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Conserved domains on  [gi|1033101485|ref|WP_064410560|]
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MULTISPECIES: phosphatase PAP2 family protein [Klebsiella]

Protein Classification

acid phosphatase( domain architecture ID 10130290)

acid phosphatase belonging to the phosphatase PAP2 family catalyzes phosphomonoester hydrolysis to yield alcohol and phosphate

CATH:  1.20.144.10
EC:  3.1.3.2
Gene Ontology:  GO:0003993|GO:0016311
PubMed:  12447906|9260289
SCOP:  4001226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
 74-309 1.67e-60

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: 196.40  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485  74 ARQNKTQADTAWLKASGYDFQTKANQQAgIELLSAFTALPQAVIEQNLATVTAINRDAVQTSRHQALADAEGIsyLYFLS 153
Cdd:cd03397    11 SQQPAPSATIRALPASGYLPPVGATPDS-LDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADLS--FPGAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 154 DALGPRLGKAflaayDKGELGKAAALIKASEVS-TGAAKKHFNNPRPFLIQGNTIHLVPDDvvvkdnkPYTADGGSFPSG 232
Cdd:cd03397    88 NAFSCALGEE-----RTPELYRLLRRVLEDAGSaTYPAKKYYNRPRPFVLNDEPICTPPDE-------SGLAKDGSYPSG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033101485 233 HTNTGYTDALLMAEMIPERFDALVTRGARYGYSRIVLGVHYPLDVMGSRMVAQRNVAHYLNDAKYRGLFNEARDQLR 309
Cdd:cd03397   156 HTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
 
Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
 74-309 1.67e-60

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: 196.40  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485  74 ARQNKTQADTAWLKASGYDFQTKANQQAgIELLSAFTALPQAVIEQNLATVTAINRDAVQTSRHQALADAEGIsyLYFLS 153
Cdd:cd03397    11 SQQPAPSATIRALPASGYLPPVGATPDS-LDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADLS--FPGAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 154 DALGPRLGKAflaayDKGELGKAAALIKASEVS-TGAAKKHFNNPRPFLIQGNTIHLVPDDvvvkdnkPYTADGGSFPSG 232
Cdd:cd03397    88 NAFSCALGEE-----RTPELYRLLRRVLEDAGSaTYPAKKYYNRPRPFVLNDEPICTPPDE-------SGLAKDGSYPSG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033101485 233 HTNTGYTDALLMAEMIPERFDALVTRGARYGYSRIVLGVHYPLDVMGSRMVAQRNVAHYLNDAKYRGLFNEARDQLR 309
Cdd:cd03397   156 HTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 105-284 1.82e-22

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: 93.95  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 105 LLSAFTALPQAVIEQNLATVTAINRDAVQTSRHQALADAEGISYLYFLSDALGPRLGKAFLAAYDKGELGKAAALIKASE 184
Cdd:COG0671     6 LLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 185 VSTGAAKKH-FNNPRPFLIQGNTIHLVPddvvvkdnkpytADGGSFPSGHTNTGYTDALLMAEMIPER--FDALVTRGAR 261
Cdd:COG0671    86 LLLLLLLKYlFGRPRPFVVPDLELLLGT------------AGGYSFPSGHAAAAFALALVLALLLPRRwlAALLLALALL 153

                         170       180
                  ....*....|....*....|...
gi 1033101485 262 YGYSRIVLGVHYPLDVMGSRMVA 284
Cdd:COG0671   154 VGLSRVYLGVHYPSDVLAGALLG 176
acidPPc smart00014
Acid phosphatase homologues;
177-284 2.41e-15

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 71.99  E-value: 2.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485  177 AALIKASEVSTGAAKKHFNNPRPF-LIQGNTIHLVPDDVVvkdnkpyTADGGSFPSGHTNTGYTDALLMAEMIPERFDAL 255
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFfLSIGDACCTPNFLLT-------LEAGYSFPSGHTAFAFAFALFLLLYLPARAGRK 73

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1033101485  256 VT------RGARYGYSRIVLGVHYPLDVMGSRMVA 284
Cdd:smart00014  74 LLifllllLALVVGFSRVYLGAHWPSDVLAGSLLG 108
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 182-284 7.77e-14

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 67.83  E-value: 7.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 182 ASEVSTGAAKKHFNNPRPFliqgntiHLVPDDVVVKDNKPYTADGGSFPSGHTNTGYTDALLMAEMIPERFDALVTRGAR 261
Cdd:pfam01569   8 LAGLLSSVLKDYFGRPRPF-------FLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1033101485 262 Y--------GYSRIVLGVHYPLDVMGSRMVA 284
Cdd:pfam01569  81 LllvlallvGLSRLYLGVHFPSDVLAGALIG 111
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 194-284 5.13e-04

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 41.15  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 194 FNNPRPFL--IQGNTIHLVPDDvvvkdnkpytadggSFPSGHTNTGYTDALLMAEMIPERFDA-LVTRGARYGYSRIVLG 270
Cdd:PRK11837   82 FPHDRPFVegIGYNFLHHAADD--------------SFPSDHGTVIFTFALAFLFWHRLWSGSlLMAIAVAIAWSRVYLG 147

                          90
                  ....*....|....
gi 1033101485 271 VHYPLDVMGSRMVA 284
Cdd:PRK11837  148 VHWPLDMLGALLVG 161
 
Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
 74-309 1.67e-60

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: 196.40  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485  74 ARQNKTQADTAWLKASGYDFQTKANQQAgIELLSAFTALPQAVIEQNLATVTAINRDAVQTSRHQALADAEGIsyLYFLS 153
Cdd:cd03397    11 SQQPAPSATIRALPASGYLPPVGATPDS-LDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADLS--FPGAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 154 DALGPRLGKAflaayDKGELGKAAALIKASEVS-TGAAKKHFNNPRPFLIQGNTIHLVPDDvvvkdnkPYTADGGSFPSG 232
Cdd:cd03397    88 NAFSCALGEE-----RTPELYRLLRRVLEDAGSaTYPAKKYYNRPRPFVLNDEPICTPPDE-------SGLAKDGSYPSG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033101485 233 HTNTGYTDALLMAEMIPERFDALVTRGARYGYSRIVLGVHYPLDVMGSRMVAQRNVAHYLNDAKYRGLFNEARDQLR 309
Cdd:cd03397   156 HTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
 111-293 2.98e-39

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: 139.88  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 111 ALPQAVIEQNLATVTAINRDAVQT----SRHQALADAEGISYLYFLSDALGPRLGKAFLAAYDKGELGKAAALIKASEV- 185
Cdd:cd03380    28 PALSAAYAADLAEVKALGALQSTArttaQTALAAFDADGGDPPPHYANAFSIALGTPGLSEERTPRLYALLARALTDAGi 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 186 STGAAKKHFNNPRPFLIQGNTIHLVPDdvvvkdNKPYTADGGSFPSGHTNTGYTDALLMAEMIPERFDALVTRGARYGYS 265
Cdd:cd03380   108 ATWDAKYHYNRPRPFVAIRLQWLPICT------PEEGTPKHPSYPSGHATFGGAAALVLAELFPERAAELLARAAEAGNS 181

                         170       180
                  ....*....|....*....|....*...
gi 1033101485 266 RIVLGVHYPLDVMGSRMVAQRNVAHYLN 293
Cdd:cd03380   182 RVVAGVHWPSDVEAGRILGEAIAAALLA 209
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 105-284 1.82e-22

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: 93.95  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 105 LLSAFTALPQAVIEQNLATVTAINRDAVQTSRHQALADAEGISYLYFLSDALGPRLGKAFLAAYDKGELGKAAALIKASE 184
Cdd:COG0671     6 LLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 185 VSTGAAKKH-FNNPRPFLIQGNTIHLVPddvvvkdnkpytADGGSFPSGHTNTGYTDALLMAEMIPER--FDALVTRGAR 261
Cdd:COG0671    86 LLLLLLLKYlFGRPRPFVVPDLELLLGT------------AGGYSFPSGHAAAAFALALVLALLLPRRwlAALLLALALL 153

                         170       180
                  ....*....|....*....|...
gi 1033101485 262 YGYSRIVLGVHYPLDVMGSRMVA 284
Cdd:COG0671   154 VGLSRVYLGVHYPSDVLAGALLG 176
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 182-284 1.78e-18

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: 80.97  E-value: 1.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 182 ASEVSTGAAKKHFNNPRPFLIQGNTIHLVPDDVvvkdnkpyTADGGSFPSGHTNTGYTDALLMAEMIPERFD------AL 255
Cdd:cd01610    14 AGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLLL--------TEGGYSFPSGHAAFAFALALFLALLLPRRLLrlllglLL 85

                          90       100
                  ....*....|....*....|....*....
gi 1033101485 256 VTRGARYGYSRIVLGVHYPLDVMGSRMVA 284
Cdd:cd01610    86 LLLALLVGLSRVYLGVHYPSDVLAGALLG 114
acidPPc smart00014
Acid phosphatase homologues;
177-284 2.41e-15

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 71.99  E-value: 2.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485  177 AALIKASEVSTGAAKKHFNNPRPF-LIQGNTIHLVPDDVVvkdnkpyTADGGSFPSGHTNTGYTDALLMAEMIPERFDAL 255
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFfLSIGDACCTPNFLLT-------LEAGYSFPSGHTAFAFAFALFLLLYLPARAGRK 73

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1033101485  256 VT------RGARYGYSRIVLGVHYPLDVMGSRMVA 284
Cdd:smart00014  74 LLifllllLALVVGFSRVYLGAHWPSDVLAGSLLG 108
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 182-284 7.77e-14

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 67.83  E-value: 7.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 182 ASEVSTGAAKKHFNNPRPFliqgntiHLVPDDVVVKDNKPYTADGGSFPSGHTNTGYTDALLMAEMIPERFDALVTRGAR 261
Cdd:pfam01569   8 LAGLLSSVLKDYFGRPRPF-------FLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1033101485 262 Y--------GYSRIVLGVHYPLDVMGSRMVA 284
Cdd:pfam01569  81 LllvlallvGLSRLYLGVHFPSDVLAGALIG 111
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
 175-284 1.92e-08

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: 53.03  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 175 KAAALIKASEV-STGAAKKHFNnPRPFLIQGNT--IHLVPDDvvvkdnkpytadggSFPSGHTNTGYTDALLMAeMIPER 251
Cdd:cd03385    37 FATIAVAVALLiNYIIGLLYFH-PRPFVVGLGHnlLPHAADS--------------SFPSDHTTLFFSIAFSLL-LRRRK 100

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1033101485 252 FD--ALVTRGARYGYSRIVLGVHYPLDVMGSRMVA 284
Cdd:cd03385   101 WAgwILLILALLVAWSRIYLGVHYPLDMLGAALVA 135
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 176-280 4.58e-08

PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239486  Cd Length: 182  Bit Score: 52.61  E-value: 4.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 176 AAALIkASEVSTGAAKKHFNNPRPfliqgnTIHLVPDDvvvkdnkpytaDGGSFPSGHTNTGYTDALLMAEMIPERFDAL 255
Cdd:cd03392    68 LLALL-GGGALNTLLKLLVQRPRP------PLHLLVPE-----------GGYSFPSGHAMGATVLYGFLAYLLARRLPRR 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1033101485 256 VTRGARY----------GYSRIVLGVHYPLDVMGS 280
Cdd:cd03392   130 RVRILLLilaailillvGLSRLYLGVHYPSDVLAG 164
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 182-283 1.18e-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: 48.41  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 182 ASEVSTGAAKKHFNNPRPfliqgnTIHLVPDDVVVKDNKPytaDGGSFPSGHTNTGYTDALLMAEMIPERF--DALVTRG 259
Cdd:cd03395    68 ADQLASGFLKPLVARLRP------CNALDGVRLVVLGDQG---GSYSFASSHAANSFALALFIWLFFRRGLfsPVLLLWA 138

                          90       100
                  ....*....|....*....|....
gi 1033101485 260 ARYGYSRIVLGVHYPLDVMGSRMV 283
Cdd:cd03395   139 LLVGYSRVYVGVHYPGDVIAGALI 162
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 146-280 6.41e-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: 45.06  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 146 ISYLYFLSDA-LGPRLGKAFLAAYdkgelgkaaalikaseVSTGAAKKHFNNPRPFliqgntihlvPDDVVVKDNKPyTA 224
Cdd:cd03393     3 LSLIYWLVDKrLGRYLGLALCASG----------------YLNAALKEVFKIPRPF----------TYDGIQAIYEE-SA 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 225 DGGSFPSGHTNTGYTDALLMAEMIPER----FDALVTRGAryGYSRIVLGVHYPLDVMGS 280
Cdd:cd03393    56 GGYGFPSGHAQTSATFWGSLMLHVRKKwftlIGVVLVVLI--SFSRLYLGVHWPSDVIGG 113
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 228-278 2.10e-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: 45.00  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1033101485 228 SFPSGHTNTGYTDALLMAEMIPERFDALVTRGARYGYSRIVLGVHYPLDVM 278
Cdd:cd03389   119 SFPSGHSATAGAAAAALALLFPRYRWAFILLALLIAFSRVIVGAHYPSDVI 169
PAP2_like_6 cd03396
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 136-273 3.31e-04

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: 41.52  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 136 RHQALADAEGISYLYFLSDALGPRLGKAFLAAYdkgelgkAAALIKASEVSTGAAKKHFNNPRPFLIQ---GNTIHLVPD 212
Cdd:cd03396    39 RLLSIALAVLLLALALLFFRRKRLRRRRRALLL-------LILVIGLGLLVVAILKSHWGRPRPWDLTefgGDAPYTPLF 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033101485 213 DVVVKDNKPytadGGSFPSGHTNTGYTdALLMAEMIPERFDALVTR--------GARYGYSRIVLGVHY 273
Cdd:cd03396   112 SGPSNGCGK----GCSFPSGHASAGFA-LLALYFLFRRRRPRLARLvlaaglalGALMGLARMARGAHF 175
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 221-277 3.88e-04

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: 39.62  E-value: 3.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033101485 221 PYTADGG--SFPSGHTNTGYTDALLMAEMIPERFDALVTRG--ARYGYSRIVLGVHYPLDV 277
Cdd:cd03394    31 PDGSNNGyrSFPSGHTASAFAAATFLQYRYGWRWYGIPAYAlaSLVGASRVVANRHWLSDV 91
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 194-284 5.13e-04

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 41.15  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 194 FNNPRPFL--IQGNTIHLVPDDvvvkdnkpytadggSFPSGHTNTGYTDALLMAEMIPERFDA-LVTRGARYGYSRIVLG 270
Cdd:PRK11837   82 FPHDRPFVegIGYNFLHHAADD--------------SFPSDHGTVIFTFALAFLFWHRLWSGSlLMAIAVAIAWSRVYLG 147

                          90
                  ....*....|....
gi 1033101485 271 VHYPLDVMGSRMVA 284
Cdd:PRK11837  148 VHWPLDMLGALLVG 161
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
 188-277 6.64e-03

PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to eukaryota, lacks functional characterization and may act as a membrane-associated phosphatidic acid phosphatase.


Pssm-ID: 239485 [Multi-domain]  Cd Length: 159  Bit Score: 37.30  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033101485 188 GAAKKHFNNPRPfliqgntIHLVPDDVVVkdnkpYTADGGSFPSGHTntgyTDALLMAEM--------IPERFdALVTRG 259
Cdd:cd03391    64 AILKALVRRRRP-------AYNSPDMLDY-----VAVDKYSFPSGHA----SRAAFVARFllnhlvlaVPLRV-LLVLWA 126

                          90
                  ....*....|....*...
gi 1033101485 260 ARYGYSRIVLGVHYPLDV 277
Cdd:cd03391   127 TVVGISRVLLGRHHVLDV 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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