
Membrane-associated enzyme, PAP2 (acid phosphatase) superfamily [General function prediction only];
Pssm-ID: 443113 Cd Length: 236 Bit Score: 42.19 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 58 RYPLKDNtvPFW------AVPILAILLPFIVIIVYYF-IRRDVYDLHHAILGLLFSVLITGVITDSI-KNAVGRPRPdff 129
Cdd:COG3907 50 QFPLRDN--WLLelllhdGGKWLVILVAVLLLLLLLAsFKRPRLRRYRRRLLYLLLSLALGLLVVSLlKSHTGRPCP--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 130 WRCFPDG-----KGVFDPVTKDvmctglksviKEGHKSFPSGHTSwsfAGLGFLALYLSGKirvfDRRGHVAKLCIVFlP 204
Cdd:COG3907 125 WDLVEFGgdapyVPLFEPGPAG----------AGPGRCFPAGHAS---AGFALLALYFLLR----RRRPRLARLGLAA-G 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1965349704 205 LLIAALVGISRVDDYWHHWQDVFAGGLLGITVSSFCYLQFFPAP 248
Cdd:COG3907 187 LALGLLMGLAQMLRGAHFLSHTLWSAWICWLVALLLYWLLLRRP 230
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
66-241 |
1.86e-04 |
|
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which mainly contains bacterial proteins, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239490 Cd Length: 197 Bit Score: 41.90 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 66 VPFWAVPILAILLPFIVIIVYYFIRRDVydLHHAILGLLFSVLITGVITDSI---KNAVGRPRP------------DFFW 130
Cdd:cd03396 34 LHLGGRLLSIALAVLLLALALLFFRRKR--LRRRRRALLLLILVIGLGLLVVailKSHWGRPRPwdltefggdapyTPLF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 131 RCFPDGKGvfdpvtkdvmctglksvikeGHKSFPSGHTSWSFAglgFLALYLSGKirvfDRRGHVAKLCIVFLpLLIAAL 210
Cdd:cd03396 112 SGPSNGCG--------------------KGCSFPSGHASAGFA---LLALYFLFR----RRRPRLARLVLAAG-LALGAL 163
|
170 180 190
....*....|....*....|....*....|.
gi 1965349704 211 VGISRVDDYWHHWQDVFAGGLLGITVSSFCY 241
Cdd:cd03396 164 MGLARMARGAHFLSDVLWSLLLVWLIALLLY 194
|
|
| PAP2_diacylglycerolkinase |
cd03383 |
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ... |
152-244 |
8.97e-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: 35.38 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965349704 152 LKSVIKEG---HKSFPSGHTSWSFAGLGFLALYLSGKIrvfdrrghvaklcIVFLPLLIAALVGISRVDDYWHHWQDVFA 228
Cdd:cd03383 27 LKAYFGRGtplEGGMPSGHAAIAFSIATAISLITNNPI-------------ISILSVLLAVMVAHSRVEMKIHTMWEVVV 93
|
90
....*....|....*.
gi 1965349704 229 GGLLGITVSSFCYLQF 244
Cdd:cd03383 94 GAILGALITLLIFKIF 109
|
|
| |
