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Conserved domains on  [gi|28571521|ref|NP_788583|]
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uncharacterized protein Dmel_CG12746, isoform D [Drosophila melanogaster]

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

 Zoom to residue level

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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. ...
 104-302 5.48e-84

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: 252.91  E-value: 5.48e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 104 WLYKNPRRPD-IVRGGELLFWVIVAPFLVTIAFYWYTRDRR-DFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRC 181
Cdd:cd03390   1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISLFFRRSLwDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 182 FPDGVMVLNTTSNGVDTsildfnCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDsrGRGHTWRLCIAVI 261
Cdd:cd03390  81 FPDGGTPSDTLVGIDIC------CTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFD--PRGSSWRLLLALL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28571521 262 PLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISYTQY 302
Cdd:cd03390 153 PLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 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. ...
 104-302 5.48e-84

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: 252.91  E-value: 5.48e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 104 WLYKNPRRPD-IVRGGELLFWVIVAPFLVTIAFYWYTRDRR-DFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRC 181
Cdd:cd03390   1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISLFFRRSLwDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 182 FPDGVMVLNTTSNGVDTsildfnCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDsrGRGHTWRLCIAVI 261
Cdd:cd03390  81 FPDGGTPSDTLVGIDIC------CTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFD--PRGSSWRLLLALL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28571521 262 PLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISYTQY 302
Cdd:cd03390 153 PLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
PLN02250 PLN02250
lipid phosphate phosphatase
 122-314 8.49e-55

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 182.43  E-value: 8.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  122 FW-----VIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVMVLNTTSNgv 196
Cdd:PLN02250  68 FWavpliAILLPFAVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTT-- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  197 dtsilDFNCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDSRGrgHTWRLCIAVIPLFIALLVAVSRTCD 276
Cdd:PLN02250 146 -----DVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRG--HVAKLCIVFLPLLVAALVGVSRVDD 218

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 28571521  277 YHHHWQDVTIGGLIGLFAGYISYTQYYPSIFCPDAGIP 314
Cdd:PLN02250 219 YWHHWQDVFAGALIGLTVASFCYLQFFPPPYDIDGWGP 256
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 154-303 2.22e-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: 96.34  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521   154 LALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVMVLNTTsngvdtsildfnctglpgdinEGRKSFPSGHSSFAFASFGF 233
Cdd:pfam01569   4 LALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP---------------------GLGYSFPSGHSATAFALALL 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521   234 IAYYIgaklhafdsRGRGHTWRLCIAVIPLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISYTQYY 303
Cdd:pfam01569  63 LALLL---------RRLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
154-297 6.13e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 75.85  E-value: 6.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521    154 LALCMNGIPTSVLKITVGRPRPDYFYRCfpdgvmvlnttsngvdtsilDFNCTGLPGDINEGRKSFPSGHSSFAFASFGF 233
Cdd:smart00014   2 LLAVVSQLFNGVIKNYFGRPRPFFLSIG--------------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALF 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571521    234 IAYYIGAKLHafdsrgrghtWRLCIAVIpLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYI 297
Cdd:smart00014  62 LLLYLPARAG----------RKLLIFLL-LLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 120-302 6.12e-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: 72.38  E-value: 6.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 120 LLFWVIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFyrcfPDGVMVLNTTSNGvdts 199
Cdd:COG0671  46 ILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVV----PDLELLLGTAGGY---- 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 200 ildfnctglpgdinegrkSFPSGHSSFAFASFGFIAYYIgaklhafdsrgrghtWRLCIAVIPLFIALLVAVSRTCDYHH 279
Cdd:COG0671 118 ------------------SFPSGHAAAAFALALVLALLL---------------PRRWLAALLLALALLVGLSRVYLGVH 164

                       170       180
                ....*....|....*....|...
gi 28571521 280 HWQDVTIGGLIGLFAGYISYTQY 302
Cdd:COG0671 165 YPSDVLAGALLGLAIALLLLALL 187
 
Name Accession Description Interval E-value
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 104-302 5.48e-84

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: 252.91  E-value: 5.48e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 104 WLYKNPRRPD-IVRGGELLFWVIVAPFLVTIAFYWYTRDRR-DFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRC 181
Cdd:cd03390   1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISLFFRRSLwDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 182 FPDGVMVLNTTSNGVDTsildfnCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDsrGRGHTWRLCIAVI 261
Cdd:cd03390  81 FPDGGTPSDTLVGIDIC------CTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFD--PRGSSWRLLLALL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28571521 262 PLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISYTQY 302
Cdd:cd03390 153 PLLLAILVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
PLN02250 PLN02250
lipid phosphate phosphatase
 122-314 8.49e-55

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 182.43  E-value: 8.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  122 FW-----VIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVMVLNTTSNgv 196
Cdd:PLN02250  68 FWavpliAILLPFAVILVYYFIRRDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGKGVFHPVTT-- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  197 dtsilDFNCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDSRGrgHTWRLCIAVIPLFIALLVAVSRTCD 276
Cdd:PLN02250 146 -----DVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDRRG--HVAKLCIVFLPLLVAALVGVSRVDD 218

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 28571521  277 YHHHWQDVTIGGLIGLFAGYISYTQYYPSIFCPDAGIP 314
Cdd:PLN02250 219 YWHHWQDVFAGALIGLTVASFCYLQFFPPPYDIDGWGP 256
PLN02731 PLN02731
Putative lipid phosphate phosphatase
 123-347 1.90e-46

Putative lipid phosphate phosphatase


Pssm-ID: 178332  Cd Length: 333  Bit Score: 161.35  E-value: 1.90e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  123 WVIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVMVLNttsngvdtSILD 202
Cdd:PLN02731  93 YAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYD--------SLGD 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  203 FNCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDsrGRGHTWRLCIAVIPLFIALLVAVSRTCDYHHHWQ 282
Cdd:PLN02731 165 VICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFD--GKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQ 242

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571521  283 DVTIGGLIGLFAGYISYTQYYPSIFCPDAGIPLVRWPSREGSQYQRLSgkddNGS--RGPHHLDGGD 347
Cdd:PLN02731 243 DVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAA----NGAvqQPPPQVNNGE 305
PLN02715 PLN02715
lipid phosphate phosphatase
 88-307 3.59e-40

lipid phosphate phosphatase


Pssm-ID: 178317 [Multi-domain]  Cd Length: 327  Bit Score: 144.43  E-value: 3.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521   88 LETMTAFKREIHEEELWLYKNPRRPDIVRGGELLFWVIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLK 167
Cdd:PLN02715  64 LNLISPFYRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLPIILFVCFYLKRRCVYDLHHSILGLLFAVLITGVITDSIK 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  168 ITVGRPRPDYFYRCFPDGVMVLNTTSNGVdtsildfnCTGLPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFDS 247
Cdd:PLN02715 144 VATGRPRPNFYWRCFPDGKELYDALGGVI--------CHGKAAEVKEGHKSFPSGHTSWSFAGLTFLSLYLSGKIKAFNG 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521  248 RGrgHTWRLCIAVIPLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISYTQYYPSIF 307
Cdd:PLN02715 216 EG--HVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCYRQFYPNPY 273
PAP2_wunen cd03384
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ...
 156-297 6.67e-28

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: 106.56  E-value: 6.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 156 LCMNGIPTSVLKITVGRPRPDYFYRCFPDgvMVLNTTSNGVDTSILDFNCTGLPGDINEGRKSFPSGHSSFAFASFGFIA 235
Cdd:cd03384  13 LFATQLLTDLGKYVTGRLRPHFLDVCKPN--YTDLTCSLDHQYIADCTCCTGDPDLIREARLSFPSGHASLSMYAAVFLA 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571521 236 YYIGAKLhafdSRGRGHTWRLCIAVIPLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYI 297
Cdd:cd03384  91 LYLQARL----KLRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIALF 148
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 145-299 1.39e-27

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: 104.85  E-value: 1.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 145 FRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVmvlnttsngvdtsildfnctglPGDINEGRKSFPSGHS 224
Cdd:cd01610   1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGD----------------------PLLLTEGGYSFPSGHA 58

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571521 225 SFAFASFGFIAYYIGAKLhafdsrgrghtWRLCIAVIPLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISY 299
Cdd:cd01610  59 AFAFALALFLALLLPRRL-----------LRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 154-303 2.22e-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: 96.34  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521   154 LALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVMVLNTTsngvdtsildfnctglpgdinEGRKSFPSGHSSFAFASFGF 233
Cdd:pfam01569   4 LALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP---------------------GLGYSFPSGHSATAFALALL 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521   234 IAYYIgaklhafdsRGRGHTWRLCIAVIPLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISYTQYY 303
Cdd:pfam01569  63 LALLL---------RRLRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
154-297 6.13e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 75.85  E-value: 6.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521    154 LALCMNGIPTSVLKITVGRPRPDYFYRCfpdgvmvlnttsngvdtsilDFNCTGLPGDINEGRKSFPSGHSSFAFASFGF 233
Cdd:smart00014   2 LLAVVSQLFNGVIKNYFGRPRPFFLSIG--------------------DACCTPNFLLTLEAGYSFPSGHTAFAFAFALF 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571521    234 IAYYIGAKLHafdsrgrghtWRLCIAVIpLFIALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYI 297
Cdd:smart00014  62 LLLYLPARAG----------RKLLIFLL-LLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 120-302 6.12e-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: 72.38  E-value: 6.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 120 LLFWVIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFyrcfPDGVMVLNTTSNGvdts 199
Cdd:COG0671  46 ILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVV----PDLELLLGTAGGY---- 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 200 ildfnctglpgdinegrkSFPSGHSSFAFASFGFIAYYIgaklhafdsrgrghtWRLCIAVIPLFIALLVAVSRTCDYHH 279
Cdd:COG0671 118 ------------------SFPSGHAAAAFALALVLALLL---------------PRRWLAALLLALALLVGLSRVYLGVH 164

                       170       180
                ....*....|....*....|...
gi 28571521 280 HWQDVTIGGLIGLFAGYISYTQY 302
Cdd:COG0671 165 YPSDVLAGALLGLAIALLLLALL 187
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 122-302 2.22e-14

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: 70.72  E-value: 2.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 122 FWVIVAPFLVTIAFYWYTRDRRdfraASWAWTLALCMNGIPTSVLKITVGRPRPDYFYRCFPDGvmvlnttsngvdtsil 201
Cdd:cd03392  41 PAVLLIIVLLLALLLLLKRRRR----AALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVPEGG---------------- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 202 dfnctglpgdinegrKSFPSGHSSFAFASFGFIAYYIGAKLHAFdsrgrghTWRLCIAVIPLFIALLVAVSRTcdY-HHH 280
Cdd:cd03392 101 ---------------YSFPSGHAMGATVLYGFLAYLLARRLPRR-------RVRILLLILAAILILLVGLSRL--YlGVH 156

                       170       180
                ....*....|....*....|....*..
gi 28571521 281 W-QDVtIGG----LIGLFAGYISYTQY 302
Cdd:cd03392 157 YpSDV-LAGwllgLAWLALLILLYRRL 182
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 141-299 1.56e-13

PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239488 [Multi-domain]  Cd Length: 106  Bit Score: 66.20  E-value: 1.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 141 DRRDFRAASWAWTLALCMngipTSVLKITVGRPRPDyfyrcfpdgvmvlnttsngvdtsildfnctglpGDiNEGRKSFP 220
Cdd:cd03394   1 DREGLLILAEAAALTAAV----TEGLKFAVGRARPD---------------------------------GS-NNGYRSFP 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 221 SGHSSFAFASFGFIAYYIGAKLHAfdsrgrghtwrlciavIPLF-IALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISY 299
Cdd:cd03394  43 SGHTASAFAAATFLQYRYGWRWYG----------------IPAYaLASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 123-299 3.73e-12

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: 64.26  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 123 WVIVAPFLVTIAFY------WYTRDRRDFRAASWAWTL---ALCMNGIPTSVLKITVGRPRPDYFyrcFPDGvmvlntts 193
Cdd:cd03389  36 WYLIPSLLLFLLFRfgdlrgLSAPSRARFPKAAWAGLFlfaTVALSGILVNLLKFIIGRARPKLL---FDDG-------- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 194 ngvdtsILDFNctglPGDINEGRKSFPSGHSSFAFASFGFIAYYIGAKLHAFdsrgrghtwrlciavipLFIALLVAVSR 273
Cdd:cd03389 105 ------LYGFD----PFHADYAFTSFPSGHSATAGAAAAALALLFPRYRWAF-----------------ILLALLIAFSR 157

                       170       180
                ....*....|....*....|....*.
gi 28571521 274 TCDYHHHWQDVTIGGLIGLFAGYISY 299
Cdd:cd03389 158 VIVGAHYPSDVIAGSLLGAVTALALY 183
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 122-299 1.62e-11

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: 62.28  E-value: 1.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 122 FWVIV------APFLVTIAFYWYtrdrrdFRAASWAWT-------LALCMNGIPTSVLKITVGRPRPdyfyrCFPDgvmv 188
Cdd:cd03395  25 LMPFLtgkklsVPIFLLLALFIL------FRKGPIGLLilllvllAVGFADQLASGFLKPLVARLRP-----CNAL---- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 189 lnttsNGVDTSILdfnctglpgdINEGRK-SFPSGH--SSFAFASFGFIAYyigaklhafdsrgrghtWRLCIAVIPLFI 265
Cdd:cd03395  90 -----DGVRLVVL----------GDQGGSySFASSHaaNSFALALFIWLFF-----------------RRGLFSPVLLLW 137

                       170       180       190
                ....*....|....*....|....*....|....
gi 28571521 266 ALLVAVSRTCDYHHHWQDVTIGGLIGLFAGYISY 299
Cdd:cd03395 138 ALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFY 171
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 124-299 5.53e-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: 51.89  E-value: 5.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 124 VIVAPFLVTIAFYwytrdRRDFRAASWAwtLALCMNGIPTSVLKITVGRPRPdyfyrcfpdgvmvlnttsngvdTSILDF 203
Cdd:cd03382  26 VAILVGYATLILF-----RRELEAIYLF--IGLLANEALNYVLKRIIKEPRP----------------------CSGAYF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 204 NCTGlPGdinegrksFPSGHSSFAFasfgFIAYYIGAKLHAFDSRGRGHTWRLCIAVIPLFIALLVAVSRTCDYHHHWQD 283
Cdd:cd03382  77 VRSG-YG--------MPSSHSQFMG----FFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQ 143

                       170
                ....*....|....*.
gi 28571521 284 VTIGGLIGLFAGYISY 299
Cdd:cd03382 144 VVVGAIVGILLGILWF 159
PAP2_Aur1_like cd03386
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
 122-300 1.31e-07

PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.


Pssm-ID: 239481  Cd Length: 186  Bit Score: 51.16  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 122 FWVIVAPFLVTIAF-YWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPDYFYrcFPDGVMVLNTTSNGVDT-- 198
Cdd:cd03386  32 FPYGSLHFLVPLALlAWLFLFRPPGTLRRFRRALGLANLLGLLIYLLFPTAPPRYEPPY--GLILLVLLMYGSAGYTSgf 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 199 --SILDFNCtglpgdinegrksFPSGHSSFAFASFGFIAYYigaklhafdsrgRGHTWRLCIAVIPLFIALLVAVSRtcd 276
Cdd:cd03386 110 ggFDNPFNA-------------FPSLHVAWAVLAALFLWRH------------RRRLLRWLAVLWPLLIWLSTLYLG--- 161

                       170       180
                ....*....|....*....|....
gi 28571521 277 yHHHWQDVTIGGLIGLFAGYISYT 300
Cdd:cd03386 162 -NHYFIDLVGGIALALLSFYLARR 184
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
 129-298 7.20e-06

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: 45.39  E-value: 7.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 129 FLVTIAFYWytrdrrdfRAASWAWT-------LALCMNGIPTSVLKITVGRPRPDYFYRCFPDGVmvlnttsnGVDtsil 201
Cdd:cd03391  30 LAGTISCLW--------ISSSPAGQevlvnllLGLLLDIITVAILKALVRRRRPAYNSPDMLDYV--------AVD---- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 202 dfnctglpgdinegRKSFPSGHSSFAFASFGFIAYYIGAKLHafdsrgrghtwrlciAVIPLFI-ALLVAVSRTCDYHHH 280
Cdd:cd03391  90 --------------KYSFPSGHASRAAFVARFLLNHLVLAVP---------------LRVLLVLwATVVGISRVLLGRHH 140

                       170
                ....*....|....*...
gi 28571521 281 WQDVTIGGLIGLFAGYIS 298
Cdd:cd03391 141 VLDVLAGAFLGYLEALLV 158
PAP2_like_6 cd03396
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 116-233 4.04e-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: 41.13  E-value: 4.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 116 RGGELLFWVIVAPFLVTIAFYWYTRDRRDFRAASWAWTLALCMNGIPTSVLKITVGRPRPdyfyrcfpdgvmvLNTTSNG 195
Cdd:cd03396  36 LGGRLLSIALAVLLLALALLFFRRKRLRRRRRALLLLILVIGLGLLVVAILKSHWGRPRP-------------WDLTEFG 102

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 28571521 196 VDTSILDFNCTGLPGdiNEGRKSFPSGHSSFAFASFGF 233
Cdd:cd03396 103 GDAPYTPLFSGPSNG--CGKGCSFPSGHASAGFALLAL 138
COG3907 COG3907
Membrane-associated enzyme, PAP2 (acid phosphatase) superfamily [General function prediction ...
 102-273 1.40e-03

Membrane-associated enzyme, PAP2 (acid phosphatase) superfamily [General function prediction only];


Pssm-ID: 443113  Cd Length: 236  Bit Score: 39.88  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 102 ELWLYKNPRRPDIvrggellfWVIVAPFLVTIAFYWYTRDRRDFRAAswaWTLALCMNGIPT--SVLKITVGRPRP---D 176
Cdd:COG3907  60 ELLLHDGGKWLVI--------LVAVLLLLLLLASFKRPRLRRYRRRL---LYLLLSLALGLLvvSLLKSHTGRPCPwdlV 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571521 177 YFyrcfpdgvmvlnttsNGVDTSILDFNCTGLPGDINegrKSFPSGHSSFAFASFGFiayyigaklhAFDSRGRGHTWRL 256
Cdd:COG3907 129 EF---------------GGDAPYVPLFEPGPAGAGPG---RCFPAGHASAGFALLAL----------YFLLRRRRPRLAR 180

                       170
                ....*....|....*..
gi 28571521 257 CIAVIPLFIALLVAVSR 273
Cdd:COG3907 181 LGLAAGLALGLLMGLAQ 197
 
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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