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Conserved domains on  [gi|1910870446|ref|XP_036121470|]
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phospholipid phosphatase 4 [Molossus molossus]

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 1.42e-90

PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.


:

Pssm-ID: 239484 [Multi-domain]  Cd Length: 193  Bit Score: 266.39  E-value: 1.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  37 WLYKNPLVQSDSIPTRLMFAISFLTPLAVICVVKIIRRTDRTEVKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRC 116
Cdd:cd03390     1 PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 117 FPDGVMNSEMQ------CTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKLRCFteTGRGKSWRLCAAILPLCCAT 190
Cdd:cd03390    81 FPDGGTPSDTLvgidicCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIF--DPRGSSWRLLLALLPLLLAI 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1910870446 191 MIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQH 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 1.42e-90

PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.


Pssm-ID: 239484 [Multi-domain]  Cd Length: 193  Bit Score: 266.39  E-value: 1.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  37 WLYKNPLVQSDSIPTRLMFAISFLTPLAVICVVKIIRRTDRTEVKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRC 116
Cdd:cd03390     1 PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 117 FPDGVMNSEMQ------CTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKLRCFteTGRGKSWRLCAAILPLCCAT 190
Cdd:cd03390    81 FPDGGTPSDTLvgidicCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIF--DPRGSSWRLLLALLPLLLAI 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1910870446 191 MIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQH 225
Cdd:cd03390   159 LVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
PLN02250 PLN02250
lipid phosphate phosphatase
 12-228 3.37e-63

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 200.92  E-value: 3.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  12 ALLFGIFVLTEFLDPFQRVIQPEEIWLYKNPLvQSDSIPTRLMFAISFLTPLAVICVVKIIRRtDRTEVKEAFLAVSLAL 91
Cdd:PLN02250   30 LLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPL-QDNTIPFWAVPLIAILLPFAVILVYYFIRR-DVYDLHHAILGLLFSV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  92 ALNGVCTNTIKLIVGRPRPDFFYRCFPDGV-----MNSEMQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKLR 166
Cdd:PLN02250  108 LITGVITDAIKDAVGRPRPDFFWRCFPDGKgvfhpVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIR 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1910870446 167 CFTEtgRGKSWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQHYPP 228
Cdd:PLN02250  188 VFDR--RGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPP 247
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 86-226 1.32e-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: 89.79  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  86 AVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDgvmnsemqcTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGkl 165
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL---------VPAPSTLPGLGYSFPSGHSATAFALALLLALLLRR-- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1910870446 166 rcftetgRGKSWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQHY 226
Cdd:pfam01569  70 -------LRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
83-222 7.19e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 74.30  E-value: 7.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446   83 AFLAVSLALAlngvcTNTIKLIVGRPRPDFFYRCFPdgvmnsemQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLA 162
Cdd:smart00014   1 ALLAVVSQLF-----NGVIKNYFGRPRPFFLSIGDA--------CCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLP 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  163 gklrcftetGRGKSWRLCAAILPLCCAtmIALSRLCDYKHHWQDSFVGGVIGLIFAYTCY 222
Cdd:smart00014  68 ---------ARAGRKLLIFLLLLLALV--VGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 12-223 8.82e-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: 62.36  E-value: 8.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  12 ALLFGIFVLTEFLDPFQRVIQPEEIWLYKNPLVQSDSIPTRLMFAISFLTPLAVICVVKIIRRTDRTEVKEAFLAVSLAL 91
Cdd:COG0671     3 LALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  92 ALNGVCTNTIKLIVGRPRPDffyrcfpdgvmnseMQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLagklrcftet 171
Cdd:COG0671    83 LLLLLLLLLLKYLFGRPRPF--------------VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL---------- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1910870446 172 grgksWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYR 223
Cdd:COG0671   139 -----PRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLA 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 1.42e-90

PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.


Pssm-ID: 239484 [Multi-domain]  Cd Length: 193  Bit Score: 266.39  E-value: 1.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  37 WLYKNPLVQSDSIPTRLMFAISFLTPLAVICVVKIIRRTDRTEVKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRC 116
Cdd:cd03390     1 PSISYPFAESETVPTWLLVIISVGIPLLVIILISLFFRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 117 FPDGVMNSEMQ------CTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKLRCFteTGRGKSWRLCAAILPLCCAT 190
Cdd:cd03390    81 FPDGGTPSDTLvgidicCTGDPGVLKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIF--DPRGSSWRLLLALLPLLLAI 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1910870446 191 MIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQH 225
Cdd:cd03390   159 LVAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
PLN02250 PLN02250
lipid phosphate phosphatase
 12-228 3.37e-63

lipid phosphate phosphatase


Pssm-ID: 215139  Cd Length: 314  Bit Score: 200.92  E-value: 3.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  12 ALLFGIFVLTEFLDPFQRVIQPEEIWLYKNPLvQSDSIPTRLMFAISFLTPLAVICVVKIIRRtDRTEVKEAFLAVSLAL 91
Cdd:PLN02250   30 LLLVVIEVVLNVIEPFHRFVGKDMLTDLSYPL-QDNTIPFWAVPLIAILLPFAVILVYYFIRR-DVYDLHHAILGLLFSV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  92 ALNGVCTNTIKLIVGRPRPDFFYRCFPDGV-----MNSEMQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKLR 166
Cdd:PLN02250  108 LITGVITDAIKDAVGRPRPDFFWRCFPDGKgvfhpVTTDVLCTGAKSVIKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIR 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1910870446 167 CFTEtgRGKSWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQHYPP 228
Cdd:PLN02250  188 VFDR--RGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPP 247
PLN02731 PLN02731
Putative lipid phosphate phosphatase
 24-263 1.60e-49

Putative lipid phosphate phosphatase


Pssm-ID: 178332  Cd Length: 333  Bit Score: 166.36  E-value: 1.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  24 LDPFQRVIQPEEIWLYKNPLvQSDSIPTRLMFAISFLTPLaVICVVKIIRRTDRTEVKEAFLAVSLALALNGVCTNTIKL 103
Cdd:PLN02731   61 IHPFYRFVGKDMMTDLSYPL-KSNTVPIWSVPVYAMLLPL-VIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKN 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 104 IVGRPRPDFFYRCFPDG--VMNS--EMQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKLRCFTetGRGKSWRL 179
Cdd:PLN02731  139 AVGRPRPDFFWRCFPDGkaLYDSlgDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFD--GKGHVAKL 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 180 CAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQHYPPLANTACHKPYVSLRAPASLKKEERPVDSAPS 259
Cdd:PLN02731  217 CIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQ 296


                  ....
gi 1910870446 260 PPPE 263
Cdd:PLN02731  297 PPPQ 300
PLN02715 PLN02715
lipid phosphate phosphatase
 10-243 5.70e-44

lipid phosphate phosphatase


Pssm-ID: 178317 [Multi-domain]  Cd Length: 327  Bit Score: 151.74  E-value: 5.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  10 VRALLFGIFVLTEFLDPFQRVIQPEEIWLYKNPLvQSDSIPTRLMFAISFLTPLaVICVVKIIRRTDRTEVKEAFLAVSL 89
Cdd:PLN02715   53 ILVILIAIEIGLNLISPFYRYVGKDMMTDLKYPF-KDNTVPIWSVPVYAVLLPI-ILFVCFYLKRRCVYDLHHSILGLLF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  90 ALALNGVCTNTIKLIVGRPRPDFFYRCFPDGVMNSE----MQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGKL 165
Cdd:PLN02715  131 AVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDalggVICHGKAAEVKEGHKSFPSGHTSWSFAGLTFLSLYLSGKI 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910870446 166 RCFTETGRGKswRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQHYPPLANTACHKPYVSLRA 243
Cdd:PLN02715  211 KAFNGEGHVA--KLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCYRQFYPNPYHEEGWGPYAYFKA 286
PAP2_wunen cd03384
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ...
 84-221 1.17e-26

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: 101.17  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  84 FLAVSLA-LALNGVCTNTIKLIVGRPRPDFFYRCFPDG----------VMNSEMQCTGDPDLVSEGRKSFPSIHSSSAFS 152
Cdd:cd03384     5 FVGVFLFgLFATQLLTDLGKYVTGRLRPHFLDVCKPNYtdltcsldhqYIADCTCCTGDPDLIREARLSFPSGHASLSMY 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 153 GLGFTTFYLAGKLRcfteTGRGKSWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFA-YTC 221
Cdd:cd03384    85 AAVFLALYLQARLK----LRGSRLLRPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSVIAlFLV 150
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 83-222 2.39e-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: 97.15  E-value: 2.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  83 AFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGvmnsemqctgDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLA 162
Cdd:cd01610     4 LALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG----------DPLLLTEGGYSFPSGHAAFAFALALFLALLLP 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 163 GKLrcftetgrgksWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCY 222
Cdd:cd01610    74 RRL-----------LRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 86-226 1.32e-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: 89.79  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  86 AVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDgvmnsemqcTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLAGkl 165
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGL---------VPAPSTLPGLGYSFPSGHSATAFALALLLALLLRR-- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1910870446 166 rcftetgRGKSWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYRQHY 226
Cdd:pfam01569  70 -------LRKIVRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
83-222 7.19e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 74.30  E-value: 7.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446   83 AFLAVSLALAlngvcTNTIKLIVGRPRPDFFYRCFPdgvmnsemQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLA 162
Cdd:smart00014   1 ALLAVVSQLF-----NGVIKNYFGRPRPFFLSIGDA--------CCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLP 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  163 gklrcftetGRGKSWRLCAAILPLCCAtmIALSRLCDYKHHWQDSFVGGVIGLIFAYTCY 222
Cdd:smart00014  68 ---------ARAGRKLLIFLLLLLALV--VGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 81-219 7.19e-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: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  81 KEAFLAVSLALALNGVCTNTIKLIVGRPRPDffyrcfpdgvmnsemqctGDPDlvseGRKSFPSIHSSSAFSGLGFTTFY 160
Cdd:cd03394     2 REGLLILAEAAALTAAVTEGLKFAVGRARPD------------------GSNN----GYRSFPSGHTASAFAAATFLQYR 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1910870446 161 LagklrcftetgrGKSWRLCAAILPlccATMIALSRLCDYKHHWQDSFVGGVIGLIFAY 219
Cdd:cd03394    60 Y------------GWRWYGIPAYAL---ASLVGASRVVANRHWLSDVLAGAAIGILVGY 103
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 12-223 8.82e-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: 62.36  E-value: 8.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  12 ALLFGIFVLTEFLDPFQRVIQPEEIWLYKNPLVQSDSIPTRLMFAISFLTPLAVICVVKIIRRTDRTEVKEAFLAVSLAL 91
Cdd:COG0671     3 LALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  92 ALNGVCTNTIKLIVGRPRPDffyrcfpdgvmnseMQCTGDPDLVSEGRKSFPSIHSSSAFSGLGFTTFYLagklrcftet 171
Cdd:COG0671    83 LLLLLLLLLLKYLFGRPRPF--------------VVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLL---------- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1910870446 172 grgksWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYR 223
Cdd:COG0671   139 -----PRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLA 185
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 51-224 1.96e-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: 55.69  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  51 TRLMFAISFL------TPL-AVICVVKIIRRTDRtevkEAFLAVsLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGvmn 123
Cdd:cd03392    29 TAFMTAITFLgspavlLIIvLLLALLLLLKRRRR----AALFLL-LALLGGGALNTLLKLLVQRPRPPLHLLVPEGG--- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 124 semqctgdpdlvsegrKSFPSIHSSSAFSGLGFTTFYLAGKLrcftetgRGKSWRLCAAILPLCCATMIALSRLcdYKH- 202
Cdd:cd03392   101 ----------------YSFPSGHAMGATVLYGFLAYLLARRL-------PRRRVRILLLILAAILILLVGLSRL--YLGv 155

                         170       180
                  ....*....|....*....|....*.
gi 1910870446 203 HW-QD---SFVGGVIGLIFAYTCYRQ 224
Cdd:cd03392   156 HYpSDvlaGWLLGLAWLALLILLYRR 181
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 84-223 3.95e-08

PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239489  Cd Length: 177  Bit Score: 51.88  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  84 FLAVSLALAL-NGVCTNTIKLIVGRPRPdffyrCFPDGvmNSEMQCTGDPDlvseGRKSFPSIHSSSAFSGLGFTTFYLa 162
Cdd:cd03395    58 LLLVLLAVGFaDQLASGFLKPLVARLRP-----CNALD--GVRLVVLGDQG----GSYSFASSHAANSFALALFIWLFF- 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1910870446 163 gklrcftetgrgksWRLCAAILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYR 223
Cdd:cd03395   126 --------------RRGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFYL 172
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 89-223 7.87e-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: 48.09  E-value: 7.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  89 LALALNGVCTNTIKLIVGRPRPDFFyrcFPDGVMNSemqctgDPDLVSEGRKSFPSIHSSSAFSgLGFTTFYLAGKLRcf 168
Cdd:cd03389    76 ATVALSGILVNLLKFIIGRARPKLL---FDDGLYGF------DPFHADYAFTSFPSGHSATAGA-AAAALALLFPRYR-- 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910870446 169 tetgrgkswrlcaaILPLCCATMIALSRLCDYKHHWQDSFVGGVIGLIFAYTCYR 223
Cdd:cd03389   144 --------------WAFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQ 184
PAP2_like_6 cd03396
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 27-166 4.39e-03

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: 37.28  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  27 FQRVIQPEEIWLYKNPLVQSDSIPTRLM-----FAISFLTPLAVICVVKIIRRTDRtevkeAFLAVSLALALNGVCTNTI 101
Cdd:cd03396    12 FYDAGGGVFPFPLRHSWILETLLHLGGRllsiaLAVLLLALALLFFRRKRLRRRRR-----ALLLLILVIGLGLLVVAIL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1910870446 102 KLIVGRPRP----DF---FYRCFPDGVMNSEMqctgdpdlvsEGRKSFPSIHSSSAFSGLGFTTFYLAGKLR 166
Cdd:cd03396    87 KSHWGRPRPwdltEFggdAPYTPLFSGPSNGC----------GKGCSFPSGHASAGFALLALYFLFRRRRPR 148
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
 89-215 7.36e-03

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: 36.14  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  89 LALALNGVCTNTIKLIVGRPRPdffyrcfpdgVMNSemqcTGDPDLVSEGRKSFPSIHSSSAFSGLGF--TTFYLAGKLR 166
Cdd:cd03391    54 LGLLLDIITVAILKALVRRRRP----------AYNS----PDMLDYVAVDKYSFPSGHASRAAFVARFllNHLVLAVPLR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1910870446 167 cftetgrgkswrlcaaILPLCCATMIALSRLCDYKHHWQDSFVGGVIGL 215
Cdd:cd03391   120 ----------------VLLVLWATVVGISRVLLGRHHVLDVLAGAFLGY 152
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 55-222 8.99e-03

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: 36.10  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446  55 FAISFLTPLAVI--CVVKIIRRTDrtevKEAFLAVsLALALNGVCTNTIKLIVGRPRPdffyrCFPDGVMNSEmqctgdp 132
Cdd:cd03382    18 LAYLSLLPVAILvgYATLILFRRE----LEAIYLF-IGLLANEALNYVLKRIIKEPRP-----CSGAYFVRSG------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910870446 133 dlvsegrKSFPSIHSSsaFSGLGFTTFYLAGKLRCFTETGRGKSWRLCAAILPLCCAtmIALSRLCDYKHHWQDSFVGGV 212
Cdd:cd03382    81 -------YGMPSSHSQ--FMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALL--VSYSRVYLGYHTVSQVVVGAI 149

                         170
                  ....*....|
gi 1910870446 213 IGLIFAYTCY 222
Cdd:cd03382   150 VGILLGILWF 159
 
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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