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Conserved domains on  [gi|16129239|ref|NP_415794|]
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phosphatidylglycerophosphatase B [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

phosphatidylglycerophosphatase B( domain architecture ID 10013608)

phosphatidylglycerophosphatase B catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG); also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate; can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10699 PRK10699
phosphatidylglycerophosphatase B; Provisional
1-244 5.57e-153

phosphatidylglycerophosphatase B; Provisional


:

Pssm-ID: 182658  Cd Length: 244  Bit Score: 425.60  E-value: 5.57e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239    1 MRSIARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFA 80
Cdd:PRK10699   1 MYSIAKRTAVGAALLLVMPLAVWISGWQWQPGEQSWWLKGLFWVTETVTQPWGILTHVLLCGWFLWCLRFRLKAALVLFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239   81 ILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAERGNLVKEQLAEEKNIPQYLRSHWQKETGFAFP 160
Cdd:PRK10699  81 ILAAAILVGQGVKSWIKERVQEPRPFVVWLEKTHHIPVDEFYTLKRAERGELVKEQLAEQSNIPQWLRSHWQKETGFAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  161 SGHTMFAASWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRICGPLTPP 240
Cdd:PRK10699 161 SGHTMFAASWALLAVGLLWPRRRYKTVALLMLWATGVMGSRLLLGMHWPRDLVVATLISWLLVTVATWLAQRICGPLTPP 240

                 ....
gi 16129239  241 AEEN 244
Cdd:PRK10699 241 PEEN 244
 
Name Accession Description Interval E-value
PRK10699 PRK10699
phosphatidylglycerophosphatase B; Provisional
1-244 5.57e-153

phosphatidylglycerophosphatase B; Provisional


Pssm-ID: 182658  Cd Length: 244  Bit Score: 425.60  E-value: 5.57e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239    1 MRSIARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFA 80
Cdd:PRK10699   1 MYSIAKRTAVGAALLLVMPLAVWISGWQWQPGEQSWWLKGLFWVTETVTQPWGILTHVLLCGWFLWCLRFRLKAALVLFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239   81 ILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAERGNLVKEQLAEEKNIPQYLRSHWQKETGFAFP 160
Cdd:PRK10699  81 ILAAAILVGQGVKSWIKERVQEPRPFVVWLEKTHHIPVDEFYTLKRAERGELVKEQLAEQSNIPQWLRSHWQKETGFAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  161 SGHTMFAASWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRICGPLTPP 240
Cdd:PRK10699 161 SGHTMFAASWALLAVGLLWPRRRYKTVALLMLWATGVMGSRLLLGMHWPRDLVVATLISWLLVTVATWLAQRICGPLTPP 240

                 ....
gi 16129239  241 AEEN 244
Cdd:PRK10699 241 PEEN 244
acidPPc smart00014
Acid phosphatase homologues;
83-226 1.33e-22

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 89.33  E-value: 1.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239     83 AAAILVGQGVKSWIKDKVQEPRPFVIWlekthhipvdefytlkraergnlvkeqlaeEKNIPQYLRSHWQKETGFAFPSG 162
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLS------------------------------IGDACCTPNFLLTLEAGYSFPSG 50
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129239    163 HTMFAASWALLAVGLLWPR-RRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVA 226
Cdd:smart00014  51 HTAFAFAFALFLLLYLPARaGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
81-232 6.52e-21

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: 85.16  E-value: 6.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239    81 ILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAergnlvkeqlaeeknipqylrshwqketgfaFP 160
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGLGYS-------------------------------FP 49
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129239   161 SGHTMFAASWALLAVGLLWPRR---RTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQR 232
Cdd:pfam01569  50 SGHSATAFALALLLALLLRRLRkivRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVPK 124
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
5-232 1.05e-16

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: 75.85  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239   5 ARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFAILAA 84
Cdd:COG0671   1 LLLALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  85 AILVGQGVKSWIKDKVQEPRPFVIwlekthhipvdefytlkraergnlvkeqlaeeknipQYLRSHWQKETGFAFPSGHT 164
Cdd:COG0671  81 LLLLLLLLLLLLKYLFGRPRPFVV------------------------------------PDLELLLGTAGGYSFPSGHA 124
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129239 165 MFAASWALlAVGLLWPRRrtLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQR 232
Cdd:COG0671 125 AAAFALAL-VLALLLPRR--WLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLRR 189
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
75-226 5.52e-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: 69.41  E-value: 5.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  75 AFVLFAILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPvdefytlkraergnlvkeqlaeeknipqylrsHWQKE 154
Cdd:cd01610   1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDP--------------------------------LLLTE 48
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129239 155 TGFAFPSGHTMFAASWALLAVGLLWPRR-RTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVA 226
Cdd:cd01610  49 GGYSFPSGHAAFAFALALFLALLLPRRLlRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLV 121
 
Name Accession Description Interval E-value
PRK10699 PRK10699
phosphatidylglycerophosphatase B; Provisional
1-244 5.57e-153

phosphatidylglycerophosphatase B; Provisional


Pssm-ID: 182658  Cd Length: 244  Bit Score: 425.60  E-value: 5.57e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239    1 MRSIARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFA 80
Cdd:PRK10699   1 MYSIAKRTAVGAALLLVMPLAVWISGWQWQPGEQSWWLKGLFWVTETVTQPWGILTHVLLCGWFLWCLRFRLKAALVLFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239   81 ILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAERGNLVKEQLAEEKNIPQYLRSHWQKETGFAFP 160
Cdd:PRK10699  81 ILAAAILVGQGVKSWIKERVQEPRPFVVWLEKTHHIPVDEFYTLKRAERGELVKEQLAEQSNIPQWLRSHWQKETGFAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  161 SGHTMFAASWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRICGPLTPP 240
Cdd:PRK10699 161 SGHTMFAASWALLAVGLLWPRRRYKTVALLMLWATGVMGSRLLLGMHWPRDLVVATLISWLLVTVATWLAQRICGPLTPP 240

                 ....
gi 16129239  241 AEEN 244
Cdd:PRK10699 241 PEEN 244
acidPPc smart00014
Acid phosphatase homologues;
83-226 1.33e-22

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 89.33  E-value: 1.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239     83 AAAILVGQGVKSWIKDKVQEPRPFVIWlekthhipvdefytlkraergnlvkeqlaeEKNIPQYLRSHWQKETGFAFPSG 162
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLS------------------------------IGDACCTPNFLLTLEAGYSFPSG 50
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129239    163 HTMFAASWALLAVGLLWPR-RRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVA 226
Cdd:smart00014  51 HTAFAFAFALFLLLYLPARaGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
81-232 6.52e-21

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: 85.16  E-value: 6.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239    81 ILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAergnlvkeqlaeeknipqylrshwqketgfaFP 160
Cdd:pfam01569   1 ILLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGLGYS-------------------------------FP 49
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129239   161 SGHTMFAASWALLAVGLLWPRR---RTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQR 232
Cdd:pfam01569  50 SGHSATAFALALLLALLLRRLRkivRVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVPK 124
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
5-232 1.05e-16

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: 75.85  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239   5 ARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFAILAA 84
Cdd:COG0671   1 LLLALLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  85 AILVGQGVKSWIKDKVQEPRPFVIwlekthhipvdefytlkraergnlvkeqlaeeknipQYLRSHWQKETGFAFPSGHT 164
Cdd:COG0671  81 LLLLLLLLLLLLKYLFGRPRPFVV------------------------------------PDLELLLGTAGGYSFPSGHA 124
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129239 165 MFAASWALlAVGLLWPRRrtLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQR 232
Cdd:COG0671 125 AAAFALAL-VLALLLPRR--WLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLRR 189
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
75-226 5.52e-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: 69.41  E-value: 5.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  75 AFVLFAILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPvdefytlkraergnlvkeqlaeeknipqylrsHWQKE 154
Cdd:cd01610   1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDP--------------------------------LLLTE 48
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129239 155 TGFAFPSGHTMFAASWALLAVGLLWPRR-RTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVA 226
Cdd:cd01610  49 GGYSFPSGHAAFAFALALFLALLLPRRLlRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLV 121
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
19-233 1.29e-11

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: 61.47  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  19 PVAVWISGWRwqpgeQSWLLKAAFWVTeTVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFAILAAAILVgqgvkSWIKD 98
Cdd:cd03392  15 SVLSLLRSLR-----TPLLTAFMTAIT-FLGSPAVLLIIVLLLALLLLLKRRRRAALFLLLALLGGGALN-----TLLKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  99 KVQEPRPfviwlekTHHIPVDEfytlkraergnlvkeqlaeeknipqylrshwqkeTGFAFPSGHTMFAASWALLAVGLL 178
Cdd:cd03392  84 LVQRPRP-------PLHLLVPE----------------------------------GGYSFPSGHAMGATVLYGFLAYLL 122
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239 179 WPRR-----RTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRI 233
Cdd:cd03392 123 ARRLprrrvRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLLGLAWLALLILLYRRL 182
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
157-225 8.88e-09

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: 53.00  E-value: 8.88e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129239 157 FAFPSGHTMFAASWALLAVGLLWPRRRTLTI---AILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAV 225
Cdd:cd03388  78 YGFPSTHAMNATAISFYLLIYLYDRYQYPFVlglILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLF 149
PAP2_like_6 cd03396
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
23-229 2.98e-08

PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which mainly contains bacterial proteins, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239490  Cd Length: 197  Bit Score: 52.30  E-value: 2.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  23 WISGWRWQPGEQSWLLKAAF-WVTETVTQPWG-----VITHLILFGWFLWCLRFRIKAAFVLFAILAAAILVGQGVKSWI 96
Cdd:cd03396   7 WVAGLFYDAGGGVFPFPLRHsWILETLLHLGGrllsiALAVLLLALALLFFRRKRLRRRRRALLLLILVIGLGLLVVAIL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  97 KDKVQEPRPFVIWLEKTHHIPVdefytlkraergnlvkeqlaeekniPQYLRSHWQKETGFAFPSGHTMFAASWALLAVG 176
Cdd:cd03396  87 KSHWGRPRPWDLTEFGGDAPYT-------------------------PLFSGPSNGCGKGCSFPSGHASAGFALLALYFL 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129239 177 LLWPRRRTLTIAILLVWATG-VMG-SRLLLGMHWPRDLVVATLISWALVAVATWL 229
Cdd:cd03396 142 FRRRRPRLARLVLAAGLALGaLMGlARMARGAHFLSDVLWSLLLVWLIALLLYRL 196
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
97-226 3.43e-08

PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.


Pssm-ID: 239491  Cd Length: 232  Bit Score: 52.72  E-value: 3.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  97 KDKVQEPRPFViWLEKTHHIPVDEFYTlkraergnlvkeqlaeeknipqylrshwqkETGFAFPSGHTMFAASWALLAVG 176
Cdd:cd03397 121 KKYYNRPRPFV-LNDEPICTPPDESGL------------------------------AKDGSYPSGHTAAGYAWALILAE 169
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129239 177 LLwPRRRTltiAILlvwATG-VMG-SRLLLGMHWPRDLVVATLISWALVAVA 226
Cdd:cd03397 170 LV-PERAD---EIL---ARGsEYGqSRIVCGVHWPSDVMGGRIMAAALVAAL 214
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
41-233 4.41e-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: 45.72  E-value: 4.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239  41 AFWVTETVTQPWGVITHLILFgwFLWCLRFRIKAAFVLFAILAAAILVGQGVkSWIKDKVQEPRPfviwlekTHHIPVDE 120
Cdd:cd03395  24 DLMPFLTGKKLSVPIFLLLAL--FILFRKGPIGLLILLLVLLAVGFADQLAS-GFLKPLVARLRP-------CNALDGVR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129239 121 FYTLKRAERGnlvkeqlaeeknipqylrshwqketgFAFPSGHTmfAASWAL-LAVGLLWPRRrtLTIAILLVWATGVMG 199
Cdd:cd03395  94 LVVLGDQGGS--------------------------YSFASSHA--ANSFALaLFIWLFFRRG--LFSPVLLLWALLVGY 143
                       170       180       190
                ....*....|....*....|....*....|....
gi 16129239 200 SRLLLGMHWPRDLVVATLISWALVAVATWLAQRI 233
Cdd:cd03395 144 SRVYVGVHYPGDVIAGALIGIISGLLFYLLFSWL 177
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
152-223 5.64e-06

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: 44.67  E-value: 5.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129239 152 QKETGFAFPSGHTMFAAS-WALLAVGLlwpRRRTLT-IAILLVwaTGVMGSRLLLGMHWPRDLVVATLISWALV 223
Cdd:cd03393  53 ESAGGYGFPSGHAQTSATfWGSLMLHV---RKKWFTlIGVVLV--VLISFSRLYLGVHWPSDVIGGVLIGLLVL 121
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
159-232 2.79e-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: 43.02  E-value: 2.79e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129239 159 FPSGHT--MFAASWALLavglLWPRRRTltIAILLVWATGVMGSRLLLGMHWPRDLVVATLISwalvAVATWLAQR 232
Cdd:cd03385  79 FPSDHTtlFFSIAFSLL----LRRRKWA--GWILLILALLVAWSRIYLGVHYPLDMLGAALVA----VLSALLVFQ 144
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
159-229 3.94e-05

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: 43.08  E-value: 3.94e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129239 159 FPSGHTmfAASWALLAV-GLLWPRRRTLTIAILLVwatgVMGSRLLLGMHWPRDLVVATLIS-WALVAVATWL 229
Cdd:cd03389 120 FPSGHS--ATAGAAAAAlALLFPRYRWAFILLALL----IAFSRVIVGAHYPSDVIAGSLLGaVTALALYQRF 186
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
158-226 7.57e-05

PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases.


Pssm-ID: 239475  Cd Length: 209  Bit Score: 42.42  E-value: 7.57e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129239 158 AFPSGHTMFAASWALL---AVGLLWPR--RRTLTIAIllvwatgvmgSRLLLGMHWPRDLVVATLISWALVAVA 226
Cdd:cd03380 144 SYPSGHATFGGAAALVlaeLFPERAAEllARAAEAGN----------SRVVAGVHWPSDVEAGRILGEAIAAAL 207
PAP2_Aur1_like cd03386
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
158-228 1.83e-04

PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.


Pssm-ID: 239481  Cd Length: 186  Bit Score: 41.14  E-value: 1.83e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129239 158 AFPSGHTmfaaSWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATW 228
Cdd:cd03386 118 AFPSLHV----AWAVLAALFLWRHRRRLLRWLAVLWPLLIWLSTLYLGNHYFIDLVGGIALALLSFYLARR 184
 
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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