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Conserved domains on  [gi|504513069|ref|WP_014700171|]
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phosphatase PAP2 family protein [Pectobacterium parmentieri]

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 ...
 80-315 2.25e-64

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: 206.42  E-value: 2.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069  80 AQETSQQADIEWLHNSGYDFAVKANQQAgIALLESFSHLSTDVLQQNTAIVTRINREATKGQREQALVDAEGQgyLYYLA 159
Cdd:cd03397   11 SQQPAPSATIRALPASGYLPPVGATPDS-LDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADLS--FPGAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 160 DALGPRLGKvfitaYDRGEIRKAAVLLKLSAVS-TSAAKQHFNYPRPFLQPNNTIHLVPDTavigdnkPYTATGGAFPSG 238
Cdd:cd03397   88 NAFSCALGE-----ERTPELYRLLRRVLEDAGSaTYPAKKYYNRPRPFVLNDEPICTPPDE-------SGLAKDGSYPSG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513069 239 HTNTGYTDALLLAEMIPERFVPLIDRGARYGYSRVVLGVHYPLDVMGSRMIAERNVAHYLNDPQYRRLFEQAKAELR 315
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 ...
 80-315 2.25e-64

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: 206.42  E-value: 2.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069  80 AQETSQQADIEWLHNSGYDFAVKANQQAgIALLESFSHLSTDVLQQNTAIVTRINREATKGQREQALVDAEGQgyLYYLA 159
Cdd:cd03397   11 SQQPAPSATIRALPASGYLPPVGATPDS-LDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADLS--FPGAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 160 DALGPRLGKvfitaYDRGEIRKAAVLLKLSAVS-TSAAKQHFNYPRPFLQPNNTIHLVPDTavigdnkPYTATGGAFPSG 238
Cdd:cd03397   88 NAFSCALGE-----ERTPELYRLLRRVLEDAGSaTYPAKKYYNRPRPFVLNDEPICTPPDE-------SGLAKDGSYPSG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513069 239 HTNTGYTDALLLAEMIPERFVPLIDRGARYGYSRVVLGVHYPLDVMGSRMIAERNVAHYLNDPQYRRLFEQAKAELR 315
Cdd:cd03397  156 HTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 182-290 3.08e-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: 93.57  E-value: 3.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 182 AAVLLKLSAVSTSAAKQHFNYPRPFLQPNNTIHLVPdtavigdnkpytATGGAFPSGHTNTGYTDALLLAEMIPER--FV 259
Cdd:COG0671   78 AALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGT------------AGGYSFPSGHAAAAFALALVLALLLPRRwlAA 145

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504513069 260 PLIDRGARYGYSRVVLGVHYPLDVMGSRMIA 290
Cdd:COG0671  146 LLLALALLVGLSRVYLGVHYPSDVLAGALLG 176
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 188-290 1.52e-13

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


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 67.06  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069  188 LSAVSTSAAKQHFNYPRPFlqpnntiHLVPDTAVIGDNKPYTATGGAFPSGHTNTGYTDALLLAEMIPERFVPLIDRGAR 267
Cdd:pfam01569   8 LAGLLSSVLKDYFGRPRPF-------FLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 504513069  268 Y--------GYSRVVLGVHYPLDVMGSRMIA 290
Cdd:pfam01569  81 LllvlallvGLSRLYLGVHFPSDVLAGALIG 111
acidPPc smart00014
Acid phosphatase homologues;
196-290 1.50e-12

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 63.90  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069   196 AKQHFNYPRPF-LQPNNTIHLVPDTAVigdnkpyTATGGAFPSGHTNTGYTDALLLAEMIPERF------VPLIDRGARY 268
Cdd:smart00014  14 IKNYFGRPRPFfLSIGDACCTPNFLLT-------LEAGYSFPSGHTAFAFAFALFLLLYLPARAgrklliFLLLLLALVV 86

                           90       100
                   ....*....|....*....|..
gi 504513069   269 GYSRVVLGVHYPLDVMGSRMIA 290
Cdd:smart00014  87 GFSRVYLGAHWPSDVLAGSLLG 108
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 179-290 2.12e-03

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 39.23  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 179 IRKAAVLLKLSAVSTSAAKQHFNYPRPFlqpnntihlvpdTAVIGDNKPYTATGGAFPSGHTNTGYTDALLLAEMIPERF 258
Cdd:PRK11837  61 VIKIAIALAISLLVSWTIGHLFPHDRPF------------VEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWS 128

                         90       100       110
                 ....*....|....*....|....*....|...
gi 504513069 259 -VPLIDRGARYGYSRVVLGVHYPLDVMGSRMIA 290
Cdd:PRK11837 129 gSLLMAIAVAIAWSRVYLGVHWPLDMLGALLVG 161
 
Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
 80-315 2.25e-64

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: 206.42  E-value: 2.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069  80 AQETSQQADIEWLHNSGYDFAVKANQQAgIALLESFSHLSTDVLQQNTAIVTRINREATKGQREQALVDAEGQgyLYYLA 159
Cdd:cd03397   11 SQQPAPSATIRALPASGYLPPVGATPDS-LDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADLS--FPGAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 160 DALGPRLGKvfitaYDRGEIRKAAVLLKLSAVS-TSAAKQHFNYPRPFLQPNNTIHLVPDTavigdnkPYTATGGAFPSG 238
Cdd:cd03397   88 NAFSCALGE-----ERTPELYRLLRRVLEDAGSaTYPAKKYYNRPRPFVLNDEPICTPPDE-------SGLAKDGSYPSG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513069 239 HTNTGYTDALLLAEMIPERFVPLIDRGARYGYSRVVLGVHYPLDVMGSRMIAERNVAHYLNDPQYRRLFEQAKAELR 315
Cdd:cd03397  156 HTAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
 117-299 1.66e-42

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: 148.74  E-value: 1.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 117 HLSTDVLQQNTAIVTRINREATKG----QREQALVDAEGQGYLYYLADALGPRLGKVFITAYDRGEIRKAAVLLKLSAV- 191
Cdd:cd03380   28 PALSAAYAADLAEVKALGALQSTArttaQTALAAFDADGGDPPPHYANAFSIALGTPGLSEERTPRLYALLARALTDAGi 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 192 STSAAKQHFNYPRPFLQPNNTIHlvpdtaVIGDNKPYTATGGAFPSGHTNTGYTDALLLAEMIPERFVPLIDRGARYGYS 271
Cdd:cd03380  108 ATWDAKYHYNRPRPFVAIRLQWL------PICTPEEGTPKHPSYPSGHATFGGAAALVLAELFPERAAELLARAAEAGNS 181

                        170       180
                 ....*....|....*....|....*...
gi 504513069 272 RVVLGVHYPLDVMGSRMIAERNVAHYLN 299
Cdd:cd03380  182 RVVAGVHWPSDVEAGRILGEAIAAALLA 209
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 182-290 3.08e-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: 93.57  E-value: 3.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 182 AAVLLKLSAVSTSAAKQHFNYPRPFLQPNNTIHLVPdtavigdnkpytATGGAFPSGHTNTGYTDALLLAEMIPER--FV 259
Cdd:COG0671   78 AALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGT------------AGGYSFPSGHAAAAFALALVLALLLPRRwlAA 145

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504513069 260 PLIDRGARYGYSRVVLGVHYPLDVMGSRMIA 290
Cdd:COG0671  146 LLLALALLVGLSRVYLGVHYPSDVLAGALLG 176
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 188-290 2.69e-17

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: 77.50  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 188 LSAVSTSAAKQHFNYPRPFLQPNNTIHLVPDTAvigdnkpyTATGGAFPSGHTNTGYTDALLLAEMIPERF------VPL 261
Cdd:cd01610   14 AGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLLL--------TEGGYSFPSGHAAFAFALALFLALLLPRRLlrlllgLLL 85

                         90       100
                 ....*....|....*....|....*....
gi 504513069 262 IDRGARYGYSRVVLGVHYPLDVMGSRMIA 290
Cdd:cd01610   86 LLLALLVGLSRVYLGVHYPSDVLAGALLG 114
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 188-290 1.52e-13

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


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 67.06  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069  188 LSAVSTSAAKQHFNYPRPFlqpnntiHLVPDTAVIGDNKPYTATGGAFPSGHTNTGYTDALLLAEMIPERFVPLIDRGAR 267
Cdd:pfam01569   8 LAGLLSSVLKDYFGRPRPF-------FLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 504513069  268 Y--------GYSRVVLGVHYPLDVMGSRMIA 290
Cdd:pfam01569  81 LllvlallvGLSRLYLGVHFPSDVLAGALIG 111
acidPPc smart00014
Acid phosphatase homologues;
196-290 1.50e-12

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 63.90  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069   196 AKQHFNYPRPF-LQPNNTIHLVPDTAVigdnkpyTATGGAFPSGHTNTGYTDALLLAEMIPERF------VPLIDRGARY 268
Cdd:smart00014  14 IKNYFGRPRPFfLSIGDACCTPNFLLT-------LEAGYSFPSGHTAFAFAFALFLLLYLPARAgrklliFLLLLLALVV 86

                           90       100
                   ....*....|....*....|..
gi 504513069   269 GYSRVVLGVHYPLDVMGSRMIA 290
Cdd:smart00014  87 GFSRVYLGAHWPSDVLAGSLLG 108
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 174-290 3.34e-08

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: 51.60  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 174 YDRGEIRKAAVLLKLSAVSTSAAKQHFNYPRPFLQPNntihlvpdtavIGDNKPYTATGGAFPSGHTNTGYTDALLLAEM 253
Cdd:cd03393   10 VDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYDG-----------IQAIYEESAGGYGFPSGHAQTSATFWGSLMLH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504513069 254 IPER--------FVPLIdrgaryGYSRVVLGVHYPLDVMGSRMIA 290
Cdd:cd03393   79 VRKKwftligvvLVVLI------SFSRLYLGVHWPSDVIGGVLIG 117
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 182-286 6.55e-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: 52.23  E-value: 6.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 182 AAVLLKLSAVSTSAAKQHFNYPRPflqpnnTIHLvpdtavigdnkPYTATGGAFPSGHTNTGYTDALLLAEMIPERFVPL 261
Cdd:cd03392   67 LLLALLGGGALNTLLKLLVQRPRP------PLHL-----------LVPEGGYSFPSGHAMGATVLYGFLAYLLARRLPRR 129

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504513069 262 IDRGARY----------GYSRVVLGVHYPLDVMGS 286
Cdd:cd03392  130 RVRILLLilaailillvGLSRLYLGVHYPSDVLAG 164
PAP2_BcrC_like cd03385
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ...
 199-290 8.94e-07

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: 48.02  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 199 HFNyPRPFLQP--NNTIHLVPDTAvigdnkpytatggaFPSGHTNTGYTDALLLAeMIPERF--VPLIDRGARYGYSRVV 274
Cdd:cd03385   56 YFH-PRPFVVGlgHNLLPHAADSS--------------FPSDHTTLFFSIAFSLL-LRRRKWagWILLILALLVAWSRIY 119

                         90
                 ....*....|....*.
gi 504513069 275 LGVHYPLDVMGSRMIA 290
Cdd:cd03385  120 LGVHYPLDMLGAALVA 135
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 235-284 1.05e-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: 45.77  E-value: 1.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 504513069 235 FPSGHTNTGYTDALLLAEMIPERFVPLIDRGARYGYSRVVLGVHYPLDVM 284
Cdd:cd03389  120 FPSGHSATAGAAAAALALLFPRYRWAFILLALLIAFSRVIVGAHYPSDVI 169
PAP2_like_4 cd03395
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 180-289 1.64e-05

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: 44.95  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 180 RKAAVLLKLSAVSTSAAKQHF-NYPRPFLQ---PNNTIHLVPDTAVIgdnkpYTATGGAFPSGHTNTGYTDALLLAEMIP 255
Cdd:cd03395   52 PIGLLILLLVLLAVGFADQLAsGFLKPLVArlrPCNALDGVRLVVLG-----DQGGSYSFASSHAANSFALALFIWLFFR 126

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504513069 256 ERF--VPLIDRGARYGYSRVVLGVHYPLDVMGSRMI 289
Cdd:cd03395  127 RGLfsPVLLLWALLVGYSRVYVGVHYPGDVIAGALI 162
PAP2_haloperoxidase cd03398
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ...
 173-292 2.22e-04

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: 42.41  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 173 AYDRGEIRKAAVLLKLSAVSTSA------AKQHFNYPRPFlQPNNTIHLVPDTAVIGDN--KPY--TATGGAFPSGHTNT 242
Cdd:cd03398   76 RPGLSLFRTARLFAAVNAAMTDAgiaawdAKYHYRRWRPV-TAIRLADTDGNPATEADPywLPLagTPPHPSYPSGHATF 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513069 243 GYTDALLLAEMIPERFVPLIDRG---------------------ARYGYSRVVLGVHYPLDVMGSRMIAER 292
Cdd:cd03398  155 AGAAATVLKALFGSDKVPDTVSEpdeggpstgvtrvwaelnelaDEVAISRVYAGVHFRSDDAAGAALGEQ 225
PRK11837 PRK11837
undecaprenyl pyrophosphate phosphatase; Provisional
 179-290 2.12e-03

undecaprenyl pyrophosphate phosphatase; Provisional


Pssm-ID: 183335  Cd Length: 202  Bit Score: 39.23  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513069 179 IRKAAVLLKLSAVSTSAAKQHFNYPRPFlqpnntihlvpdTAVIGDNKPYTATGGAFPSGHTNTGYTDALLLAEMIPERF 258
Cdd:PRK11837  61 VIKIAIALAISLLVSWTIGHLFPHDRPF------------VEGIGYNFLHHAADDSFPSDHGTVIFTFALAFLFWHRLWS 128

                         90       100       110
                 ....*....|....*....|....*....|...
gi 504513069 259 -VPLIDRGARYGYSRVVLGVHYPLDVMGSRMIA 290
Cdd:PRK11837 129 gSLLMAIAVAIAWSRVYLGVHWPLDMLGALLVG 161
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 221-283 2.63e-03

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: 37.31  E-value: 2.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513069 221 VIGDNKPYTATGGA--FPSGHTNTGYTDALLLAEMIPERFV--PLIDRGARYGYSRVVLGVHYPLDV 283
Cdd:cd03394   25 AVGRARPDGSNNGYrsFPSGHTASAFAAATFLQYRYGWRWYgiPAYALASLVGASRVVANRHWLSDV 91
PRK10699 PRK10699
phosphatidylglycerophosphatase B; Provisional
 231-289 7.53e-03

phosphatidylglycerophosphatase B; Provisional


Pssm-ID: 182658  Cd Length: 244  Bit Score: 37.70  E-value: 7.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513069 231 TGGAFPSGHTNTGYTDALLLAEMI-PERfvplidrgaRYGY-------------SRVVLGVHYPLDVMGSRMI 289
Cdd:PRK10699 155 TGFAFPSGHTMFAASWALLAVGLLwPRR---------RYKTvallmlwatgvmgSRLLLGMHWPRDLVVATLI 218
 
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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