|
Name |
Accession |
Description |
Interval |
E-value |
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
126-272 |
1.60e-66 |
|
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: 205.17 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 126 ALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSvGYIQNYR----CRGEDSKVQEARKSFFSGHA 201
Cdd:cd03384 1 RLYRFVGVFLFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNYTDLTCS-LDHQYIAdctcCTGDPDLIREARLSFPSGHA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497984 202 SFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIV 272
Cdd:cd03384 80 SLSMYAAVFLALYLQARLKLRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALFLV 150
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
135-272 |
1.11e-32 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 117.06 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 135 LFGCAISQSFTDIAKVSIGRLRPHFLnvcnpdfsqincsvgYIQNYRCRGEDSKVQEARKSFFSGHASFSMYTMLYLVLY 214
Cdd:smart00014 1 ALLAVVSQLFNGVIKNYFGRPRPFFL---------------SIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLY 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 115497984 215 LQARFTWRgarllrpLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIV 272
Cdd:smart00014 66 LPARAGRK-------LLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
133-275 |
3.40e-20 |
|
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: 84.39 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 133 CFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQIncsvgyiqnyrcrgedSKVQEARKSFFSGHASFSMYTMLYLV 212
Cdd:pfam01569 1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAP----------------STLPGLGYSFPSGHSATAFALALLLA 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115497984 213 LYLQARFTWrgarlLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFV 275
Cdd:pfam01569 65 LLLRRLRKI-----VRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLV 122
|
|
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
49-274 |
3.97e-20 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 88.83 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 49 LPFIIIET--STIKPYHRgFYCND--ESIKYPQKTgETINDAVLTAVGIVIAILAIItgefyrIYYLkeksrstIQNPyV 124
Cdd:PLN02250 30 LLLVVIEVvlNVIEPFHR-FVGKDmlTDLSYPLQD-NTIPFWAVPLIAILLPFAVIL------VYYF-------IRRD-V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 125 AALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSVgyIQNYRCRGEDSKVQEARKSFFSGHASFS 204
Cdd:PLN02250 94 YDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPV--TTDVLCTGAKSVIKEGHKSFPSGHTSWS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115497984 205 MYTMLYLVLYLQAR---FTWRGaRLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVA--CCIVFF 274
Cdd:PLN02250 172 FAGLGFLSLYLSGKirvFDRRG-HVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVAsfCYLQFF 245
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
195-275 |
2.05e-10 |
|
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: 58.90 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 195 SFFSGHASFSMytMLYLVLYLqarftwrgaRLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFF 274
Cdd:COG0671 118 SFPSGHAAAAF--ALALVLAL---------LLPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
|
.
gi 115497984 275 V 275
Cdd:COG0671 187 L 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
126-272 |
1.60e-66 |
|
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: 205.17 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 126 ALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSvGYIQNYR----CRGEDSKVQEARKSFFSGHA 201
Cdd:cd03384 1 RLYRFVGVFLFGLFATQLLTDLGKYVTGRLRPHFLDVCKPNYTDLTCS-LDHQYIAdctcCTGDPDLIREARLSFPSGHA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497984 202 SFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIV 272
Cdd:cd03384 80 SLSMYAAVFLALYLQARLKLRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALFLV 150
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
72-273 |
3.25e-34 |
|
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: 123.48 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 72 SIKYPQKTGETINDAVLTAVGIVIAILAIITGEFYRIYYLKEksrstiqnpyvaaLYKQVGCFLFGCAISQSFTDIAKVS 151
Cdd:cd03390 2 SISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWD-------------LHTSLLGLLLSVSLNGVITNVLKNY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 152 IGRLRPHFLNVCNPDfSQINCSVGYIQNYRCRGEDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTW--RGARLLRP 229
Cdd:cd03390 69 AGRPRPDFLARCFPD-GGTPSDTLVGIDICCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIfdPRGSSWRL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 115497984 230 LLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVF 273
Cdd:cd03390 148 LLALLPLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYR 191
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
135-272 |
1.11e-32 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 117.06 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 135 LFGCAISQSFTDIAKVSIGRLRPHFLnvcnpdfsqincsvgYIQNYRCRGEDSKVQEARKSFFSGHASFSMYTMLYLVLY 214
Cdd:smart00014 1 ALLAVVSQLFNGVIKNYFGRPRPFFL---------------SIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLY 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 115497984 215 LQARFTWRgarllrpLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIV 272
Cdd:smart00014 66 LPARAGRK-------LLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
131-269 |
5.85e-24 |
|
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: 94.45 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 131 VGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSqincsvgyiqnyrcrgeDSKVQEARKSFFSGHASFSMYTMLY 210
Cdd:cd01610 5 ALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGD-----------------PLLLTEGGYSFPSGHAAFAFALALF 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 115497984 211 LVLYLqarftwrGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVAC 269
Cdd:cd01610 68 LALLL-------PRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVAL 119
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
133-275 |
3.40e-20 |
|
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: 84.39 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 133 CFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQIncsvgyiqnyrcrgedSKVQEARKSFFSGHASFSMYTMLYLV 212
Cdd:pfam01569 1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAP----------------STLPGLGYSFPSGHSATAFALALLLA 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115497984 213 LYLQARFTWrgarlLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFV 275
Cdd:pfam01569 65 LLLRRLRKI-----VRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLV 122
|
|
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
49-274 |
3.97e-20 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 88.83 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 49 LPFIIIET--STIKPYHRgFYCND--ESIKYPQKTgETINDAVLTAVGIVIAILAIItgefyrIYYLkeksrstIQNPyV 124
Cdd:PLN02250 30 LLLVVIEVvlNVIEPFHR-FVGKDmlTDLSYPLQD-NTIPFWAVPLIAILLPFAVIL------VYYF-------IRRD-V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 125 AALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSVgyIQNYRCRGEDSKVQEARKSFFSGHASFS 204
Cdd:PLN02250 94 YDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPV--TTDVLCTGAKSVIKEGHKSFPSGHTSWS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115497984 205 MYTMLYLVLYLQAR---FTWRGaRLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVA--CCIVFF 274
Cdd:PLN02250 172 FAGLGFLSLYLSGKirvFDRRG-HVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVAsfCYLQFF 245
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
52-268 |
1.33e-17 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 81.64 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 52 IIIETSTIKPYHRgfYCNDE---SIKYPQKTgetiNDAVLTAVGIVIAILAIITgefYRIYYLKEKSrstiqnpyVAALY 128
Cdd:PLN02715 60 IEIGLNLISPFYR--YVGKDmmtDLKYPFKD----NTVPIWSVPVYAVLLPIIL---FVCFYLKRRC--------VYDLH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 129 KQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSVGYIQnyrCRGEDSKVQEARKSFFSGHASFSMYTM 208
Cdd:PLN02715 123 HSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDALGGVI---CHGKAAEVKEGHKSFPSGHTSWSFAGL 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115497984 209 LYLVLYLQAR---FTWRGARLLRPLLQFTLiMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVA 268
Cdd:PLN02715 200 TFLSLYLSGKikaFNGEGHVAKLCLVIFPL-LAACLVGISRVDDYWHHWQDVFAGALIGILVA 261
|
|
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
59-274 |
4.89e-15 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 74.30 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 59 IKPYHRgFYCND--ESIKYPQKTgetiNDAVLTAVGIVIAILAIITgeFYRIYYLKEKsrstiqnpyVAALYKQVGCFLF 136
Cdd:PLN02731 61 IHPFYR-FVGKDmmTDLSYPLKS----NTVPIWSVPVYAMLLPLVI--FIFIYFRRRD---------VYDLHHAVLGLLY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 137 GCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSVGyiqNYRCRGEDSKVQEARKSFFSGHASFSMYTMLYLVLYLQ 216
Cdd:PLN02731 125 SVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLG---DVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLS 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115497984 217 AR---FTWRG--ARLLRPLLQftlIMMAFYTGLSRVSDHKHHPSDVLAGFAQG--ALVACCIVFF 274
Cdd:PLN02731 202 GKiqaFDGKGhvAKLCIVILP---LLFAALVGISRVDDYWHHWQDVFAGGLLGlaISTICYLQFF 263
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
87-274 |
9.19e-13 |
|
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: 65.32 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 87 VLTAVG---IVIAILAIITGEFYRIYYlkeksrstiqnpYVAALYkqvgcFLFGCAISQSFTDIAKVSIGRLRPHFLNVC 163
Cdd:cd03392 34 AITFLGspaVLLIIVLLLALLLLLKRR------------RRAALF-----LLLALLGGGALNTLLKLLVQRPRPPLHLLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 164 NPDfsqincsvGYiqnyrcrgedskvqearkSFFSGHASFSMytMLYLVL-YLQARFTWRgaRLLRPLLQFTLIMMAFYT 242
Cdd:cd03392 97 PEG--------GY------------------SFPSGHAMGAT--VLYGFLaYLLARRLPR--RRVRILLLILAAILILLV 146
|
170 180 190
....*....|....*....|....*....|...
gi 115497984 243 GLSRVSDHKHHPSDVLAGFAQG-ALVACCIVFF 274
Cdd:cd03392 147 GLSRLYLGVHYPSDVLAGWLLGlAWLALLILLY 179
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
195-275 |
2.05e-10 |
|
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: 58.90 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 195 SFFSGHASFSMytMLYLVLYLqarftwrgaRLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFF 274
Cdd:COG0671 118 SFPSGHAAAAF--ALALVLAL---------LLPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
|
.
gi 115497984 275 V 275
Cdd:COG0671 187 L 187
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
134-268 |
5.88e-09 |
|
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: 52.72 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 134 FLFGCAISQSFTDIAKVSIGRLRPhflnvcnpdfsqincsVGYIQNYRcrgedskvqearkSFFSGHAS--FSMYTMLyl 211
Cdd:cd03394 8 LAEAAALTAAVTEGLKFAVGRARP----------------DGSNNGYR-------------SFPSGHTAsaFAAATFL-- 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 115497984 212 vlylQARFTWRgarlLRPLLQFTLimmAFYTGLSRVSDHKHHPSDVLAGFAQGALVA 268
Cdd:cd03394 57 ----QYRYGWR----WYGIPAYAL---ASLVGASRVVANRHWLSDVLAGAAIGILVG 102
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
92-268 |
1.37e-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: 50.78 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 92 GIVIAILAIITGEFYRIYYLKEKSRSTIQNPYVAALykqvGCFLFGC-AISQSFTDIAKVSIGRLRPHFL---NVCNPDF 167
Cdd:cd03389 35 GWYLIPSLLLFLLFRFGDLRGLSAPSRARFPKAAWA----GLFLFATvALSGILVNLLKFIIGRARPKLLfddGLYGFDP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 168 SQINcsvgyiqnyrcrgedskvqEARKSFFSGHAS--FSMYTMLYLvLYLQARFTWRGARLLrpllqftlimmafyTGLS 245
Cdd:cd03389 111 FHAD-------------------YAFTSFPSGHSAtaGAAAAALAL-LFPRYRWAFILLALL--------------IAFS 156
|
170 180
....*....|....*....|...
gi 115497984 246 RVSDHKHHPSDVLAGFAQGALVA 268
Cdd:cd03389 157 RVIVGAHYPSDVIAGSLLGAVTA 179
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
135-280 |
2.72e-07 |
|
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: 49.57 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 135 LFGCAIS---QSFTDIAKVSIGRLRPhflnvCNPDfsqINCSVGYIQnYRCRGedskvqearKSFFSGHASFSMYTMLYL 211
Cdd:cd03395 60 LVLLAVGfadQLASGFLKPLVARLRP-----CNAL---DGVRLVVLG-DQGGS---------YSFASSHAANSFALALFI 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497984 212 VLYLQAR-FTWrgarllrpllqfTLIMMAFYTGLSRVSDHKHHPSDVLAgfaqGALVACCIVFFVSDLFK 280
Cdd:cd03395 122 WLFFRRGlFSP------------VLLLWALLVGYSRVYVGVHYPGDVIA----GALIGIISGLLFYLLFS 175
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
195-266 |
1.36e-05 |
|
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: 44.62 E-value: 1.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115497984 195 SFFSGHAS--FSMYTMLYLVLYLqarftwrgARLLRPLLqftlIMMAFYTGLSRVSDHKHHPSDVLAGFAQGAL 266
Cdd:cd03391 92 SFPSGHASraAFVARFLLNHLVL--------AVPLRVLL----VLWATVVGISRVLLGRHHVLDVLAGAFLGYL 153
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
198-268 |
6.18e-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: 6.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497984 198 SGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVA 268
Cdd:cd03382 85 SSHSQFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLG 155
|
|
| |
