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Conserved domains on  [gi|23510289|ref|NP_689599|]
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sphingosine-1-phosphate phosphatase 2 isoform a [Homo sapiens]

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
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 ...
84-233 4.60e-72

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: 222.49  E-value: 4.60e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  84 YFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIA-EYGM 162
Cdd:cd03388   1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510289 163 PSTHAMAATAIAFTLLISTMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:cd03388  81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
 
Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
84-233 4.60e-72

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: 222.49  E-value: 4.60e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  84 YFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIA-EYGM 162
Cdd:cd03388   1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510289 163 PSTHAMAATAIAFTLLISTMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:cd03388  81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
PLN02525 PLN02525
phosphatidic acid phosphatase family protein
101-350 3.85e-25

phosphatidic acid phosphatase family protein


Pssm-ID: 215288  Cd Length: 352  Bit Score: 104.82  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  101 FYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPV-----VKLEKRLIAEYGMPSTHAMAATAIAF 175
Cdd:PLN02525  20 FYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVrrvtaTKDEEENAMEYGLPSSHTLNTVCLSG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  176 TLLISTMDRYQYP----FVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLtypaWTFIDC-LDS------ 244
Cdd:PLN02525 100 YLLHYVLSYLQNVdasvIFAGLALFCLLVALVGFGRLYLGMHSPIDIIAGLAIGLVILAF----WLTVDEyVDAfitsgq 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  245 -ASPLFpvcvIVVPFFLCYNYPVSDYYSPTRADTTtilaAGAGVTIG--FWINHFFQlvSKPAESLPVIQNiPPLTTYML 321
Cdd:PLN02525 176 nVTPFW----AALSFLLLFAYPTPEFPTPSFEYHT----AFNGVAFGivAGVQQTYS--QFHHEAAPRIFS-PQLPIAAF 244
                        250       260
                 ....*....|....*....|....*....
gi 23510289  322 vlgLTKFAVGIVLILLVRQLVQNLSLQVL 350
Cdd:PLN02525 245 ---LGRVAVGIPTILAVKFCSKALAKWLL 270
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
121-233 2.30e-14

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: 69.37  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289   121 LIIIWVLVMYIGQVAKDVLKWPRPS-----SPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLISTMDRYQYPFVLGLVM 195
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALL 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 23510289   196 AVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
100-236 4.06e-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: 64.68  E-value: 4.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 100 VFYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLi 179
Cdd:COG0671  57 LLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLA- 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23510289 180 stmdrYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAW 236
Cdd:COG0671 136 -----LLLPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALL 187
acidPPc smart00014
Acid phosphatase homologues;
126-233 1.08e-09

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 55.82  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289    126 VLVMYIGQVAKDVLKW----PRP------SSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLISTMDRYQYPFVLGLVM 195
Cdd:smart00014   1 ALLAVVSQLFNGVIKNyfgrPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 23510289    196 AVVFstLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:smart00014  81 LLAL--VVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
 
Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
84-233 4.60e-72

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: 222.49  E-value: 4.60e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  84 YFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIA-EYGM 162
Cdd:cd03388   1 PFLDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510289 163 PSTHAMAATAIAFTLLISTMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:cd03388  81 PSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
PLN02525 PLN02525
phosphatidic acid phosphatase family protein
101-350 3.85e-25

phosphatidic acid phosphatase family protein


Pssm-ID: 215288  Cd Length: 352  Bit Score: 104.82  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  101 FYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPV-----VKLEKRLIAEYGMPSTHAMAATAIAF 175
Cdd:PLN02525  20 FYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVrrvtaTKDEEENAMEYGLPSSHTLNTVCLSG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  176 TLLISTMDRYQYP----FVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLtypaWTFIDC-LDS------ 244
Cdd:PLN02525 100 YLLHYVLSYLQNVdasvIFAGLALFCLLVALVGFGRLYLGMHSPIDIIAGLAIGLVILAF----WLTVDEyVDAfitsgq 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289  245 -ASPLFpvcvIVVPFFLCYNYPVSDYYSPTRADTTtilaAGAGVTIG--FWINHFFQlvSKPAESLPVIQNiPPLTTYML 321
Cdd:PLN02525 176 nVTPFW----AALSFLLLFAYPTPEFPTPSFEYHT----AFNGVAFGivAGVQQTYS--QFHHEAAPRIFS-PQLPIAAF 244
                        250       260
                 ....*....|....*....|....*....
gi 23510289  322 vlgLTKFAVGIVLILLVRQLVQNLSLQVL 350
Cdd:PLN02525 245 ---LGRVAVGIPTILAVKFCSKALAKWLL 270
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
121-233 3.31e-16

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: 74.42  E-value: 3.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 121 LIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLI----AEYGMPSTHAMAATAIAFTLLISTMDRYQYPFVLGLvmA 196
Cdd:cd01610   8 LLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLllteGGYSFPSGHAAFAFALALFLALLLPRRLLRLLLGLL--L 85
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 23510289 197 VVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:cd01610  86 LLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
105-231 1.68e-15

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: 72.40  E-value: 1.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 105 FLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAE-YGMPSTHAMAATAIAFTLLISTMD 183
Cdd:cd03393   2 VLSLIYWLVDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYDGIQAIYEESAGgYGFPSGHAQTSATFWGSLMLHVRK 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 23510289 184 RYQYPFvlglvmAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVL 231
Cdd:cd03393  82 KWFTLI------GVVLVVLISFSRLYLGVHWPSDVIGGVLIGLLVLVL 123
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
121-233 2.30e-14

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: 69.37  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289   121 LIIIWVLVMYIGQVAKDVLKWPRPS-----SPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLISTMDRYQYPFVLGLVM 195
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALL 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 23510289   196 AVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
100-236 4.06e-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: 64.68  E-value: 4.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 100 VFYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLi 179
Cdd:COG0671  57 LLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLA- 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23510289 180 stmdrYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAW 236
Cdd:COG0671 136 -----LLLPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALL 187
acidPPc smart00014
Acid phosphatase homologues;
126-233 1.08e-09

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 55.82  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289    126 VLVMYIGQVAKDVLKW----PRP------SSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLISTMDRYQYPFVLGLVM 195
Cdd:smart00014   1 ALLAVVSQLFNGVIKNyfgrPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 23510289    196 AVVFstLVCLSRLYTGMHTVLDVLGGVLITALLIVLTY 233
Cdd:smart00014  81 LLAL--VVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
119-235 1.62e-08

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: 53.77  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 119 RRLIIIWVLVMYIGQVAKDVLKW----PRPSSPPVVklekrLIAEYGMPSTHAMAATAIAFTLLI-----STMDRYQYPF 189
Cdd:cd03392  61 RRAALFLLLALLGGGALNTLLKLlvqrPRPPLHLLV-----PEGGYSFPSGHAMGATVLYGFLAYllarrLPRRRVRILL 135
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 23510289 190 VLGLVMAVVfstLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPA 235
Cdd:cd03392 136 LILAAILIL---LVGLSRLYLGVHYPSDVLAGWLLGLAWLALLILL 178
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
100-228 2.37e-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: 53.05  E-value: 2.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 100 VFYITFLPFThwnidpylsRRLIIIWVLvmyIGQVA--------KDVLKWPRPSSPpvvklEKRLIAEYGMPSTHA--MA 169
Cdd:cd03382  30 VGYATLILFR---------RELEAIYLF---IGLLAnealnyvlKRIIKEPRPCSG-----AYFVRSGYGMPSSHSqfMG 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510289 170 ATAIAFTLLISTMDRYQYPFVLGLVMAVVF---STLVCLSRLYTGMHTVLDVLGGVLITALL 228
Cdd:cd03382  93 FFAVYLLLFIYLRLGRLNSLVSRFLLSLGLlllALLVSYSRVYLGYHTVSQVVVGAIVGILL 154
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
101-239 4.60e-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: 52.65  E-value: 4.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 101 FYITFLPFTHWNIDPYLsRRLIIIWVLVMYIGQVAKDVLK----WPRPSSPPVVKLEKRLIAE---YGMPSTHAMAATAI 173
Cdd:cd03395  39 FLLLALFILFRKGPIGL-LILLLVLLAVGFADQLASGFLKplvaRLRPCNALDGVRLVVLGDQggsYSFASSHAANSFAL 117
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23510289 174 AFTLLIStmdryqYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAWTFI 239
Cdd:cd03395 118 ALFIWLF------FRRGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFYLLFSWL 177
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
126-227 3.16e-05

PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as bacitracin transport permeases, as it was suspected that they form the permease component of an ABC transporter system. It was shown, however, that BcrC from Bacillus subtilis posesses undecaprenyl pyrophosphate (UPP) phospatase activity, and it is hypothesized that it competes with bacitracin for UPP, increasing the cell's resistance to bacitracin.


Pssm-ID: 239480  Cd Length: 144  Bit Score: 43.40  E-value: 3.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289 126 VLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLIStmdRYQYPFVLGLVMAVvfstLVCL 205
Cdd:cd03385  43 AVALLINYIIGLLYFHPRPFVVGLGHNLLPHAADSSFPSDHTTLFFSIAFSLLLR---RRKWAGWILLILAL----LVAW 115
                        90       100
                ....*....|....*....|..
gi 23510289 206 SRLYTGMHTVLDVLGGVLITAL 227
Cdd:cd03385 116 SRIYLGVHYPLDMLGAALVAVL 137
PAP2_diacylglycerolkinase cd03383
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ...
161-231 3.15e-04

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: 40.00  E-value: 3.15e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510289 161 GMPSTHAMAATAIAFTLLISTMDryqyPFVLGLVMAVVFstLVCLSRLYTGMHTVLDVLGGVLITALLIVL 231
Cdd:cd03383  40 GMPSGHAAIAFSIATAISLITNN----PIISILSVLLAV--MVAHSRVEMKIHTMWEVVVGAILGALITLL 104
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
161-234 1.94e-03

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: 38.84  E-value: 1.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23510289 161 GMPSTHAMAATAIAFTLLIsTMDRYQYPFVLGLVmavvfstLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYP 234
Cdd:cd03389 119 SFPSGHSATAGAAAAALAL-LFPRYRWAFILLAL-------LIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQ 184
PAP2_3 pfam14378
PAP2 superfamily;
162-231 4.03e-03

PAP2 superfamily;


Pssm-ID: 433919  Cd Length: 190  Bit Score: 38.09  E-value: 4.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510289   162 MPSTHAmaATAIAFTLLISTMDRYQYPFVLGLVMAVvfstLVCLSRLYTGMHTVLDVLGGVLITALLIVL 231
Cdd:pfam14378 127 MPSLHV--AWALLCALALWRLRRTRILRWLAVAYNV----LMIVSTVATGNHYLLDVVAGVALALAAIAL 190
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
158-231 5.30e-03

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 37.95  E-value: 5.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23510289  158 AEYGMPSTHA-MAATAIAFTllistMDRYQYPFVLGLVMAVVfstLVCLSRLYTGMHTVLDVLGGVLITALLIVL 231
Cdd:PRK09597 117 GNFNMPSGHSsMVGLAVAFL-----MRRYSFKKYWWLLPLIP---LTMLARIYLDMHTIGAVLAGLGVGMLCVSL 183
PRK10699 PRK10699
phosphatidylglycerophosphatase B; Provisional
160-231 6.19e-03

phosphatidylglycerophosphatase B; Provisional


Pssm-ID: 182658  Cd Length: 244  Bit Score: 38.09  E-value: 6.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23510289  160 YGMPSTHAM-AAT--AIAFTLListMDRYQYPFVlglVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVL 231
Cdd:PRK10699 157 FAFPSGHTMfAASwaLLAVGLL---WPRRRYKTV---ALLMLWATGVMGSRLLLGMHWPRDLVVATLISWLLVTV 225
 
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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