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Conserved domains on  [gi|495176583|ref|WP_007901377|]
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MULTISPECIES: undecaprenyl-diphosphate phosphatase [Cronobacter]

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
1-197 4.96e-118

undecaprenyl pyrophosphate phosphatase; Provisional


:

Pssm-ID: 183335  Cd Length: 202  Bit Score: 333.13  E-value: 4.96e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   1 MMEALNQFLFLQINATPASPGWLIALATFIARDLISIVPLLPVVLWLWRP-----TERRLVVKFALALLISLAVSWLAGH 75
Cdd:PRK11837   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGPrdqltAQRQLVIKIAIALAISLLVSWTIGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  76 LFPHPRPFVVGLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWHRVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLV 155
Cdd:PRK11837  81 LFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIAWSRVYLGVHWPLDMLGALLV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495176583 156 AMLACLSAQILWAPLGEPLYRTLRQLYRLCFALPIRKGWVRD 197
Cdd:PRK11837 161 GMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD 202
 
Name Accession Description Interval E-value
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
1-197 4.96e-118

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 333.13  E-value: 4.96e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   1 MMEALNQFLFLQINATPASPGWLIALATFIARDLISIVPLLPVVLWLWRP-----TERRLVVKFALALLISLAVSWLAGH 75
Cdd:PRK11837   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGPrdqltAQRQLVIKIAIALAISLLVSWTIGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  76 LFPHPRPFVVGLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWHRVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLV 155
Cdd:PRK11837  81 LFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIAWSRVYLGVHWPLDMLGALLV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495176583 156 AMLACLSAQILWAPLGEPLYRTLRQLYRLCFALPIRKGWVRD 197
Cdd:PRK11837 161 GMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD 202
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
23-165 2.42e-55

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: 172.06  E-value: 2.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  23 LIALATFIARDLISIVPLLPVVLWLWRPTERRLVVKFA-LALLISLAVSWLAGHLFPHPRPFVVGLGHQFLPHAPDDSYP 101
Cdd:cd03385    1 LDALAIFIAEYLIYILPLLLVVLWLWGGEKQRKVVLFAtIAVAVALLINYIIGLLYFHPRPFVVGLGHNLLPHAADSSFP 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495176583 102 SDHGTVIFTFALAFLFWHRVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLVAMLACLSAQI 165
Cdd:cd03385   81 SDHTTLFFSIAFSLLLRRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSALLVFQ 144
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
1-167 1.73e-18

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: 78.93  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   1 MMEALNQFLFLQINATPASPGWLIALATFIARDLISIVPLLPVVLWLWRPTERRLVVKFALALLISLAVSWLAG--HLFP 78
Cdd:COG0671   18 DLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLlkYLFG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  79 HPRPFVVGLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWH-RVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLVAM 157
Cdd:COG0671   98 RPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLpRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGL 177
                        170
                 ....*....|
gi 495176583 158 LACLSAQILW 167
Cdd:COG0671  178 AIALLLLALL 187
acidPPc smart00014
Acid phosphatase homologues;
60-164 1.89e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 74.30  E-value: 1.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583    60 ALALLISLAVSWLAGHLFPHPRPFVV------GLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWHRVWSG-----ALLM 128
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLsigdacCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGrklliFLLL 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 495176583   129 AVACAIAWSRVYLGVHWPLDMAGGLLVAMLACLSAQ 164
Cdd:smart00014  81 LLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
59-161 1.58e-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: 53.58  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   59 FALALLISLAVSWLAGHLFPHPRPFVVGLGHQFLP-----HAPDDSYPSDHGTVIFTFALAFLFW-------HRVWSGAL 126
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPapstlPGLGYSFPSGHSATAFALALLLALLlrrlrkiVRVLLALL 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 495176583  127 LMAVACAIAWSRVYLGVHWPLDMAGGLLVAMLACL 161
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLAL 116
 
Name Accession Description Interval E-value
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
1-197 4.96e-118

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 333.13  E-value: 4.96e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   1 MMEALNQFLFLQINATPASPGWLIALATFIARDLISIVPLLPVVLWLWRP-----TERRLVVKFALALLISLAVSWLAGH 75
Cdd:PRK11837   1 MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLILIVPLLAVVLWLWGPrdqltAQRQLVIKIAIALAISLLVSWTIGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  76 LFPHPRPFVVGLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWHRVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLV 155
Cdd:PRK11837  81 LFPHDRPFVEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWSGSLLMAIAVAIAWSRVYLGVHWPLDMLGALLV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495176583 156 AMLACLSAQILWAPLGEPLYRTLRQLYRLCFALPIRKGWVRD 197
Cdd:PRK11837 161 GMIGCLSAQIIWQLFGEKLYQRLQRLYRFCFALPIRKGWVRD 202
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
23-165 2.42e-55

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: 172.06  E-value: 2.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  23 LIALATFIARDLISIVPLLPVVLWLWRPTERRLVVKFA-LALLISLAVSWLAGHLFPHPRPFVVGLGHQFLPHAPDDSYP 101
Cdd:cd03385    1 LDALAIFIAEYLIYILPLLLVVLWLWGGEKQRKVVLFAtIAVAVALLINYIIGLLYFHPRPFVVGLGHNLLPHAADSSFP 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495176583 102 SDHGTVIFTFALAFLFWHRVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLVAMLACLSAQI 165
Cdd:cd03385   81 SDHTTLFFSIAFSLLLRRRKWAGWILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSALLVFQ 144
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
1-167 1.73e-18

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: 78.93  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   1 MMEALNQFLFLQINATPASPGWLIALATFIARDLISIVPLLPVVLWLWRPTERRLVVKFALALLISLAVSWLAG--HLFP 78
Cdd:COG0671   18 DLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLlkYLFG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  79 HPRPFVVGLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWH-RVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLVAM 157
Cdd:COG0671   98 RPRPFVVPDLELLLGTAGGYSFPSGHAAAAFALALVLALLLpRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGL 177
                        170
                 ....*....|
gi 495176583 158 LACLSAQILW 167
Cdd:COG0671  178 AIALLLLALL 187
acidPPc smart00014
Acid phosphatase homologues;
60-164 1.89e-17

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 74.30  E-value: 1.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583    60 ALALLISLAVSWLAGHLFPHPRPFVV------GLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFWHRVWSG-----ALLM 128
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLsigdacCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGrklliFLLL 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 495176583   129 AVACAIAWSRVYLGVHWPLDMAGGLLVAMLACLSAQ 164
Cdd:smart00014  81 LLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
53-161 1.06e-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: 69.80  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  53 RRLVVKFALALLISLAVSWLAGHLFPHPRPFVV----GLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFW-----HRVWS 123
Cdd:cd01610    2 RLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLlrcgPDGDPLLLTEGGYSFPSGHAAFAFALALFLALLlprrlLRLLL 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495176583 124 GALLMAVACAIAWSRVYLGVHWPLDMAGGLLVAMLACL 161
Cdd:cd01610   82 GLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVAL 119
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
10-166 5.62e-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: 66.86  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  10 FLQINATPASPGWLIALATFIARDLISIVPLLpVVLWLWRPTERRLVVKFALALLISLAVSWLAGHLFPHPRPFvvglgH 89
Cdd:cd03392   19 LLRSLRTPLLTAFMTAITFLGSPAVLLIIVLL-LALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRPP-----L 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  90 QFLPHAPDDSYPSDH--GTVIFTFALAFLFWH-------RVWSGALLMAVACAIAWSRVYLGVHWPLDMAGGLLVAMLAC 160
Cdd:cd03392   93 HLLVPEGGYSFPSGHamGATVLYGFLAYLLARrlprrrvRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLLGLAWL 172

                 ....*.
gi 495176583 161 LSAQIL 166
Cdd:cd03392  173 ALLILL 178
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
1-155 4.88e-10

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: 56.12  E-value: 4.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   1 MMEALNQFLFLQINATPASPgWLIALATFIARDLISIVPLLPVVLWLWRpteRRLVVKFALALLISLAV-------SWLA 73
Cdd:cd03395    1 LLEQIDVWLFLLLNGTLVHP-LLDDLMPFLTGKKLSVPIFLLLALFILF---RKGPIGLLILLLVLLAVgfadqlaSGFL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  74 GHLFPHPRP-FVVGLGHQFLPHAPDDSY--PSDHGTVIFTFALAF-LFWHRVWSGALLMAVACAIAWSRVYLGVHWPLDM 149
Cdd:cd03395   77 KPLVARLRPcNALDGVRLVVLGDQGGSYsfASSHAANSFALALFIwLFFRRGLFSPVLLLWALLVGYSRVYVGVHYPGDV 156

                 ....*.
gi 495176583 150 AGGLLV 155
Cdd:cd03395  157 IAGALI 162
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
54-156 9.16e-10

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: 55.90  E-value: 9.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  54 RLVVKFALALLISLAVSWLAGHLFPHPRPFVVGlGHQFLPH-------APDDSYPSDHGTVIFTFA--LAFLFwHRVWSG 124
Cdd:cd03380   93 RLYALLARALTDAGIATWDAKYHYNRPRPFVAI-RLQWLPIctpeegtPKHPSYPSGHATFGGAAAlvLAELF-PERAAE 170
                         90       100       110
                 ....*....|....*....|....*....|..
gi 495176583 125 alLMAVACAIAWSRVYLGVHWPLDMAGGLLVA 156
Cdd:cd03380  171 --LLARAAEAGNSRVVAGVHWPSDVEAGRILG 200
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
59-161 1.58e-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: 53.58  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   59 FALALLISLAVSWLAGHLFPHPRPFVVGLGHQFLP-----HAPDDSYPSDHGTVIFTFALAFLFW-------HRVWSGAL 126
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPapstlPGLGYSFPSGHSATAFALALLLALLlrrlrkiVRVLLALL 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 495176583  127 LMAVACAIAWSRVYLGVHWPLDMAGGLLVAMLACL 161
Cdd:pfam01569  82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLAL 116
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
40-158 8.20e-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: 46.21  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  40 LLPVVLWLwrpTERRLVVKFALALLISLAVSWLAGHLFPHPRPFVV-GLGHQFLPHAPDDSYPSDHGTVIFTFALAFLFW 118
Cdd:cd03393    2 VLSLIYWL---VDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYdGIQAIYEESAGGYGFPSGHAQTSATFWGSLMLH 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495176583 119 HR---VWSGALLMAVAcaIAWSRVYLGVHWPLDMAGGLLVAML 158
Cdd:cd03393   79 VRkkwFTLIGVVLVVL--ISFSRLYLGVHWPSDVIGGVLIGLL 119
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
59-159 3.45e-06

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: 44.24  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  59 FALALLISLAVSWLAGHLFPHPRPFVvglghqflPHAPDDSYPSDHGTVIFTFALAF---LFWHRVWSGAllMAVACAIA 135
Cdd:cd03394    8 LAEAAALTAAVTEGLKFAVGRARPDG--------SNNGYRSFPSGHTASAFAAATFLqyrYGWRWYGIPA--YALASLVG 77
                         90       100
                 ....*....|....*....|....
gi 495176583 136 WSRVYLGVHWPLDMAGGLLVAMLA 159
Cdd:cd03394   78 ASRVVANRHWLSDVLAGAAIGILV 101
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
77-156 2.81e-05

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: 43.09  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  77 FPHPRPFVVglgHQFLPHAPDD--------SYPSDHGTVIFT--FALAFLFWHRvwsGALLMAVACAIAWSRVYLGVHWP 146
Cdd:cd03397  124 YNRPRPFVL---NDEPICTPPDesglakdgSYPSGHTAAGYAwaLILAELVPER---ADEILARGSEYGQSRIVCGVHWP 197
                         90
                 ....*....|
gi 495176583 147 LDMAGGLLVA 156
Cdd:cd03397  198 SDVMGGRIMA 207
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
94-158 5.33e-04

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: 38.75  E-value: 5.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495176583  94 HAPDDSYPSDHGTVIFTFALAFLFW------HRVWSGALLMAVACA-IAWSRVYLGVHWPLDMAGGLLVAML 158
Cdd:cd03388   74 AALEYGFPSTHAMNATAISFYLLIYlydryqYPFVLGLILALFYSTlVCLSRIYMGMHSVLDVIAGSLIGVL 145
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
40-144 7.67e-04

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: 38.41  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  40 LLPVVLWL----WRPTERRLV-VKFALALLISLAVSWLAGHLFPHPRPFvvgLGHQFLPHAPddSYPSDHGTVIFTFALA 114
Cdd:cd03382   23 LLPVAILVgyatLILFRRELEaIYLFIGLLANEALNYVLKRIIKEPRPC---SGAYFVRSGY--GMPSSHSQFMGFFAVY 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495176583 115 FL------------FWHRVWSGALLMAVACAIAWSRVYLGVH 144
Cdd:cd03382   98 LLlfiylrlgrlnsLVSRFLLSLGLLLLALLVSYSRVYLGYH 139
PAP2_Aur1_like cd03386
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
8-161 1.26e-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: 38.06  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583   8 FLFLQINATPASPGWLIALATFIardLISIVPLLPVVLWLW------RPTERRLVVKFALALLISLAVSWLaghlFPHPR 81
Cdd:cd03386   11 FLSIYLESNLQRHIPLDPLAWFP---YGSLHFLVPLALLAWlflfrpPGTLRRFRRALGLANLLGLLIYLL----FPTAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  82 PFVVGLGHQFLPHAPDDSY-----------------PSDHGTVIFTFALAFLFWHRVWSGALLMAVACAIAWSRVYLGVH 144
Cdd:cd03386   84 PRYEPPYGLILLVLLMYGSagytsgfggfdnpfnafPSLHVAWAVLAALFLWRHRRRLLRWLAVLWPLLIWLSTLYLGNH 163
                        170
                 ....*....|....*..
gi 495176583 145 WPLDMAGGLLVAMLACL 161
Cdd:cd03386  164 YFIDLVGGIALALLSFY 180
PAP2_containing_2_like cd03391
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ...
53-158 2.70e-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: 36.91  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495176583  53 RRLVVKFALALLISLAVSWLAGHLFPHPRPFVVGLGhQFLPHAPDD-SYPSDHGTVIFtFALAFLFWHRVWSGALLMAV- 130
Cdd:cd03391   46 QEVLVNLLLGLLLDIITVAILKALVRRRRPAYNSPD-MLDYVAVDKySFPSGHASRAA-FVARFLLNHLVLAVPLRVLLv 123
                         90       100       110
                 ....*....|....*....|....*....|
gi 495176583 131 --ACAIAWSRVYLGVHWPLDMAGGLLVAML 158
Cdd:cd03391  124 lwATVVGISRVLLGRHHVLDVLAGAFLGYL 153
PAP2_haloperoxidase cd03398
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ...
99-154 3.34e-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: 37.02  E-value: 3.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495176583  99 SYPSDHGTVIFTFA--LAFLF--------------------WHRVWSGALLMAVAcaIAWSRVYLGVHWPLDMAGGLL 154
Cdd:cd03398  146 SYPSGHATFAGAAAtvLKALFgsdkvpdtvsepdeggpstgVTRVWAELNELADE--VAISRVYAGVHFRSDDAAGAA 221
 
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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