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Conserved domains on  [gi|15242619|ref|NP_195928|]
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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

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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 ...
 11-171 2.18e-59

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: 184.01  E-value: 2.18e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  11 VTLTHVRYRPGDQLGHFLAWISLVPVFIsLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARPETCTLLeAC 90
Cdd:cd03382   1 FSLTHVLYDPGDLLSFLLAYLSLLPVAI-LVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSGAYF-VR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  91 DSHGWPSSHSQFMFFFATYFSLMGCKGIGFWFGLRSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASW 170
Cdd:cd03382  79 SGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILW 158


                .
gi 15242619 171 F 171
Cdd:cd03382 159 F 159
 
Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 11-171 2.18e-59

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: 184.01  E-value: 2.18e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  11 VTLTHVRYRPGDQLGHFLAWISLVPVFIsLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARPETCTLLeAC 90
Cdd:cd03382   1 FSLTHVLYDPGDLLSFLLAYLSLLPVAI-LVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSGAYF-VR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  91 DSHGWPSSHSQFMFFFATYFSLMGCKGIGFWFGLRSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASW 170
Cdd:cd03382  79 SGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILW 158


                .
gi 15242619 171 F 171
Cdd:cd03382 159 F 159
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 58-175 5.64e-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: 63.59  E-value: 5.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619    58 FGIGLVISQFINEFIKTSVEQARP---------ETCTLLEACDSHGWPSSHSQFMFFFATYFSLMgckgIGFWFGLRSRW 128
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPfflllegglVPAPSTLPGLGYSFPSGHSATAFALALLLALL----LRRLRKIVRVL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15242619   129 IMNLLhWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFWVVN 175
Cdd:pfam01569  78 LALLL-LVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
60-171 4.02e-10

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 55.43  E-value: 4.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619     60 IGLVISQFINEFIKTSVEQARPETCTLLEACDSH----------GWPSSHSQFMFFFATYFSlmgckgigFWFGLRSRWI 129
Cdd:smart00014   2 LLAVVSQLFNGVIKNYFGRPRPFFLSIGDACCTPnflltleagySFPSGHTAFAFAFALFLL--------LYLPARAGRK 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 15242619    130 MN-LLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWF 171
Cdd:smart00014  74 LLiFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 24-175 1.75e-09

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: 55.43  E-value: 1.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  24 LGHFLAWISLVPVFISLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARP----ETCTLLEACDSHGWPSSH 99
Cdd:COG0671  44 LLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPfvvpDLELLLGTAGGYSFPSGH 123

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242619 100 SQFMFFFATYFSLMgckgigfwfgLRSRWIMNLLhWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFWVVN 175
Cdd:COG0671 124 AAAAFALALVLALL----------LPRRWLAALL-LALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLR 188
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
92-163 1.34e-03

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 38.33  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242619   92 SHGWPSSHSQFMfffatyfslmgckGIGFWFGLRsRWIMNLLHWSLAVV--TMYSRVYLGYHTVAQVFAGAALG 163
Cdd:PRK09597 118 NFNMPSGHSSMV-------------GLAVAFLMR-RYSFKKYWWLLPLIplTMLARIYLDMHTIGAVLAGLGVG 177
 
Name Accession Description Interval E-value
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 11-171 2.18e-59

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: 184.01  E-value: 2.18e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  11 VTLTHVRYRPGDQLGHFLAWISLVPVFIsLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARPETCTLLeAC 90
Cdd:cd03382   1 FSLTHVLYDPGDLLSFLLAYLSLLPVAI-LVGYATLILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRPCSGAYF-VR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  91 DSHGWPSSHSQFMFFFATYFSLMGCKGIGFWFGLRSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASW 170
Cdd:cd03382  79 SGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILW 158


                .
gi 15242619 171 F 171
Cdd:cd03382 159 F 159
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 51-171 5.03e-14

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: 66.33  E-value: 5.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  51 RELQGIFFGIGLVISQFINEFIKTSVEQARPETCTLLEAC--------DSHGWPSSHSQFMFFFATYFSLmgckgigFWF 122
Cdd:cd01610   1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDgdplllteGGYSFPSGHAAFAFALALFLAL-------LLP 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15242619 123 GLRSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWF 171
Cdd:cd01610  74 RRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 58-175 5.64e-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: 63.59  E-value: 5.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619    58 FGIGLVISQFINEFIKTSVEQARP---------ETCTLLEACDSHGWPSSHSQFMFFFATYFSLMgckgIGFWFGLRSRW 128
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPfflllegglVPAPSTLPGLGYSFPSGHSATAFALALLLALL----LRRLRKIVRVL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15242619   129 IMNLLhWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFWVVN 175
Cdd:pfam01569  78 LALLL-LVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVP 123
acidPPc smart00014
Acid phosphatase homologues;
60-171 4.02e-10

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 55.43  E-value: 4.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619     60 IGLVISQFINEFIKTSVEQARPETCTLLEACDSH----------GWPSSHSQFMFFFATYFSlmgckgigFWFGLRSRWI 129
Cdd:smart00014   2 LLAVVSQLFNGVIKNYFGRPRPFFLSIGDACCTPnflltleagySFPSGHTAFAFAFALFLL--------LYLPARAGRK 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 15242619    130 MN-LLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWF 171
Cdd:smart00014  74 LLiFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 24-175 1.75e-09

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: 55.43  E-value: 1.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  24 LGHFLAWISLVPVFISLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARP----ETCTLLEACDSHGWPSSH 99
Cdd:COG0671  44 LLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPfvvpDLELLLGTAGGYSFPSGH 123

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242619 100 SQFMFFFATYFSLMgckgigfwfgLRSRWIMNLLhWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFWVVN 175
Cdd:COG0671 124 AAAAFALALVLALL----------LPRRWLAALL-LALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLR 188
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 22-174 1.89e-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: 54.92  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  22 DQLGHFLAWISLVPV--FISLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARPetcTLLEACDSHGW--PS 97
Cdd:cd03392  29 TAFMTAITFLGSPAVllIIVLLLALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRP---PLHLLVPEGGYsfPS 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  98 SHSqfMFFFATYFSLMgckgIGFWFGLRSRWIMNLLHWSLAVVT---MYSRVYLGYHTVAQVFAGAALGGIVGASWFWVV 174
Cdd:cd03392 106 GHA--MGATVLYGFLA----YLLARRLPRRRVRILLLILAAILIllvGLSRLYLGVHYPSDVLAGWLLGLAWLALLILLY 179
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 22-173 5.45e-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: 50.73  E-value: 5.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  22 DQLGHFLAWISLVPVFISLGGFVshFLFRRELQG--IFFGIGLVIS---QFINEFIKTSVEQARPetCTLLEACD----- 91
Cdd:cd03395  23 DDLMPFLTGKKLSVPIFLLLALF--ILFRKGPIGllILLLVLLAVGfadQLASGFLKPLVARLRP--CNALDGVRlvvlg 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  92 ----SHGWPSSHSQFMFFFATYFSLMgckgigFWFGLRSRWImnllhWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVG 167
Cdd:cd03395  99 dqggSYSFASSHAANSFALALFIWLF------FRRGLFSPVL-----LLWALLVGYSRVYVGVHYPGDVIAGALIGIISG 167


                ....*.
gi 15242619 168 ASWFWV 173
Cdd:cd03395 168 LLFYLL 173
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 61-172 3.22e-07

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: 47.33  E-value: 3.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  61 GLVISQFINEFIKTSVEQARPETctllEACDSHGWPSSHSQFMFFFATYfslmgckgIGFWFGLRSRWIMNLLhwsLAVV 140
Cdd:cd03394  11 AAALTAAVTEGLKFAVGRARPDG----SNNGYRSFPSGHTASAFAAATF--------LQYRYGWRWYGIPAYA---LASL 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 15242619 141 TMYSRVYLGYHTVAQVFAGAALGGIVGAsWFW 172
Cdd:cd03394  76 VGASRVVANRHWLSDVLAGAAIGILVGY-LVT 106
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 62-171 3.60e-05

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: 42.60  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  62 LVISQFINEFIKTSVEQARP--ETCTLLEACDSH---GWPSSHSQ----FMFFFatYFSLMGCKGIGFWFGLrsrwiMNL 132
Cdd:cd03388  42 LALGMYIGQFIKDLFCLPRPssPPVVRLTMSSAAleyGFPSTHAMnataISFYL--LIYLYDRYQYPFVLGL-----ILA 114

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15242619 133 LHWSLAVVtmYSRVYLGYHTVAQVFAGAALGGIVGASWF 171
Cdd:cd03388 115 LFYSTLVC--LSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
PAP2_diacylglycerolkinase cd03383
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ...
 94-171 1.55e-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: 1.55e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242619  94 GWPSSHSQFMFFFATYFSLMGckgigfwfglrSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWF 171
Cdd:cd03383  40 GMPSGHAAIAFSIATAISLIT-----------NNPIISILSVLLAVMVAHSRVEMKIHTMWEVVVGAILGALITLLIF 106
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
92-163 1.34e-03

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 38.33  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242619   92 SHGWPSSHSQFMfffatyfslmgckGIGFWFGLRsRWIMNLLHWSLAVV--TMYSRVYLGYHTVAQVFAGAALG 163
Cdd:PRK09597 118 NFNMPSGHSSMV-------------GLAVAFLMR-RYSFKKYWWLLPLIplTMLARIYLDMHTIGAVLAGLGVG 177
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
 36-172 1.47e-03

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: 37.62  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242619  36 VFISLGGFVSHFLFRRELQ---GIFFGIGLVISQFINEFIKTSVEQARP----ETCTLLEACDSHGWPSSHSQFMFFFAt 108
Cdd:cd03385  13 IYILPLLLVVLWLWGGEKQrkvVLFATIAVAVALLINYIIGLLYFHPRPfvvgLGHNLLPHAADSSFPSDHTTLFFSIA- 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242619 109 yFSLMgckgigFWFGLRSRWIMnllhWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFW 172
Cdd:cd03385  92 -FSLL------LRRRKWAGWIL----LILALLVAWSRIYLGVHYPLDMLGAALVAVLSALLVFQ 144
 
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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