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Conserved domains on  [gi|532474207|ref|WP_020967269|]
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phosphatase PAP2 family protein [Prevotella sp. oral taxon 299]

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130278)

type 2 phosphatidic acid phosphatase (PAP2) family protein similar to Helicobacter pylori lipid A 4'-phosphatase that removes the 4'-phosphate group from tetra- and hexa-acylated lipid A species

CATH:  1.20.144.10
EC:  3.1.3.-
Gene Ontology:  GO:0016791|GO:0016311|GO:0008610|GO:0006644
PubMed:  9122162|12447906|9260289
SCOP:  3001110|4001226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 130-232 9.37e-28

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: 107.03  E-value: 9.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 130 ALSNVLSLAFMGIATNGMKYSVRELRPDGSTR--NSFPSGHTAFAFAAATILHKEYGqtrSPLYSIAGYSLATLTGVGRV 207
Cdd:cd03394    5 LLILAEAAALTAAVTEGLKFAVGRARPDGSNNgyRSFPSGHTASAFAAATFLQYRYG---WRWYGIPAYALASLVGASRV 81

                         90       100
                 ....*....|....*....|....*
gi 532474207 208 LNNRHWVSDVLVGAGIGIVSTDLGY 232
Cdd:cd03394   82 VANRHWLSDVLAGAAIGILVGYLVT 106
 
Name Accession Description Interval E-value
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 130-232 9.37e-28

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: 107.03  E-value: 9.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 130 ALSNVLSLAFMGIATNGMKYSVRELRPDGSTR--NSFPSGHTAFAFAAATILHKEYGqtrSPLYSIAGYSLATLTGVGRV 207
Cdd:cd03394    5 LLILAEAAALTAAVTEGLKFAVGRARPDGSNNgyRSFPSGHTASAFAAATFLQYRYG---WRWYGIPAYALASLVGASRV 81

                         90       100
                 ....*....|....*....|....*
gi 532474207 208 LNNRHWVSDVLVGAGIGIVSTDLGY 232
Cdd:cd03394   82 VANRHWLSDVLAGAAIGILVGYLVT 106
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 106-234 7.10e-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: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 106 YVPLFGTWALKASGVEGRSSWKGLALSNVLSLAFMGIATNGMKYSVRELRPDG----------STRNSFPSGHTAFAFAA 175
Cdd:COG0671   51 LLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVvpdlelllgtAGGYSFPSGHAAAAFAL 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532474207 176 ATILHKEYGQTrspLYSIAGYSLATLTGVGRVLNNRHWVSDVLVGAGIGIVSTDLGYFL 234
Cdd:COG0671  131 ALVLALLLPRR---WLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 134-228 2.86e-10

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: 58.20  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207  134 VLSLAFMGIATNGMKYSVRELRPD---------------GSTRNSFPSGHTAFAFAAATILHKEYGQTRSPLYSIA---G 195
Cdd:pfam01569   3 LLALALAGLLSSVLKDYFGRPRPFflllegglvpapstlPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLallL 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 532474207  196 YSLATLTGVGRVLNNRHWVSDVLVGAGIGIVST 228
Cdd:pfam01569  83 LVLALLVGLSRLYLGVHFPSDVLAGALIGILLA 115
acidPPc smart00014
Acid phosphatase homologues;
134-226 3.28e-08

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 51.96  E-value: 3.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207   134 VLSLAFMGIATNGMKYSVRELRPDG----------------STRNSFPSGHTAFAFAAATILhKEYGQTR--SPLYSIAG 195
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFlsigdacctpnflltlEAGYSFPSGHTAFAFAFALFL-LLYLPARagRKLLIFLL 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 532474207   196 YSLATLTGVGRVLNNRHWVSDVLVGAGIGIV 226
Cdd:smart00014  80 LLLALVVGFSRVYLGAHWPSDVLAGSLLGIL 110
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
53-230 8.11e-03

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 37.56  E-value: 8.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207  53 KSFSRNAFNYnfsyvGLGFITSGFFI---KRQKDQFRSMRHYFTPHYSKSFDNYTQY-VPLFgtwalkasgvegRSSWKG 128
Cdd:PRK09597  16 KSFSKTLLAL-----SLGLILLGIFApfpKVPKQPSVPLAFHFTEHYARFIPTILSVaIPLI------------QRDAIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 129 LALSNVLSLAfMGIATNGMKYSVREL---------RPDGSTRNsFPSGHTAFAFAAATILHKEYGQTRspLYSIAgySLA 199
Cdd:PRK09597  79 LFQVANASIA-TTLLTHTTKRALNHVtindqrlgeRPYGGNFN-MPSGHSSMVGLAVAFLMRRYSFKK--YWWLL--PLI 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 532474207 200 TLTGVGRVLNNRHWVSDVLVGAGIGIVSTDL 230
Cdd:PRK09597 153 PLTMLARIYLDMHTIGAVLAGLGVGMLCVSL 183
 
Name Accession Description Interval E-value
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 130-232 9.37e-28

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: 107.03  E-value: 9.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 130 ALSNVLSLAFMGIATNGMKYSVRELRPDGSTR--NSFPSGHTAFAFAAATILHKEYGqtrSPLYSIAGYSLATLTGVGRV 207
Cdd:cd03394    5 LLILAEAAALTAAVTEGLKFAVGRARPDGSNNgyRSFPSGHTASAFAAATFLQYRYG---WRWYGIPAYALASLVGASRV 81

                         90       100
                 ....*....|....*....|....*
gi 532474207 208 LNNRHWVSDVLVGAGIGIVSTDLGY 232
Cdd:cd03394   82 VANRHWLSDVLAGAAIGILVGYLVT 106
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 126-232 4.91e-13

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: 65.94  E-value: 4.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 126 WKGLALSNVLSLAFMGIATNGMKYSVRELRPD--------------GSTRNSFPSGHTAFAFAAATILHKEYGQTRS-PL 190
Cdd:cd01610    1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYfllrcgpdgdplllTEGGYSFPSGHAAFAFALALFLALLLPRRLLrLL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 532474207 191 YSIAGYSLATLTGVGRVLNNRHWVSDVLVGAGIGIVSTDLGY 232
Cdd:cd01610   81 LGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 106-234 7.10e-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: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 106 YVPLFGTWALKASGVEGRSSWKGLALSNVLSLAFMGIATNGMKYSVRELRPDG----------STRNSFPSGHTAFAFAA 175
Cdd:COG0671   51 LLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVvpdlelllgtAGGYSFPSGHAAAAFAL 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532474207 176 ATILHKEYGQTrspLYSIAGYSLATLTGVGRVLNNRHWVSDVLVGAGIGIVSTDLGYFL 234
Cdd:COG0671  131 ALVLALLLPRR---WLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 134-228 2.86e-10

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: 58.20  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207  134 VLSLAFMGIATNGMKYSVRELRPD---------------GSTRNSFPSGHTAFAFAAATILHKEYGQTRSPLYSIA---G 195
Cdd:pfam01569   3 LLALALAGLLSSVLKDYFGRPRPFflllegglvpapstlPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLallL 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 532474207  196 YSLATLTGVGRVLNNRHWVSDVLVGAGIGIVST 228
Cdd:pfam01569  83 LVLALLVGLSRLYLGVHFPSDVLAGALIGILLA 115
acidPPc smart00014
Acid phosphatase homologues;
134-226 3.28e-08

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 51.96  E-value: 3.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207   134 VLSLAFMGIATNGMKYSVRELRPDG----------------STRNSFPSGHTAFAFAAATILhKEYGQTR--SPLYSIAG 195
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFlsigdacctpnflltlEAGYSFPSGHTAFAFAFALFL-LLYLPARagRKLLIFLL 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 532474207   196 YSLATLTGVGRVLNNRHWVSDVLVGAGIGIV 226
Cdd:smart00014  80 LLLALVVGFSRVYLGAHWPSDVLAGSLLGIL 110
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 109-234 1.65e-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: 51.55  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 109 LFGTWALKASGVEGRS---SWKGLALsnVLSLAFMGIATNGMKYSVRELRPD---------------GSTRNSFPSGHTA 170
Cdd:cd03389   49 RFGDLRGLSAPSRARFpkaAWAGLFL--FATVALSGILVNLLKFIIGRARPKllfddglygfdpfhaDYAFTSFPSGHSA 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532474207 171 FAFAAATILHKEYgqtrsPLYSIAGYSLATLTGVGRVLNNRHWVSDVLVGAGIGIVSTDLGYFL 234
Cdd:cd03389  127 TAGAAAAALALLF-----PRYRWAFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQR 185
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 142-234 1.21e-05

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: 46.10  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 142 IATNGMKYSVRELRPDGStrnSFPSGHTAFAFAAATILHKEYgqtRSPLYSIAGYSLATLTGVGRVLNNRHWVSDVLVGA 221
Cdd:cd03395   87 NALDGVRLVVLGDQGGSY---SFASSHAANSFALALFIWLFF---RRGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGA 160

                         90
                 ....*....|...
gi 532474207 222 GIGIVSTDLGYFL 234
Cdd:cd03395  161 LIGIISGLLFYLL 173
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
 129-227 6.65e-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: 43.46  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 129 LALsnVLSLAFMGIatngMKYSVRELRPDGSTRN----------SFPSGHTAFAFAAATILHKEYGQTRSPLYSIAGYsl 198
Cdd:cd03391   54 LGL--LLDIITVAI----LKALVRRRRPAYNSPDmldyvavdkySFPSGHASRAAFVARFLLNHLVLAVPLRVLLVLW-- 125

                         90       100
                 ....*....|....*....|....*....
gi 532474207 199 ATLTGVGRVLNNRHWVSDVLVGAGIGIVS 227
Cdd:cd03391  126 ATVVGISRVLLGRHHVLDVLAGAFLGYLE 154
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 113-226 4.79e-04

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: 41.44  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 113 WALKASGVEGRSSWKGLALSNVLSLAFMGIATNGMKYSVRELRPDGSTRN-----SFPSGHTAFAFAAATIL------HK 181
Cdd:cd03392   47 IVLLLALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVpeggySFPSGHAMGATVLYGFLayllarRL 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 532474207 182 EYGQTRSPLYSIAGySLATLTGVGRVLNNRHWVSDVLVGAGIGIV 226
Cdd:cd03392  127 PRRRVRILLLILAA-ILILLVGLSRLYLGVHYPSDVLAGWLLGLA 170
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
53-230 8.11e-03

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 37.56  E-value: 8.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207  53 KSFSRNAFNYnfsyvGLGFITSGFFI---KRQKDQFRSMRHYFTPHYSKSFDNYTQY-VPLFgtwalkasgvegRSSWKG 128
Cdd:PRK09597  16 KSFSKTLLAL-----SLGLILLGIFApfpKVPKQPSVPLAFHFTEHYARFIPTILSVaIPLI------------QRDAIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532474207 129 LALSNVLSLAfMGIATNGMKYSVREL---------RPDGSTRNsFPSGHTAFAFAAATILHKEYGQTRspLYSIAgySLA 199
Cdd:PRK09597  79 LFQVANASIA-TTLLTHTTKRALNHVtindqrlgeRPYGGNFN-MPSGHSSMVGLAVAFLMRRYSFKK--YWWLL--PLI 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 532474207 200 TLTGVGRVLNNRHWVSDVLVGAGIGIVSTDL 230
Cdd:PRK09597 153 PLTMLARIYLDMHTIGAVLAGLGVGMLCVSL 183
 
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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