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Conserved domains on  [gi|1333675752|ref|XP_023498189|]
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sphingosine-1-phosphate phosphatase 2 isoform X2 [Equus caballus]

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130232)

type 2 phosphatidic acid phosphatase (PAP2) 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.-
PubMed:  9122162
SCOP:  3001110

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 ...
 66-172 3.94e-47

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: 156.24  E-value: 3.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  66 LVMYVGQVAKDILKWPRPFSPPVVRLEKRLIA-EYGMPSTHAMAATAIPFTILISTVDRYQYPFVWGLIVAVVFSTLVCL 144
Cdd:cd03388    44 LGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGFPSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCL 123

                          90       100
                  ....*....|....*....|....*...
gi 1333675752 145 SRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:cd03388   124 SRIYMGMHSVLDVIAGSLIGVLILLFRF 151
 
Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 66-172 3.94e-47

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: 156.24  E-value: 3.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  66 LVMYVGQVAKDILKWPRPFSPPVVRLEKRLIA-EYGMPSTHAMAATAIPFTILISTVDRYQYPFVWGLIVAVVFSTLVCL 144
Cdd:cd03388    44 LGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGFPSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCL 123

                          90       100
                  ....*....|....*....|....*...
gi 1333675752 145 SRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:cd03388   124 SRIYMGMHSVLDVIAGSLIGVLILLFRF 151
PLN02525 PLN02525
phosphatidic acid phosphatase family protein
 69-289 5.08e-16

phosphatidic acid phosphatase family protein


Pssm-ID: 215288  Cd Length: 352  Bit Score: 77.86  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  69 YVGQVAKDILKWPRPFSPPVVRL-----EKRLIAEYGMPSTHAMAATAIPFTIL--ISTVDRYQYPFVW--GLIVAVVFS 139
Cdd:PLN02525   49 YVGNCIKDVVSAPRPSCPPVRRVtatkdEEENAMEYGLPSSHTLNTVCLSGYLLhyVLSYLQNVDASVIfaGLALFCLLV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752 140 TLVCLSRLYTGMHTVLDVLGGILITMILIVLtypaW-TLIDHLNS-------ASPLFpvcvIVVPFFLCYNYPVSEYYSP 211
Cdd:PLN02525  129 ALVGFGRLYLGMHSPIDIIAGLAIGLVILAF----WlTVDEYVDAfitsgqnVTPFW----AALSFLLLFAYPTPEFPTP 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333675752 212 TRADTTTILAAGAGMIIGFWiNHFFQLVSEPI-ESFPVIQNIPPLTTDMLvlgltkftVGIVLIFLVRQLVQNLSLQVL 289
Cdd:PLN02525  201 SFEYHTAFNGVAFGIVAGVQ-QTYSQFHHEAApRIFSPQLPIAAFLGRVA--------VGIPTILAVKFCSKALAKWLL 270
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 66-172 2.72e-13

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: 65.90  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  66 LVMYVGQVAKDILKWPRPF-----SPPVVRLEKRLIAEYGMPSTHAMAATAIPFTILISTVDRYQYPFVWGLIVAVVFST 140
Cdd:pfam01569   8 LAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALLLLVLAL 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1333675752 141 LVCLSRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:pfam01569  88 LVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 55-175 1.61e-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: 62.36  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  55 AHGLRRVTASQLVMYVGQVAKDILKWPRPFSPPVVRLEKRLIAEYGMPSTHAMAATAIpFTILIstvdrYQYPFVWGLIV 134
Cdd:COG0671    73 LLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFAL-ALVLA-----LLLPRRWLAAL 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1333675752 135 AVVFSTLVCLSRLYTGMHTVLDVLGGILITMILIVLTYPAW 175
Cdd:COG0671   147 LLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALL 187
acidPPc smart00014
Acid phosphatase homologues;
65-172 3.08e-09

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 54.27  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752   65 QLVMYVGQVAKDILKW----PRPF------SPPVVRLEKRLIAEYGMPSTHAMAATAipFTILISTVDRYQYPFVWGLIV 134
Cdd:smart00014   1 ALLAVVSQLFNGVIKNyfgrPRPFflsigdACCTPNFLLTLEAGYSFPSGHTAFAFA--FALFLLLYLPARAGRKLLIFL 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1333675752  135 AVVFSTLVCLSRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:smart00014  79 LLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
 
Name Accession Description Interval E-value
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 66-172 3.94e-47

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: 156.24  E-value: 3.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  66 LVMYVGQVAKDILKWPRPFSPPVVRLEKRLIA-EYGMPSTHAMAATAIPFTILISTVDRYQYPFVWGLIVAVVFSTLVCL 144
Cdd:cd03388    44 LGMYIGQFIKDLFCLPRPSSPPVVRLTMSSAAlEYGFPSTHAMNATAISFYLLIYLYDRYQYPFVLGLILALFYSTLVCL 123

                          90       100
                  ....*....|....*....|....*...
gi 1333675752 145 SRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:cd03388   124 SRIYMGMHSVLDVIAGSLIGVLILLFRF 151
PLN02525 PLN02525
phosphatidic acid phosphatase family protein
 69-289 5.08e-16

phosphatidic acid phosphatase family protein


Pssm-ID: 215288  Cd Length: 352  Bit Score: 77.86  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  69 YVGQVAKDILKWPRPFSPPVVRL-----EKRLIAEYGMPSTHAMAATAIPFTIL--ISTVDRYQYPFVW--GLIVAVVFS 139
Cdd:PLN02525   49 YVGNCIKDVVSAPRPSCPPVRRVtatkdEEENAMEYGLPSSHTLNTVCLSGYLLhyVLSYLQNVDASVIfaGLALFCLLV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752 140 TLVCLSRLYTGMHTVLDVLGGILITMILIVLtypaW-TLIDHLNS-------ASPLFpvcvIVVPFFLCYNYPVSEYYSP 211
Cdd:PLN02525  129 ALVGFGRLYLGMHSPIDIIAGLAIGLVILAF----WlTVDEYVDAfitsgqnVTPFW----AALSFLLLFAYPTPEFPTP 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333675752 212 TRADTTTILAAGAGMIIGFWiNHFFQLVSEPI-ESFPVIQNIPPLTTDMLvlgltkftVGIVLIFLVRQLVQNLSLQVL 289
Cdd:PLN02525  201 SFEYHTAFNGVAFGIVAGVQ-QTYSQFHHEAApRIFSPQLPIAAFLGRVA--------VGIPTILAVKFCSKALAKWLL 270
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 66-172 4.33e-15

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: 70.57  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  66 LVMYVGQVAKDILKWPRPFSPPVVRLEKRLI----AEYGMPSTHAMAATAIPFTILISTVDRYQYPFVWglIVAVVFSTL 141
Cdd:cd01610    14 AGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLllteGGYSFPSGHAAFAFALALFLALLLPRRLLRLLLG--LLLLLLALL 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1333675752 142 VCLSRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:cd01610    92 VGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 66-172 2.72e-13

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: 65.90  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  66 LVMYVGQVAKDILKWPRPF-----SPPVVRLEKRLIAEYGMPSTHAMAATAIPFTILISTVDRYQYPFVWGLIVAVVFST 140
Cdd:pfam01569   8 LAGLLSSVLKDYFGRPRPFfllleGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLALLLLVLAL 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1333675752 141 LVCLSRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:pfam01569  88 LVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 55-175 1.61e-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: 62.36  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  55 AHGLRRVTASQLVMYVGQVAKDILKWPRPFSPPVVRLEKRLIAEYGMPSTHAMAATAIpFTILIstvdrYQYPFVWGLIV 134
Cdd:COG0671    73 LLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGHAAAAFAL-ALVLA-----LLLPRRWLAAL 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1333675752 135 AVVFSTLVCLSRLYTGMHTVLDVLGGILITMILIVLTYPAW 175
Cdd:COG0671   147 LLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALL 187
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 57-170 6.65e-11

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: 58.92  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  57 GLRRVTASQLVMYVGQVAKDILKWPRPFSPPVVRLEKRLIAE-YGMPSTHAMAATaipfTILISTVDRYQYPFVWglIVA 135
Cdd:cd03393    15 GRYLGLALCASGYLNAALKEVFKIPRPFTYDGIQAIYEESAGgYGFPSGHAQTSA----TFWGSLMLHVRKKWFT--LIG 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1333675752 136 VVFSTLVCLSRLYTGMHTVLDVLGGILITMILIVL 170
Cdd:cd03393    89 VVLVVLISFSRLYLGVHWPSDVIGGVLIGLLVLVL 123
acidPPc smart00014
Acid phosphatase homologues;
65-172 3.08e-09

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 54.27  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752   65 QLVMYVGQVAKDILKW----PRPF------SPPVVRLEKRLIAEYGMPSTHAMAATAipFTILISTVDRYQYPFVWGLIV 134
Cdd:smart00014   1 ALLAVVSQLFNGVIKNyfgrPRPFflsigdACCTPNFLLTLEAGYSFPSGHTAFAFA--FALFLLLYLPARAGRKLLIFL 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1333675752  135 AVVFSTLVCLSRLYTGMHTVLDVLGGILITMILIVLTY 172
Cdd:smart00014  79 LLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
 81-166 1.57e-06

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: 46.87  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  81 PRPFSPPVVRLEKRLIAEYGMPSTHAMAATAIPFTILIstvdryqYPFVWGLIVAVVFSTLVCLSRLYTGMHTVLDVLGG 160
Cdd:cd03385    59 PRPFVVGLGHNLLPHAADSSFPSDHTTLFFSIAFSLLL-------RRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGA 131


                  ....*.
gi 1333675752 161 ILITMI 166
Cdd:cd03385   132 ALVAVL 137
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 56-178 1.71e-06

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: 47.64  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  56 HGLRRVTASQL-VMYVGQVAKDILK----WPRP-FSPPVVRLEKRLIA--EYGMPSTHAMAATAIPFTILIStvdryqYP 127
Cdd:cd03395    53 IGLLILLLVLLaVGFADQLASGFLKplvaRLRPcNALDGVRLVVLGDQggSYSFASSHAANSFALALFIWLF------FR 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333675752 128 FVWGLIVAVVFSTLVCLSRLYTGMHTVLDVLGGILITMILIVLTYPAWTLI 178
Cdd:cd03395   127 RGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFYLLFSWL 177
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 70-178 2.93e-06

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: 46.83  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  70 VGQVAKDILKWPRPFSPPVVRLEKrliaeYGMPSTHAMAATAIPFTILISTVDRYQYPF--VWGLIVAVVFSTLVCLSRL 147
Cdd:cd03392    77 LNTLLKLLVQRPRPPLHLLVPEGG-----YSFPSGHAMGATVLYGFLAYLLARRLPRRRvrILLLILAAILILLVGLSRL 151

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1333675752 148 YTGMHTVLDVLGGILITMILIVLTYPAWTLI 178
Cdd:cd03392   152 YLGVHYPSDVLAGWLLGLAWLALLILLYRRL 182
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 73-163 8.56e-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: 45.34  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333675752  73 VAKDILKWPRPFSPpvvrlEKRLIAEYGMPSTHA--MAATAIPFTILISTVDRYQYPFVWGLIVAVVF---STLVCLSRL 147
Cdd:cd03382    60 VLKRIIKEPRPCSG-----AYFVRSGYGMPSSHSqfMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLlllALLVSYSRV 134

                          90
                  ....*....|....*.
gi 1333675752 148 YTGMHTVLDVLGGILI 163
Cdd:cd03382   135 YLGYHTVSQVVVGAIV 150
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 100-167 2.50e-03

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 38.90  E-value: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333675752 100 GMPSTHAMAATAIPFTILISTVD--------RYQYPFVWGLIVAVVFStlVCLSRLYTGMHTVLDVLGGILITMIL 167
Cdd:cd03381    73 GSPSGHAMGTTAVLLVMVTALLShlagrkrsRFLRVMLWLVFWGVQLA--VCLSRIYLAAHFPHQVIAGVISGIAV 146
PAP2_diacylglycerolkinase cd03383
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ...
 100-170 4.08e-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: 36.54  E-value: 4.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333675752 100 GMPSTHAMAATAIPFTILISTVDryqyPFVwgLIVAVVFSTLVCLSRLYTGMHTVLDVLG----GILITMILIVL 170
Cdd:cd03383    40 GMPSGHAAIAFSIATAISLITNN----PII--SILSVLLAVMVAHSRVEMKIHTMWEVVVgailGALITLLIFKI 108
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
97-170 5.44e-03

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 37.56  E-value: 5.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333675752  97 AEYGMPSTHA-MAATAIPFTIlistvDRYQYPFVWGLIVAVVfstLVCLSRLYTGMHTVLDVLGGILITMILIVL 170
Cdd:PRK09597  117 GNFNMPSGHSsMVGLAVAFLM-----RRYSFKKYWWLLPLIP---LTMLARIYLDMHTIGAVLAGLGVGMLCVSL 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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