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Conserved domains on  [gi|398365285|ref|NP_011550|]
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dolichyldiphosphatase [Saccharomyces cerevisiae S288C]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 17-179 6.29e-64

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: 196.34  E-value: 6.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  17 FDDTYILYDSHDFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFgasfqND 96
Cdd:cd03382    1 FSLTHVLYDPGDLLSFLLAYLSLLPVAILVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSG-----AY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  97 TIRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLN-FLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTG 175
Cdd:cd03382   76 FVRSGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNsLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLG 155


                 ....
gi 398365285 176 SLYF 179
Cdd:cd03382  156 ILWF 159
 
Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 17-179 6.29e-64

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: 196.34  E-value: 6.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  17 FDDTYILYDSHDFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFgasfqND 96
Cdd:cd03382    1 FSLTHVLYDPGDLLSFLLAYLSLLPVAILVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSG-----AY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  97 TIRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLN-FLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTG 175
Cdd:cd03382   76 FVRSGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNsLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLG 155


                 ....
gi 398365285 176 SLYF 179
Cdd:cd03382  156 ILWF 159
acidPPc smart00014
Acid phosphatase homologues;
64-179 2.87e-21

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 85.48  E-value: 2.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285    64 AFGQLMNEIFNNVIKNIIKQPRP------VSFGASFQNDTIRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLNFlekci 137
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLL----- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 398365285   138 fSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYF 179
Cdd:smart00014  76 -IFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 62-182 2.47e-12

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: 62.05  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285   62 IVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFQNDT-----IRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLNFLEKC 136
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPapstlPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 398365285  137 IFsgalALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYFFIV 182
Cdd:pfam01569  81 LL----LVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLV 122
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 15-182 3.06e-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: 51.96  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  15 IPFDDTYILYDSHDFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFQ 94
Cdd:COG0671   30 LLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  95 NDTIRSGYGMPSAHSQfMGFCFtynslkiYTSWknLNFLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALT 174
Cdd:COG0671  110 LLGTAGGYSFPSGHAA-AAFAL-------ALVL--ALLLPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAI 179


                 ....*...
gi 398365285 175 GSLYFFIV 182
Cdd:COG0671  180 ALLLLALL 187
 
Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 17-179 6.29e-64

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: 196.34  E-value: 6.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  17 FDDTYILYDSHDFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFgasfqND 96
Cdd:cd03382    1 FSLTHVLYDPGDLLSFLLAYLSLLPVAILVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSG-----AY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  97 TIRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLN-FLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTG 175
Cdd:cd03382   76 FVRSGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNsLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLG 155


                 ....
gi 398365285 176 SLYF 179
Cdd:cd03382  156 ILWF 159
acidPPc smart00014
Acid phosphatase homologues;
64-179 2.87e-21

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 85.48  E-value: 2.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285    64 AFGQLMNEIFNNVIKNIIKQPRP------VSFGASFQNDTIRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLNFlekci 137
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLL----- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 398365285   138 fSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYF 179
Cdd:smart00014  76 -IFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 56-179 3.82e-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: 72.11  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  56 RELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFQNDTIR----SGYGMPSAHSQFMGFCFTYnsLKIYTSWKnln 131
Cdd:cd01610    1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLllteGGYSFPSGHAAFAFALALF--LALLLPRR--- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 398365285 132 fLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYF 179
Cdd:cd01610   76 -LLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 62-182 2.47e-12

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: 62.05  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285   62 IVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFQNDT-----IRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLNFLEKC 136
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPapstlPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 398365285  137 IFsgalALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYFFIV 182
Cdd:pfam01569  81 LL----LVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLV 122
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 39-180 6.42e-09

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: 6.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  39 LMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFqndtiRSGYGMPSAHSqfMGFCFTY 118
Cdd:cd03392   43 VLLIIVLLLALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVP-----EGGYSFPSGHA--MGATVLY 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365285 119 NSLKIYTSWKNLNFLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGA--LTGSLYFF 180
Cdd:cd03392  116 GFLAYLLARRLPRRRVRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLLGLawLALLILLY 179
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 15-182 3.06e-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: 51.96  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  15 IPFDDTYILYDSHDFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFQ 94
Cdd:COG0671   30 LLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  95 NDTIRSGYGMPSAHSQfMGFCFtynslkiYTSWknLNFLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALT 174
Cdd:COG0671  110 LLGTAGGYSFPSGHAA-AAFAL-------ALVL--ALLLPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAI 179


                 ....*...
gi 398365285 175 GSLYFFIV 182
Cdd:COG0671  180 ALLLLALL 187
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 28-181 6.16e-07

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: 48.03  E-value: 6.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  28 DFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFG---QLMNEIFNNVIKNIIKQPRPvSFGASFQNDTIRS---- 100
Cdd:cd03395   24 DLMPFLTGKKLSVPIFLLLALFILFRKGPIGLLILLLVLlavGFADQLASGFLKPLVARLRP-CNALDGVRLVVLGdqgg 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285 101 GYGMPSAH-SQFMGFCFTYnslkiytswknLNFLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYF 179
Cdd:cd03395  103 SYSFASSHaANSFALALFI-----------WLFFRRGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFY 171


                 ..
gi 398365285 180 FI 181
Cdd:cd03395  172 LL 173
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 32-179 2.59e-06

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: 45.68  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  32 FLSAYFSLMPILV-LAFY------LSWFIITRELEACIVAFGQLMneIFNNVIKNIIKQPRPVS-----FGASfqndTIR 99
Cdd:cd03388    2 FLDYYFAFTALLGtHTFYilflpfLFWNGDPYVGRDLVVVLALGM--YIGQFIKDLFCLPRPSSppvvrLTMS----SAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285 100 SGYGMPSAHSqFMGFCFTYNSL-KIYTSWKNLNFLEKCIfsgaLALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLY 178
Cdd:cd03388   76 LEYGFPSTHA-MNATAISFYLLiYLYDRYQYPFVLGLIL----ALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFR 150


                 .
gi 398365285 179 F 179
Cdd:cd03388  151 F 151
PAP2_wunen cd03384
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ...
 64-173 3.54e-04

PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid phosphatases. Wunen is a drosophila protein expressed in the central nervous system, which provides repellent activity towards primordial germ cells (PGCs), controls the survival of PGCs and is essential in the migration process of these cells towards the somatic gonadal precursors.


Pssm-ID: 239479  Cd Length: 150  Bit Score: 39.54  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  64 AFGQLMNEIFNNVIKNIIKQPRP----------VSFGASFQNDTIRSGYGM--------------PSAHSQFMGFCFTYN 119
Cdd:cd03384   10 LFGLFATQLLTDLGKYVTGRLRPhfldvckpnyTDLTCSLDHQYIADCTCCtgdpdlirearlsfPSGHASLSMYAAVFL 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 398365285 120 SLKIYT--SWKNLNFLeKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGAL 173
Cdd:cd03384   90 ALYLQArlKLRGSRLL-RPLLQFLLLALALYVGLSRISDYKHHWSDVLAGALLGSV 144
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 97-218 1.18e-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: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  97 TIRSGYGMPSAHSqfMGF-CFTYNSLKIYTSWKNLNF---LEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGA 172
Cdd:cd03381   67 TCETGPGSPSGHA--MGTtAVLLVMVTALLSHLAGRKrsrFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGI 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398365285 173 LTGSLYFFIVGI----IRELGLINWFLKLRIVRLFYMTDSYNLAPL-TLKE 218
Cdd:cd03381  145 AVAETFSHIRYIysasLKRYVLITFFLFGFALGFYLLLKWLGVDLLwSLEK 195
PAP2_containing_1_like cd03390
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ...
 39-180 4.53e-03

PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.


Pssm-ID: 239484 [Multi-domain]  Cd Length: 193  Bit Score: 36.81  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  39 LMPILVLaFYLSWFIITR--ELEACIVAFGQ--LMNEIFNNVIKNIIKQPRP----------------VSFGASFQND-- 96
Cdd:cd03390   24 GIPLLVI-ILISLFFRRSlwDLHTSLLGLLLsvSLNGVITNVLKNYAGRPRPdflarcfpdggtpsdtLVGIDICCTGdp 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  97 -TIRSGY-GMPSAHSQFMGFCFTYNSLKIY---TSWKNLNFLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVG 171
Cdd:cd03390  103 gVLKEGRkSFPSGHSSFAFAGLGFLSLYLAgklHIFDPRGSSWRLLLALLPLLLAILVAVSRTRDYRHHFSDVIAGSLIG 182


                 ....*....
gi 398365285 172 ALTGSLYFF 180
Cdd:cd03390  183 LIIAYLSYR 191
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 72-178 4.92e-03

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: 36.20  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365285  72 IFNNVIKNIIKQPRPVSF-GASFQNDTIRSGYGMPSAHSQFMGfcftynslkiyTSWKNLNFL-EKCIFSGALALLSFCV 149
Cdd:cd03393   27 YLNAALKEVFKIPRPFTYdGIQAIYEESAGGYGFPSGHAQTSA-----------TFWGSLMLHvRKKWFTLIGVVLVVLI 95

                         90       100
                 ....*....|....*....|....*....
gi 398365285 150 CFSRVYLHYHNLDQVIVGFSVGALTGSLY 178
Cdd:cd03393   96 SFSRLYLGVHWPSDVIGGVLIGLLVLVLG 124
 
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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