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Conserved domains on  [gi|70887258|gb|EAO00018|]
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phosphatidic acid phosphatase, putative [Trypanosoma cruzi]

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130247)

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

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. ...
 143-291 1.01e-59

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: 189.35  E-value: 1.01e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 143 NARWWLFLEKLNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEGYSEKSTGV-------DWCKVAREGRLSFP 215
Cdd:cd03390  34 SLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARCFPDGGTPSDTLVgidicctGDPGVLKEGRKSFP 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70887258 216 SGHAAISFSSIVTLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSV 291
Cdd:cd03390 114 SGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSwRLLLALLPLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSY 190
 
Name Accession Description Interval E-value
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 143-291 1.01e-59

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: 189.35  E-value: 1.01e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 143 NARWWLFLEKLNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEGYSEKSTGV-------DWCKVAREGRLSFP 215
Cdd:cd03390  34 SLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARCFPDGGTPSDTLVgidicctGDPGVLKEGRKSFP 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70887258 216 SGHAAISFSSIVTLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSV 291
Cdd:cd03390 114 SGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSwRLLLALLPLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSY 190
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 161-296 7.48e-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: 83.62  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258   161 AFSVTLSMFIVDITKLYAGRLRPDFLARLenegysekSTGVDWCKVAREGRLSFPSGHAAISFSSIVTLVLFFvghlqvF 240
Cdd:pfam01569   3 LLALALAGLLSSVLKDYFGRPRPFFLLLE--------GGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLL------R 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887258   241 YFASPLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSVTVLFR 296
Cdd:pfam01569  69 RLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVPK 124
PLN02250 PLN02250
lipid phosphate phosphatase
 153-287 1.01e-18

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 84.98  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258  153 LNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEG---YSEKSTGVdWC----KVAREGRLSFPSGHAAISFSS 225
Cdd:PLN02250  96 LHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGkgvFHPVTTDV-LCtgakSVIKEGHKSFPSGHTSWSFAG 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887258  226 IVTLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCA 287
Cdd:PLN02250 175 LGFLSLYLSGKIRVFDRRGHVaKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVA 237
acidPPc smart00014
Acid phosphatase homologues;
167-289 6.25e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 75.46  E-value: 6.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258    167 SMFIVDITKLYAGRLRPDFLARLENEGYSEKSTGvdwckvaREGRLSFPSGHAAISFSsivtLVLFFVGHLQVFYfaspL 246
Cdd:smart00014   7 SQLFNGVIKNYFGRPRPFFLSIGDACCTPNFLLT-------LEAGYSFPSGHTAFAFA----FALFLLLYLPARA----G 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 70887258    247 RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALL 289
Cdd:smart00014  72 RKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 144-296 6.17e-12

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: 63.52  E-value: 6.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 144 ARWWLFLEKLNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEGYSEKStgvdwckvaregrLSFPSGHAAISF 223
Cdd:COG0671  62 LLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGG-------------YSFPSGHAAAAF 128

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887258 224 SSIVTLVLFFvghlqvfyfaspLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSVTVLFR 296
Cdd:COG0671 129 ALALVLALLL------------PRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLRR 189
 
Name Accession Description Interval E-value
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 143-291 1.01e-59

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: 189.35  E-value: 1.01e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 143 NARWWLFLEKLNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEGYSEKSTGV-------DWCKVAREGRLSFP 215
Cdd:cd03390  34 SLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARCFPDGGTPSDTLVgidicctGDPGVLKEGRKSFP 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70887258 216 SGHAAISFSSIVTLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSV 291
Cdd:cd03390 114 SGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSwRLLLALLPLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSY 190
PAP2_wunen cd03384
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ...
 161-291 5.25e-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: 98.09  E-value: 5.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 161 AFSVTLSMFIVDITKLYAGRLRPDFLAR------LENEGYSEKSTGVDWC-----KVAREGRLSFPSGHAAISFSSIVTL 229
Cdd:cd03384  10 LFGLFATQLLTDLGKYVTGRLRPHFLDVckpnytDLTCSLDHQYIADCTCctgdpDLIREARLSFPSGHASLSMYAAVFL 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70887258 230 VLFFVGHLQVfYFASPLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSV 291
Cdd:cd03384  90 ALYLQARLKL-RGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALFLV 150
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 155-291 4.76e-21

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: 86.75  E-value: 4.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 155 HWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLenegyseksTGVDWCKVAREGRLSFPSGHAAISFSSIVTLVLFFV 234
Cdd:cd01610   3 LLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRC---------GPDGDPLLLTEGGYSFPSGHAAFAFALALFLALLLP 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 70887258 235 GHLqvfyfaspLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSV 291
Cdd:cd01610  74 RRL--------LRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 161-296 7.48e-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: 83.62  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258   161 AFSVTLSMFIVDITKLYAGRLRPDFLARLenegysekSTGVDWCKVAREGRLSFPSGHAAISFSSIVTLVLFFvghlqvF 240
Cdd:pfam01569   3 LLALALAGLLSSVLKDYFGRPRPFFLLLE--------GGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLL------R 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887258   241 YFASPLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSVTVLFR 296
Cdd:pfam01569  69 RLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVPK 124
PLN02250 PLN02250
lipid phosphate phosphatase
 153-287 1.01e-18

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 84.98  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258  153 LNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEG---YSEKSTGVdWC----KVAREGRLSFPSGHAAISFSS 225
Cdd:PLN02250  96 LHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGkgvFHPVTTDV-LCtgakSVIKEGHKSFPSGHTSWSFAG 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887258  226 IVTLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCA 287
Cdd:PLN02250 175 LGFLSLYLSGKIRVFDRRGHVaKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVA 237
acidPPc smart00014
Acid phosphatase homologues;
167-289 6.25e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 75.46  E-value: 6.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258    167 SMFIVDITKLYAGRLRPDFLARLENEGYSEKSTGvdwckvaREGRLSFPSGHAAISFSsivtLVLFFVGHLQVFYfaspL 246
Cdd:smart00014   7 SQLFNGVIKNYFGRPRPFFLSIGDACCTPNFLLT-------LEAGYSFPSGHTAFAFA----FALFLLLYLPARA----G 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 70887258    247 RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALL 289
Cdd:smart00014  72 RKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
PLN02731 PLN02731
Putative lipid phosphate phosphatase
 153-295 2.11e-16

Putative lipid phosphate phosphatase


Pssm-ID: 178332  Cd Length: 333  Bit Score: 78.53  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258  153 LNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEGYS-EKSTGVDWC----KVAREGRLSFPSGHAAISFSSIV 227
Cdd:PLN02731 115 LHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKAlYDSLGDVIChgdkSVIREGHKSFPSGHTSWSFSGLG 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887258  228 TLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGtgcaLLSVTVLF 295
Cdd:PLN02731 195 FLSLYLSGKIQAFDGKGHVaKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLG----LAISTICY 259
PLN02715 PLN02715
lipid phosphate phosphatase
 153-284 2.83e-15

lipid phosphate phosphatase


Pssm-ID: 178317 [Multi-domain]  Cd Length: 327  Bit Score: 75.09  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258  153 LNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEG---YSEKSTGVDWCKVA--REGRLSFPSGHAAISFSSIV 227
Cdd:PLN02715 121 LHHSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGkelYDALGGVICHGKAAevKEGHKSFPSGHTSWSFAGLT 200

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 70887258  228 TLVLFFVGHLQVFYFASPL-RLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGT 284
Cdd:PLN02715 201 FLSLYLSGKIKAFNGEGHVaKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGI 258
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 157-291 1.08e-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: 63.50  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 157 LLAQAFSVTLSMFIVDITKLYAGRLRPDflarlenegysekstgvdwckVAREGRLSFPSGHAAISFSSIVTLvlffvgH 236
Cdd:cd03394   5 LLILAEAAALTAAVTEGLKFAVGRARPD---------------------GSNNGYRSFPSGHTASAFAAATFL------Q 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 70887258 237 LQVFYFASPLRLFLsmlpliLPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSV 291
Cdd:cd03394  58 YRYGWRWYGIPAYA------LASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 144-296 6.17e-12

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: 63.52  E-value: 6.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 144 ARWWLFLEKLNHWLLAQAFSVTLSMFIVDITKLYAGRLRPDFLARLENEGYSEKStgvdwckvaregrLSFPSGHAAISF 223
Cdd:COG0671  62 LLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGG-------------YSFPSGHAAAAF 128

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887258 224 SSIVTLVLFFvghlqvfyfaspLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSVTVLFR 296
Cdd:COG0671 129 ALALVLALLL------------PRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLRR 189
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 156-289 4.87e-10

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: 57.66  E-value: 4.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 156 WLLAQAFSVTLSMFI-VDITKLYAGRLRPDFLARLenegysekstGVDWCKVAREGRLSFPSGHAAISFSSIVTLVLFFv 234
Cdd:cd03395  57 ILLLVLLAVGFADQLaSGFLKPLVARLRPCNALDG----------VRLVVLGDQGGSYSFASSHAANSFALALFIWLFF- 125

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 70887258 235 ghlqvfyfasPLRLFLSMLpLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALL 289
Cdd:cd03395 126 ----------RRGLFSPVL-LLWALLVGYSRVYVGVHYPGDVIAGALIGIISGLL 169
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 162-289 5.91e-10

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: 57.72  E-value: 5.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 162 FSVTLSMFIVDITKLYAGRLRPDFLarLENEGYsekstGVDWCKVAREgRLSFPSGHAAISFSSIVTLVLFFVGHLQVFY 241
Cdd:cd03389  76 ATVALSGILVNLLKFIIGRARPKLL--FDDGLY-----GFDPFHADYA-FTSFPSGHSATAGAAAAALALLFPRYRWAFI 147

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 70887258 242 FASplrlflsmlplilpIVVAVSRTRDNRHHFSDVLAGGIIGTGCALL 289
Cdd:cd03389 148 LLA--------------LLIAFSRVIVGAHYPSDVIAGSLLGAVTALA 181
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 145-296 7.06e-10

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: 57.23  E-value: 7.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887258 145 RWWLFLeklnHWLLAQAFSVTLSMFIvditKLYAGRLRPDFLARLENEGYSekstgvdwckvaregrlsFPSGHAAISFS 224
Cdd:cd03392  60 RRRAAL----FLLLALLGGGALNTLL----KLLVQRPRPPLHLLVPEGGYS------------------FPSGHAMGATV 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70887258 225 SIVTLVLFFVGHLQvfyfASPLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLSVTVLFR 296
Cdd:cd03392 114 LYGFLAYLLARRLP----RRRVRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLLGLAWLALLILLYRR 181
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
 213-290 4.34e-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: 43.08  E-value: 4.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70887258 213 SFPSGHAAISFssivtlvlfFVghLQVFYFASPLRLFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALLS 290
Cdd:cd03391  92 SFPSGHASRAA---------FV--ARFLLNHLVLAVPLRVLLVLWATVVGISRVLLGRHHVLDVLAGAFLGYLEALLV 158
PAP2_diacylglycerolkinase cd03383
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ...
 215-289 1.14e-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: 40.78  E-value: 1.14e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70887258 215 PSGHAAISFSSIVTLVLFFVGHlqvfyfasplrlFLSMLPLILPIVVAVSRTRDNRHHFSDVLAGGIIGTGCALL 289
Cdd:cd03383  42 PSGHAAIAFSIATAISLITNNP------------IISILSVLLAVMVAHSRVEMKIHTMWEVVVGAILGALITLL 104
 
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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