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Conserved domains on  [gi|1958801884|ref|XP_038939310|]
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sphingosine-1-phosphate phosphatase 2 isoform X2 [Rattus norvegicus]

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130232)

type 2 phosphatidic acid phosphatase (PAP2) family protein is a type 2 lipid phosphate phosphatase, such as mammalian sphingosine-1-phosphate phosphatases and fungal dihydrosphingosine 1-phosphate phosphatase

CATH:  1.20.144.10
EC:  3.1.3.-
Gene Ontology:  GO:0042577|GO:0046839|GO:0008610
PubMed:  9122162|12447906|9260289
SCOP:  3001110|4001226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 39-171 3.15e-68

PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.


:

Pssm-ID: 239482  Cd Length: 151  Bit Score: 204.77  E-value: 3.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  39 YFYYYLFRFSAALGQEVFYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVIA-EYGM 117
Cdd:cd03388     1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801884 118 PSTHAMAATAISFTLLISTMDRYQYPFILGLIMAVVFSTLVSLSRLYTGMHTVL 171
Cdd:cd03388    81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVL 134
 
Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 39-171 3.15e-68

PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.


Pssm-ID: 239482  Cd Length: 151  Bit Score: 204.77  E-value: 3.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  39 YFYYYLFRFSAALGQEVFYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVIA-EYGM 117
Cdd:cd03388     1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801884 118 PSTHAMAATAISFTLLISTMDRYQYPFILGLIMAVVFSTLVSLSRLYTGMHTVL 171
Cdd:cd03388    81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVL 134
PLN02525 PLN02525
phosphatidic acid phosphatase family protein
 56-172 4.03e-18

phosphatidic acid phosphatase family protein


Pssm-ID: 215288  Cd Length: 352  Bit Score: 80.55  E-value: 4.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  56 FYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPV-----VKLEKRVIAEYGMPSTHAMAATAISF 130
Cdd:PLN02525   20 FYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVrrvtaTKDEEENAMEYGLPSSHTLNTVCLSG 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958801884 131 TLLISTMDRYQYP----FILGLIMAVVFSTLVSLSRLYTGMHTVLN 172
Cdd:PLN02525  100 YLLHYVLSYLQNVdasvIFAGLALFCLLVALVGFGRLYLGMHSPID 145
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 76-170 8.12e-09

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: 51.65  E-value: 8.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  76 LVVIWVLVMYIGQVAKDILKWPRPS-----SPPVVKLEKRVIAEYGMPSTHAMAATAISFTLLISTMDRYQYPFILGLIM 150
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALL 81

                          90       100
                  ....*....|....*....|
gi 1958801884 151 AVVFSTLVSLSRLYTGMHTV 170
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFP 101
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 55-168 6.05e-08

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: 50.42  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  55 VFYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVIAEYGMPSTHAMAATAISFTLLi 134
Cdd:COG0671    57 LLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLA- 135

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958801884 135 stmdrYQYPFILGLIMAVVFSTLVSLSRLYTGMH 168
Cdd:COG0671   136 -----LLLPRRWLAALLLALALLVGLSRVYLGVH 164
acidPPc smart00014
Acid phosphatase homologues;
81-168 2.02e-05

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 41.95  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884   81 VLVMYIGQVAKDILKW----PRP------SSPPVVKLEKRVIAEYGMPSTHAMAATAISFTLLISTMDRYQYPFILGLIM 150
Cdd:smart00014   1 ALLAVVSQLFNGVIKNyfgrPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL 80

                           90
                   ....*....|....*...
gi 1958801884  151 AVVFstLVSLSRLYTGMH 168
Cdd:smart00014  81 LLAL--VVGFSRVYLGAH 96
 
Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 39-171 3.15e-68

PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.


Pssm-ID: 239482  Cd Length: 151  Bit Score: 204.77  E-value: 3.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  39 YFYYYLFRFSAALGQEVFYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVIA-EYGM 117
Cdd:cd03388     1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801884 118 PSTHAMAATAISFTLLISTMDRYQYPFILGLIMAVVFSTLVSLSRLYTGMHTVL 171
Cdd:cd03388    81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVL 134
PLN02525 PLN02525
phosphatidic acid phosphatase family protein
 56-172 4.03e-18

phosphatidic acid phosphatase family protein


Pssm-ID: 215288  Cd Length: 352  Bit Score: 80.55  E-value: 4.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  56 FYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPV-----VKLEKRVIAEYGMPSTHAMAATAISF 130
Cdd:PLN02525   20 FYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVrrvtaTKDEEENAMEYGLPSSHTLNTVCLSG 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958801884 131 TLLISTMDRYQYP----FILGLIMAVVFSTLVSLSRLYTGMHTVLN 172
Cdd:PLN02525  100 YLLHYVLSYLQNVdasvIFAGLALFCLLVALVGFGRLYLGMHSPID 145
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 60-168 4.31e-12

PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria and archaea, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239487 [Multi-domain]  Cd Length: 125  Bit Score: 60.46  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  60 FLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVIAE-YGMPSTHAMAATAISFTLLISTMD 138
Cdd:cd03393     2 VLSLIYWLVDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYDGIQAIYEESAGgYGFPSGHAQTSATFWGSLMLHVRK 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958801884 139 RYQYpfilglIMAVVFSTLVSLSRLYTGMH 168
Cdd:cd03393    82 KWFT------LIGVVLVVLISFSRLYLGVH 105
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 76-171 7.84e-11

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: 57.09  E-value: 7.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  76 LVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVI----AEYGMPSTHAMAATAISFTLLISTmdRYQYPFILGLIMA 151
Cdd:cd01610     8 LLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLllteGGYSFPSGHAAFAFALALFLALLL--PRRLLRLLLGLLL 85

                          90       100
                  ....*....|....*....|
gi 1958801884 152 VVFSTLVSLSRLYTGMHTVL 171
Cdd:cd01610    86 LLLALLVGLSRVYLGVHYPS 105
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 76-170 8.12e-09

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: 51.65  E-value: 8.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  76 LVVIWVLVMYIGQVAKDILKWPRPS-----SPPVVKLEKRVIAEYGMPSTHAMAATAISFTLLISTMDRYQYPFILGLIM 150
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALL 81

                          90       100
                  ....*....|....*....|
gi 1958801884 151 AVVFSTLVSLSRLYTGMHTV 170
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFP 101
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 55-168 6.05e-08

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: 50.42  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  55 VFYITFLPFTHWNIDPYLSRRLVVIWVLVMYIGQVAKDILKWPRPSSPPVVKLEKRVIAEYGMPSTHAMAATAISFTLLi 134
Cdd:COG0671    57 LLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLA- 135

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958801884 135 stmdrYQYPFILGLIMAVVFSTLVSLSRLYTGMH 168
Cdd:COG0671   136 -----LLLPRRWLAALLLALALLVGLSRVYLGVH 164
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 55-170 1.60e-06

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: 46.11  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  55 VFYITFLPFThwnidpylsRRLVVIWVLvmyIGQVA--------KDILKWPRPSSPpvvklEKRVIAEYGMPSTHA--MA 124
Cdd:cd03382    30 VGYATLILFR---------RELEAIYLF---IGLLAnealnyvlKRIIKEPRPCSG-----AYFVRSGYGMPSSHSqfMG 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801884 125 ATAISFTLLISTMDRYQYPFILGLIMAVVF---STLVSLSRLYTGMHTV 170
Cdd:cd03382    93 FFAVYLLLFIYLRLGRLNSLVSRFLLSLGLlllALLVSYSRVYLGYHTV 141
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 74-168 1.39e-05

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: 43.75  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  74 RRLVVIWVLVMYIGQVAKDILKW----PRPSSPPVVklekrVIAEYGMPSTHAMAATAISFTLLI-----STMDRYQYPF 144
Cdd:cd03392    61 RRAALFLLLALLGGGALNTLLKLlvqrPRPPLHLLV-----PEGGYSFPSGHAMGATVLYGFLAYllarrLPRRRVRILL 135

                          90       100
                  ....*....|....*....|....
gi 1958801884 145 ILGLIMAVVfstLVSLSRLYTGMH 168
Cdd:cd03392   136 LILAAILIL---LVGLSRLYLGVH 156
acidPPc smart00014
Acid phosphatase homologues;
81-168 2.02e-05

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 41.95  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884   81 VLVMYIGQVAKDILKW----PRP------SSPPVVKLEKRVIAEYGMPSTHAMAATAISFTLLISTMDRYQYPFILGLIM 150
Cdd:smart00014   1 ALLAVVSQLFNGVIKNyfgrPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL 80

                           90
                   ....*....|....*...
gi 1958801884  151 AVVFstLVSLSRLYTGMH 168
Cdd:smart00014  81 LLAL--VVGFSRVYLGAH 96
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 34-168 2.09e-03

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: 37.24  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801884  34 HVVKNYFYYYLFRF--SAALGQEVFYITFLPFTHWNIDPYLsRRLVVIWVLVMYIGQVAKDILK----WPRPSSPPVVKL 107
Cdd:cd03395    15 GTLVHPLLDDLMPFltGKKLSVPIFLLLALFILFRKGPIGL-LILLLVLLAVGFADQLASGFLKplvaRLRPCNALDGVR 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801884 108 EKRVIAE---YGMPSTHAMAATAISFTLLIStmdryqYPFILGLIMAVVFSTLVSLSRLYTGMH 168
Cdd:cd03395    94 LVVLGDQggsYSFASSHAANSFALALFIWLF------FRRGLFSPVLLLWALLVGYSRVYVGVH 151
 
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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