NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|79314709|ref|NP_001030835|]
View 

Phosphatidic acid phosphatase (PAP2) family protein [Arabidopsis thaliana]

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130181)

type 2 phosphatidic acid phosphatase (PAP2) family protein similar to dolichyldiphosphatase, a membrane-associated protein located in the endoplasmic reticulum that hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 49-183 1.55e-39

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: 133.55  E-value: 1.55e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709  49 IVNRLSKWVVSVLFGSI--ILLRHDGAALWAVIGSISNSALSVVLKRILNQERPTT---TLRSDPGMPSSHAQSISFISV 123
Cdd:cd03382  17 LLAYLSLLPVAILVGYAtlILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSgayFVRSGYGMPSSHSQFMGFFAV 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79314709 124 FAVLSVMEWLGTNG---VSLFLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWY 183
Cdd:cd03382  97 YLLLFIYLRLGRLNslvSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILWF 159
 
Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 49-183 1.55e-39

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: 133.55  E-value: 1.55e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709  49 IVNRLSKWVVSVLFGSI--ILLRHDGAALWAVIGSISNSALSVVLKRILNQERPTT---TLRSDPGMPSSHAQSISFISV 123
Cdd:cd03382  17 LLAYLSLLPVAILVGYAtlILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSgayFVRSGYGMPSSHSQFMGFFAV 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79314709 124 FAVLSVMEWLGTNG---VSLFLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWY 183
Cdd:cd03382  97 YLLLFIYLRLGRLNslvSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILWF 159
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 76-185 1.48e-05

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: 43.18  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709    76 WAVIGSISNSALSVVLKRILNQERPTTTLR-------------SDPGMPSSHAQSISFISVFAVLSVMEWLGTNGVSLFL 142
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLegglvpapstlpgLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 79314709   143 SGLILALGsyFIRLRVSQKLHTSSQVVVGAIVGSLFCILWYTM 185
Cdd:pfam01569  81 LLLVLALL--VGLSRLYLGVHFPSDVLAGALIGILLALLVYRL 121
acidPPc smart00014
Acid phosphatase homologues;
78-183 2.97e-05

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 41.95  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709     78 VIGSISNSALSVVLKRILNQERPTT--------------TLRSDPGMPSSHAQSISFISVFAVLsvmeWLGTNGVSLFLS 143
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFlsigdacctpnfllTLEAGYSFPSGHTAFAFAFALFLLL----YLPARAGRKLLI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 79314709    144 GLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWY 183
Cdd:smart00014  77 FLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
 
Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 49-183 1.55e-39

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: 133.55  E-value: 1.55e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709  49 IVNRLSKWVVSVLFGSI--ILLRHDGAALWAVIGSISNSALSVVLKRILNQERPTT---TLRSDPGMPSSHAQSISFISV 123
Cdd:cd03382  17 LLAYLSLLPVAILVGYAtlILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSgayFVRSGYGMPSSHSQFMGFFAV 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79314709 124 FAVLSVMEWLGTNG---VSLFLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWY 183
Cdd:cd03382  97 YLLLFIYLRLGRLNslvSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILWF 159
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 73-183 1.14e-08

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: 51.69  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709  73 AALWAVIGSISNSALSVVLKRILNQERPTTTLR------------SDPGMPSSHAQsisfISVFAVLSVMEWLGTNGVSL 140
Cdd:cd01610   4 LALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRcgpdgdplllteGGYSFPSGHAA----FAFALALFLALLLPRRLLRL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 79314709 141 FLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWY 183
Cdd:cd01610  80 LLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 76-185 1.48e-05

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: 43.18  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709    76 WAVIGSISNSALSVVLKRILNQERPTTTLR-------------SDPGMPSSHAQSISFISVFAVLSVMEWLGTNGVSLFL 142
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLegglvpapstlpgLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 79314709   143 SGLILALGsyFIRLRVSQKLHTSSQVVVGAIVGSLFCILWYTM 185
Cdd:pfam01569  81 LLLVLALL--VGLSRLYLGVHFPSDVLAGALIGILLALLVYRL 121
acidPPc smart00014
Acid phosphatase homologues;
78-183 2.97e-05

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 41.95  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709     78 VIGSISNSALSVVLKRILNQERPTT--------------TLRSDPGMPSSHAQSISFISVFAVLsvmeWLGTNGVSLFLS 143
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFlsigdacctpnfllTLEAGYSFPSGHTAFAFAFALFLLL----YLPARAGRKLLI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 79314709    144 GLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWY 183
Cdd:smart00014  77 FLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 75-178 3.92e-04

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: 38.85  E-value: 3.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314709  75 LWAVIGSISNSALSV-VLKRILNQERPTTTLRSDPGMPSSHAqsisfISVFAVLSVMEWLGTNGvslfLSGLIL-ALGSY 152
Cdd:cd03394   5 LLILAEAAALTAAVTeGLKFAVGRARPDGSNNGYRSFPSGHT-----ASAFAAATFLQYRYGWR----WYGIPAyALASL 75

                        90       100
                ....*....|....*....|....*.
gi 79314709 153 FIRLRVSQKLHTSSQVVVGAIVGSLF 178
Cdd:cd03394  76 VGASRVVANRHWLSDVLAGAAIGILV 101
PAP2_diacylglycerolkinase cd03383
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ...
 109-181 1.76e-03

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: 36.92  E-value: 1.76e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79314709 109 GMPSSHAqSISFiSVFAVLSVMEwlgtngVSLFLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCIL 181
Cdd:cd03383  40 GMPSGHA-AIAF-SIATAISLIT------NNPIISILSVLLAVMVAHSRVEMKIHTMWEVVVGAILGALITLL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH