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Conserved domains on  [gi|1241305447|gb|PAY72165|]
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undecaprenyl-diphosphatase [Shigella boydii]

Protein Classification

undecaprenyl-diphosphatase( domain architecture ID 10793621)

undecaprenyl-diphosphatase catalyzes the dephosphorylation of undecaprenyl diphosphate to undecaprenyl phosphate, includes Bacillus subtilis BcrC and Escherichia coli YbjG

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 1-198 2.22e-123

undecaprenyl pyrophosphate phosphatase; Provisional


:

Pssm-ID: 183335  Cd Length: 202  Bit Score: 346.61  E-value: 2.22e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLITVVPLLAAVLWLWG----LTAQRQLVIKIAIALAVSLFVSWTMGH 76
Cdd:PRK11837    1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGprdqLTAQRQLVIKIAIALAISLLVSWTIGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  77 LFPHDRPFVENIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLA 156
Cdd:PRK11837   81 LFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIAWSRVYLGVHWPLDMLGALLV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1241305447 157 GMIGCLSAQIIWQAMGHKLYQRLQSWYRFCFALPIRKGWVRD 198
Cdd:PRK11837  161 GMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD 202
 
Name Accession Description Interval E-value
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 1-198 2.22e-123

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 346.61  E-value: 2.22e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLITVVPLLAAVLWLWG----LTAQRQLVIKIAIALAVSLFVSWTMGH 76
Cdd:PRK11837    1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGprdqLTAQRQLVIKIAIALAISLLVSWTIGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  77 LFPHDRPFVENIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLA 156
Cdd:PRK11837   81 LFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIAWSRVYLGVHWPLDMLGALLV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1241305447 157 GMIGCLSAQIIWQAMGHKLYQRLQSWYRFCFALPIRKGWVRD 198
Cdd:PRK11837  161 GMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD 202
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
 23-166 1.57e-60

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: 185.54  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  23 MISLAIFIAKDLITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPHDRPFVENIGYNFLHHAADDSFP 102
Cdd:cd03385     1 LDALAIFIAEYLIYILPLLLVVLWLWGGEKQRKVVLFATIAVAVALLINYIIGLLYFHPRPFVVGLGHNLLPHAADSSFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1241305447 103 SDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCLSAQI 166
Cdd:cd03385    81 SDHTTLFFSIAFSLLLRRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSALLVFQ 144
acidPPc smart00014
Acid phosphatase homologues;
61-165 1.50e-20

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 82.39  E-value: 1.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   61 AIALAVSLFVSWTMGHLFPHDRPFVE------NIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWHRLWSGS-----LLM 129
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLsigdacCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRkllifLLL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1241305447  130 VLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCLSAQ 165
Cdd:smart00014  81 LLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 1-170 1.27e-19

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: 82.01  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPH 80
Cdd:COG0671    19 LLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  81 DRPFVENIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWH-RLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMI 159
Cdd:COG0671    99 PRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLpRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLA 178

                         170
                  ....*....|.
gi 1241305447 160 GCLSAQIIWQA 170
Cdd:COG0671   179 IALLLLALLRR 189
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 60-171 2.16e-09

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: 53.19  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  60 IAIALAVSLFVSWTMGHLFPHDRPFV-----ENIGYNFLHHAADDSFPSDHGTVIFTFALAF-------LCWHRLWSGSL 127
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFlllegGLVPAPSTLPGLGYSFPSGHSATAFALALLLalllrrlRKIVRVLLALL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1241305447 128 LMVLAVVIAWSRVYLGVHWPLDMLGGLLagmIGCLSAQIIWQAM 171
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFPSDVLAGAL---IGILLALLVYRLV 122
 
Name Accession Description Interval E-value
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 1-198 2.22e-123

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 346.61  E-value: 2.22e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLITVVPLLAAVLWLWG----LTAQRQLVIKIAIALAVSLFVSWTMGH 76
Cdd:PRK11837    1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGprdqLTAQRQLVIKIAIALAISLLVSWTIGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  77 LFPHDRPFVENIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLA 156
Cdd:PRK11837   81 LFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIAWSRVYLGVHWPLDMLGALLV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1241305447 157 GMIGCLSAQIIWQAMGHKLYQRLQSWYRFCFALPIRKGWVRD 198
Cdd:PRK11837  161 GMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD 202
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
 23-166 1.57e-60

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: 185.54  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  23 MISLAIFIAKDLITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPHDRPFVENIGYNFLHHAADDSFP 102
Cdd:cd03385     1 LDALAIFIAEYLIYILPLLLVVLWLWGGEKQRKVVLFATIAVAVALLINYIIGLLYFHPRPFVVGLGHNLLPHAADSSFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1241305447 103 SDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCLSAQI 166
Cdd:cd03385    81 SDHTTLFFSIAFSLLLRRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSALLVFQ 144
acidPPc smart00014
Acid phosphatase homologues;
61-165 1.50e-20

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 82.39  E-value: 1.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   61 AIALAVSLFVSWTMGHLFPHDRPFVE------NIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWHRLWSGS-----LLM 129
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLsigdacCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRkllifLLL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1241305447  130 VLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCLSAQ 165
Cdd:smart00014  81 LLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 1-170 1.27e-19

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: 82.01  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPH 80
Cdd:COG0671    19 LLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  81 DRPFVENIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWH-RLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMI 159
Cdd:COG0671    99 PRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLpRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLA 178

                         170
                  ....*....|.
gi 1241305447 160 GCLSAQIIWQA 170
Cdd:COG0671   179 IALLLLALLRR 189
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 21-169 2.38e-14

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: 68.02  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  21 PWMISLAIFIAK--DLITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPHDRPFVenigyNFLHHAAD 98
Cdd:cd03392    26 PLLTAFMTAITFlgSPAVLLIIVLLLALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRPPL-----HLLVPEGG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  99 DSFPSDH--GTVIFTFALAFLCWHRLWSGS-------LLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCLSAQIIWQ 169
Cdd:cd03392   101 YSFPSGHamGATVLYGFLAYLLARRLPRRRvrillliLAAILILLVGLSRLYLGVHYPSDVLAGWLLGLAWLALLILLYR 180
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 54-162 4.79e-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: 65.56  E-value: 4.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  54 RQLVIKIAIALAVSLFVSWTMGHLFPHDRPFVEN----IGYNFLHHAADDSFPSDHGTVIFTFALAFLCW-----HRLWS 124
Cdd:cd01610     2 RLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLrcgpDGDPLLLTEGGYSFPSGHAAFAFALALFLALLlprrlLRLLL 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1241305447 125 GSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCL 162
Cdd:cd01610    82 GLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVAL 119
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 1-169 3.02e-13

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: 64.59  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   1 MLENLNLSLFSLINATPDSaPWMISLAIFIAKDLITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSL---FVSWTMGHL 77
Cdd:cd03395     1 LLEQIDVWLFLLLNGTLVH-PLLDDLMPFLTGKKLSVPIFLLLALFILFRKGPIGLLILLLVLLAVGFadqLASGFLKPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  78 FPHDRPFVENIGYNFLHHAADD---SFPSDHGTVIFTFALAF-LCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGG 153
Cdd:cd03395    80 VARLRPCNALDGVRLVVLGDQGgsySFASSHAANSFALALFIwLFFRRGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAG 159

                         170
                  ....*....|....*.
gi 1241305447 154 llaGMIGCLSAQIIWQ 169
Cdd:cd03395   160 ---ALIGIISGLLFYL 172
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 60-171 2.16e-09

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: 53.19  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  60 IAIALAVSLFVSWTMGHLFPHDRPFV-----ENIGYNFLHHAADDSFPSDHGTVIFTFALAF-------LCWHRLWSGSL 127
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFlllegGLVPAPSTLPGLGYSFPSGHSATAFALALLLalllrrlRKIVRVLLALL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1241305447 128 LMVLAVVIAWSRVYLGVHWPLDMLGGLLagmIGCLSAQIIWQAM 171
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFPSDVLAGAL---IGILLALLVYRLV 122
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 63-160 1.17e-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: 48.10  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  63 ALAVSLFVSWTMGHLFPHDRPFVENIGYNflhhaaddSFPSDHGTVIFTFAlAFLCWH--RLWSGSLLMVLAVVIAWSRV 140
Cdd:cd03394    11 AAALTAAVTEGLKFAVGRARPDGSNNGYR--------SFPSGHTASAFAAA-TFLQYRygWRWYGIPAYALASLVGASRV 81

                          90       100
                  ....*....|....*....|.
gi 1241305447 141 YLGVHWPLDML-GGLLAGMIG 160
Cdd:cd03394    82 VANRHWLSDVLaGAAIGILVG 102
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 54-160 2.43e-07

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: 47.75  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  54 RQLVIKIAIALAVSLFVSWTMGHLFPHDRPFV-ENIGYNFLHHAADDSFPSDH--GTVIFTFALAFLCWHR-LWSGSLLM 129
Cdd:cd03393    12 KRLGRYLGLALCASGYLNAALKEVFKIPRPFTyDGIQAIYEESAGGYGFPSGHaqTSATFWGSLMLHVRKKwFTLIGVVL 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1241305447 130 VlaVVIAWSRVYLGVHWPLDMLGGLLAGMIG 160
Cdd:cd03393    92 V--VLISFSRLYLGVHWPSDVIGGVLIGLLV 120
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
 60-157 3.25e-07

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: 48.58  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  60 IAIALAVSLFVSWTMGHLFPHDRPFVENIGYNFLHH------AADDSFPSDHGTVIFTFA--LAFLcWHRLWSGslLMVL 131
Cdd:cd03380    98 LARALTDAGIATWDAKYHYNRPRPFVAIRLQWLPICtpeegtPKHPSYPSGHATFGGAAAlvLAEL-FPERAAE--LLAR 174

                          90       100
                  ....*....|....*....|....*.
gi 1241305447 132 AVVIAWSRVYLGVHWPLDMLGGLLAG 157
Cdd:cd03380   175 AAEAGNSRVVAGVHWPSDVEAGRILG 200
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 95-157 9.28e-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: 43.76  E-value: 9.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  95 HAADDSFPSDHGTVIFTFALAFLCW-HRLWSGSLLMVLAVVIAW------SRVYLGVHWPLDMLGGLLAG 157
Cdd:cd03388    74 AALEYGFPSTHAMNATAISFYLLIYlYDRYQYPFVLGLILALFYstlvclSRIYMGMHSVLDVIAGSLIG 143
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 9-171 6.61e-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: 41.92  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447   9 LFSLINATPDSAPWMI-SLAIFIAKDLITVVPLLAAVLWLWGLTAQRQLVIKIAIALavSLFVSWTMGHLFPHDRP--FV 85
Cdd:cd03389    24 FFRTITDFGKSGWYLIpSLLLFLLFRFGDLRGLSAPSRARFPKAAWAGLFLFATVAL--SGILVNLLKFIIGRARPklLF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  86 ENIGYNFLHHAADD---SFPSDHGTVIFTFALAF-LCWHRLWSgsLLMVLAVVIAWSRVYLGVHWPLDMLGGLLagmIGC 161
Cdd:cd03389   102 DDGLYGFDPFHADYaftSFPSGHSATAGAAAAALaLLFPRYRW--AFILLALLIAFSRVIVGAHYPSDVIAGSL---LGA 176

                         170
                  ....*....|
gi 1241305447 162 LSAQIIWQAM 171
Cdd:cd03389   177 VTALALYQRF 186
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
 35-157 2.12e-04

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: 39.99  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  35 ITVVPLLAAVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPHDRPfVENIGYNFLHHAADD-SFPSDHGTVIFtFA 113
Cdd:cd03391    27 IPWLAGTISCLWISSSPAGQEVLVNLLLGLLLDIITVAILKALVRRRRP-AYNSPDMLDYVAVDKySFPSGHASRAA-FV 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1241305447 114 LAFLCWHRLWSGSLLMVL---AVVIAWSRVYLGVHWPLDMLGGLLAG 157
Cdd:cd03391   105 ARFLLNHLVLAVPLRVLLvlwATVVGISRVLLGRHHVLDVLAGAFLG 151
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
 78-153 4.43e-04

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: 39.63  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  78 FPHDRPFVEN-----IGYNFLHHAADDSFPSDHGTVIFT--FALAFLCWHRlwsGSLLMVLAVVIAWSRVYLGVHWPLDM 150
Cdd:cd03397   124 YNRPRPFVLNdepicTPPDESGLAKDGSYPSGHTAAGYAwaLILAELVPER---ADEILARGSEYGQSRIVCGVHWPSDV 200


                  ...
gi 1241305447 151 LGG 153
Cdd:cd03397   201 MGG 203
PAP2_haloperoxidase cd03398
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ...
 131-157 1.14e-03

PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles.


Pssm-ID: 239492  Cd Length: 232  Bit Score: 38.56  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|....*..
gi 1241305447 131 LAVVIAWSRVYLGVHWPLDMLGGLLAG 157
Cdd:cd03398   197 LADEVAISRVYAGVHFRSDDAAGAALG 223
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 48-157 4.63e-03

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: 36.10  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241305447  48 WGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPHDRPfvenigYNFLHHAADD-SFPSDHGTVIFTFALAFLCW------- 119
Cdd:cd03382    35 LILFRRELEAIYLFIGLLANEALNYVLKRIIKEPRP------CSGAYFVRSGyGMPSSHSQFMGFFAVYLLLFiylrlgr 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1241305447 120 -----HRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAG 157
Cdd:cd03382   109 lnslvSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVG 151
PAP2_Aur1_like cd03386
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
 101-162 5.08e-03

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: 36.52  E-value: 5.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1241305447 101 FPSDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCL 162
Cdd:cd03386   119 FPSLHVAWAVLAALFLWRHRRRLLRWLAVLWPLLIWLSTLYLGNHYFIDLVGGIALALLSFY 180
 
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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