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Conserved domains on  [gi|123789358|sp|Q0VBU9|]
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RecName: Full=Phospholipid phosphatase 4

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130247)

type 2 phosphatidic acid phosphatase (PAP2) family protein similar to mammalian phospholipid phosphatases that catalyzes the conversion of phosphatidic acid to diacylglycerol

EC:  3.1.3.-
Gene Ontology:  GO:0006644|GO:0008195|GO:0046839
PubMed:  12447906

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 37-225 5.86e-92

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: 269.86  E-value: 5.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  37 WLYKNPLVQSDNIPTRLMFAISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRC 116
Cdd:cd03390    1 PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 117 FPDGVMNSEM------RCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLHCFteSGRGKSWRLCAAILPLYCAM 190
Cdd:cd03390   81 FPDGGTPSDTlvgidiCCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIF--DPRGSSWRLLLALLPLLLAI 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 123789358 191 MIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQH 225
Cdd:cd03390  159 LVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
 
Name Accession Description Interval E-value
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 37-225 5.86e-92

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: 269.86  E-value: 5.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  37 WLYKNPLVQSDNIPTRLMFAISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRC 116
Cdd:cd03390    1 PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 117 FPDGVMNSEM------RCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLHCFteSGRGKSWRLCAAILPLYCAM 190
Cdd:cd03390   81 FPDGGTPSDTlvgidiCCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIF--DPRGSSWRLLLALLPLLLAI 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 123789358 191 MIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQH 225
Cdd:cd03390  159 LVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
PLN02250 PLN02250
lipid phosphate phosphatase
 12-228 1.09e-61

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 197.07  E-value: 1.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  12 ALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLvQSDNIPTRLMFAISFLTPLAVICVVKIIRRtDKTEIKEAFLAVSLAL 91
Cdd:PLN02250  30 LLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPL-QDNTIPFWAVPLIAILLPFAVILVYYFIRR-DVYDLHHAILGLLFSV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  92 ALNGVCTNTIKLIVGRPRPDFFYRCFPDGV-----MNSEMRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLH 166
Cdd:PLN02250 108 LITGVITDAIKDAVGRPRPDFFWRCFPDGKgvfhpVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIR 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123789358 167 CFTEsgRGKSWRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHYPP 228
Cdd:PLN02250 188 VFDR--RGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPP 247
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 86-226 2.17e-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: 89.40  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358   86 AVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDgvmnsemrcTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGkl 165
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL---------VPAPSTLPGLGYSFPSGHSATAFALALLLALLLRR-- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123789358  166 hcftesgRGKSWRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHY 226
Cdd:pfam01569  70 -------LRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
83-222 9.18e-18

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 77.00  E-value: 9.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358    83 AFLAVSLALAlngvcTNTIKLIVGRPRPDFFYRCFPdgvmnsemRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLa 162
Cdd:smart00014   1 ALLAVVSQLF-----NGVIKNYFGRPRPFFLSIGDA--------CCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL- 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358   163 gklhcfteSGRGKSWRLCAAILPLycAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICY 222
Cdd:smart00014  67 --------PARAGRKLLIFLLLLL--ALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 12-223 1.66e-11

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: 61.59  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  12 ALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLVQSDNIPTRLMFAISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLAL 91
Cdd:COG0671    3 LALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  92 ALNGVCTNTIKLIVGRPRPDffyrcfpdgvmnseMRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLhcftes 171
Cdd:COG0671   83 LLLLLLLLLLKYLFGRPRPF--------------VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLPRRW------ 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 123789358 172 grgksWRLCAAILplycAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYR 223
Cdd:COG0671  143 -----LAALLLAL----ALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLA 185
 
Name Accession Description Interval E-value
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 37-225 5.86e-92

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: 269.86  E-value: 5.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  37 WLYKNPLVQSDNIPTRLMFAISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRC 116
Cdd:cd03390    1 PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 117 FPDGVMNSEM------RCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLHCFteSGRGKSWRLCAAILPLYCAM 190
Cdd:cd03390   81 FPDGGTPSDTlvgidiCCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIF--DPRGSSWRLLLALLPLLLAI 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 123789358 191 MIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQH 225
Cdd:cd03390  159 LVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
PLN02250 PLN02250
lipid phosphate phosphatase
 12-228 1.09e-61

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 197.07  E-value: 1.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  12 ALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLvQSDNIPTRLMFAISFLTPLAVICVVKIIRRtDKTEIKEAFLAVSLAL 91
Cdd:PLN02250  30 LLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPL-QDNTIPFWAVPLIAILLPFAVILVYYFIRR-DVYDLHHAILGLLFSV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  92 ALNGVCTNTIKLIVGRPRPDFFYRCFPDGV-----MNSEMRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLH 166
Cdd:PLN02250 108 LITGVITDAIKDAVGRPRPDFFWRCFPDGKgvfhpVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIR 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123789358 167 CFTEsgRGKSWRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHYPP 228
Cdd:PLN02250 188 VFDR--RGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPP 247
PLN02731 PLN02731
Putative lipid phosphate phosphatase
 24-243 9.88e-50

Putative lipid phosphate phosphatase


Pssm-ID: 178332  Cd Length: 333  Bit Score: 166.74  E-value: 9.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  24 LDPFQRVIQPEEIWLYKNPLvQSDNIPTRLMFAISFLTPLaVICVVKIIRRTDKTEIKEAFLAVSLALALNGVCTNTIKL 103
Cdd:PLN02731  61 IHPFYRFVGKDMMTDLSYPL-KSNTVPIWSVPVYAMLLPL-VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 104 IVGRPRPDFFYRCFPDG--VMNS--EMRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLHCFteSGRGKSWRL 179
Cdd:PLN02731 139 AVGRPRPDFFWRCFPDGkaLYDSlgDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAF--DGKGHVAKL 216

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123789358 180 CAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHYPPLANTACHKPYVSLRV 243
Cdd:PLN02731 217 CIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQV 280
PLN02715 PLN02715
lipid phosphate phosphatase
 4-242 1.74e-43

lipid phosphate phosphatase


Pssm-ID: 178317 [Multi-domain]  Cd Length: 327  Bit Score: 150.20  E-value: 1.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358   4 LAIEIGVrallfgvfvftEFLDPFQRVIQPEEIWLYKNPLvQSDNIPTRLMFAISFLTPLaVICVVKIIRRTDKTEIKEA 83
Cdd:PLN02715  58 IAIEIGL-----------NLISPFYRYVGKDMMTDLKYPF-KDNTVPIWSVPVYAVLLPI-ILFVCFYLKRRCVYDLHHS 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  84 FLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGVMNSE----MRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTF 159
Cdd:PLN02715 125 ILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDalggVICHGKAAEVKEGHKSFPSGHTSWSFAGLTFLSL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 160 YLAGKLHCFTESGRGKswRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHYPPLANTACHKPYV 239
Cdd:PLN02715 205 YLSGKIKAFNGEGHVA--KLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCYRQFYPNPYHEEGWGPYA 282


                 ...
gi 123789358 240 SLR 242
Cdd:PLN02715 283 YFK 285
PAP2_wunen cd03384
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ...
 84-220 1.39e-25

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: 98.47  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  84 FLAVSLA-LALNGVCTNTIKLIVGRPRPDFFYRCFPDG----------VMNSEMRCTGDPDLVSEGRKSFPSIHSSFAFS 152
Cdd:cd03384    5 FVGVFLFgLFATQLLTDLGKYVTGRLRPHFLDVCKPNYtdltcsldhqYIADCTCCTGDPDLIREARLSFPSGHASLSMY 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123789358 153 GLGFTTFYLAGKLhcftesgRGKSWRLCAAILPLYCAM---MIALSRMCDYKHHWQDSFVGGVIGLIFAYI 220
Cdd:cd03384   85 AAVFLALYLQARL-------KLRGSRLLRPLLQFLLLAlalYVGLSRISDYKHHWSDVLAGALLGSVIALF 148
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 83-222 3.89e-25

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: 96.38  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  83 AFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGvmnsemrctgDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLA 162
Cdd:cd01610    4 LALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG----------DPLLLTEGGYSFPSGHAAFAFALALFLALLLP 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 163 GKLhcftesgrgksWRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICY 222
Cdd:cd01610   74 RRL-----------LRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 86-226 2.17e-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: 89.40  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358   86 AVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDgvmnsemrcTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGkl 165
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL---------VPAPSTLPGLGYSFPSGHSATAFALALLLALLLRR-- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123789358  166 hcftesgRGKSWRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHY 226
Cdd:pfam01569  70 -------LRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
83-222 9.18e-18

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 77.00  E-value: 9.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358    83 AFLAVSLALAlngvcTNTIKLIVGRPRPDFFYRCFPdgvmnsemRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLa 162
Cdd:smart00014   1 ALLAVVSQLF-----NGVIKNYFGRPRPFFLSIGDA--------CCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL- 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358   163 gklhcfteSGRGKSWRLCAAILPLycAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICY 222
Cdd:smart00014  67 --------PARAGRKLLIFLLLLL--ALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 81-222 7.49e-12

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: 60.42  E-value: 7.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  81 KEAFLAVSLALALNGVCTNTIKLIVGRPRPDffyrcfpdgvmnsemrctGDPDlvseGRKSFPSIHSSFAFSGLGFTTFy 160
Cdd:cd03394    2 REGLLILAEAAALTAAVTEGLKFAVGRARPD------------------GSNN----GYRSFPSGHTASAFAAATFLQY- 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123789358 161 lagklhcftESGRGKSWrlcaaiLPLYC-AMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICY 222
Cdd:cd03394   59 ---------RYGWRWYG------IPAYAlASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 12-223 1.66e-11

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: 61.59  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  12 ALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLVQSDNIPTRLMFAISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLAL 91
Cdd:COG0671    3 LALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  92 ALNGVCTNTIKLIVGRPRPDffyrcfpdgvmnseMRCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLhcftes 171
Cdd:COG0671   83 LLLLLLLLLLKYLFGRPRPF--------------VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLPRRW------ 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 123789358 172 grgksWRLCAAILplycAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYR 223
Cdd:COG0671  143 -----LAALLLAL----ALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLA 185
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 51-222 4.20e-09

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: 54.54  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  51 TRLMFAISFL------TPL-AVICVVKIIRRTdkteiKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGvmn 123
Cdd:cd03392   29 TAFMTAITFLgspavlLIIvLLLALLLLLKRR-----RRAALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVPEGG--- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358 124 semrctgdpdlvsegrKSFPSIHSSFAFSGLGFTTFYLAGKLHcftesgrGKSWRLCAAILPLYCAMMIALSRMcdYKH- 202
Cdd:cd03392  101 ----------------YSFPSGHAMGATVLYGFLAYLLARRLP-------RRRVRILLLILAAILILLVGLSRL--YLGv 155

                        170       180
                 ....*....|....*....|.
gi 123789358 203 HWQDSFVGGV-IGLIFAYICY 222
Cdd:cd03392  156 HYPSDVLAGWlLGLAWLALLI 176
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 89-223 1.24e-06

PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria.


Pssm-ID: 239483  Cd Length: 186  Bit Score: 47.70  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123789358  89 LALALNGVCTNTIKLIVGRPRPDFFyrcFPDGVMNSemrctgDPDLVSEGRKSFPSIHSSFAFSgLGFTTFYLAGKlhcf 168
Cdd:cd03389   76 ATVALSGILVNLLKFIIGRARPKLL---FDDGLYGF------DPFHADYAFTSFPSGHSATAGA-AAAALALLFPR---- 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 123789358 169 tesgrgksWRLcaaiLPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYR 223
Cdd:cd03389  142 --------YRW----AFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQ 184
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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