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Conserved domains on  [gi|339298588|gb|AEJ50698|]
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hypothetical protein CCDC5180_1861 [Mycobacterium tuberculosis CCDC5180]

Protein Classification

patatin-like phospholipase family protein( domain architecture ID 10163346)

patatin-like phospholipase family protein similar to Legionella pneumophila VipD and Pseudomonas aeruginosa type III secretion effector protein ExoU

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 10-214 1.03e-60

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


:

Pssm-ID: 132846  Cd Length: 194  Bit Score: 192.49  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  10 DLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVTRLAEMmrsiDYPKFLDRnligHVPL 89
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKET----DFAKLLDS----PVGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  90 IGGGLSLLLSDGVYRGAYLEQLLGGLLADLGVHTFGDLRTGEAPEQFAWSLVVTASDLSRRRLVRipwdldSYGIHPDDF 169
Cdd:cd07207   73 LFLLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVV------FSAETTPDM 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 339298588 170 SVARAVHASSAIPFVFEPVR-VRGATWVDGGLLSNFPVALFDRTDA 214
Cdd:cd07207  147 PVAKAVRASMSIPFVFKPVRlAKGDVYVDGGVLDNYPVWLFDGWEL 192
 
Name Accession Description Interval E-value
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 10-214 1.03e-60

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 192.49  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  10 DLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVTRLAEMmrsiDYPKFLDRnligHVPL 89
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKET----DFAKLLDS----PVGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  90 IGGGLSLLLSDGVYRGAYLEQLLGGLLADLGVHTFGDLRTGEAPEQFAWSLVVTASDLSRRRLVRipwdldSYGIHPDDF 169
Cdd:cd07207   73 LFLLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVV------FSAETTPDM 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 339298588 170 SVARAVHASSAIPFVFEPVR-VRGATWVDGGLLSNFPVALFDRTDA 214
Cdd:cd07207  147 PVAKAVRASMSIPFVFKPVRlAKGDVYVDGGVLDNYPVWLFDGWEL 192
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 8-306 3.20e-45

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 154.68  E-value: 3.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   8 RVDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAalqtAGEPVTRLAEMMRSIDYPKFLDRNLIGHV 87
Cdd:COG1752    6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYA----AGYSADELEELWRSLDRRDLFDLSLPRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  88 PLIgggLSLLLSDGVYRGAYLEQllgGLLADLGVHTFGDLRTgeapeqfawSLVVTASDLSRRRLVRIpwdldsygihpD 167
Cdd:COG1752   82 LRL---DLGLSPGGLLDGDPLRR---LLERLLGDRDFEDLPI---------PLAVVATDLETGREVVF-----------D 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588 168 DFSVARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFDRTDAEprwPTFGIRLSARPGIPPTrpvqgPVSLGIAA 247
Cdd:COG1752  136 SGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGAD---RVIAVDLNPPLRKLPS-----LLDILGRA 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 339298588 248 IETLVSNQDNAYIdDPCTVRRTIFVPAHDVSPIDFDitaeQREALYQRGFQAGQKFLAN 306
Cdd:COG1752  208 LEIMFNSILRREL-ALEPADILIEPDLSGISLLDFS----RAEELIEAGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 11-210 5.72e-32

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 118.10  E-value: 5.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   11 LVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVtrlaEMMRSIDYPKFLDRNLIGHVPLI 90
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIE----DLLLELDLNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   91 GGGLSLLLSDGVYRGAYLEQLLGGLLADLGVHTFGDLRTGEAPEQFAWSLVVTASDLSRRRLVRIPWDLDsygihpDDFS 170
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLD------DDED 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 339298588  171 VARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFD 210
Cdd:pfam01734 151 LADAVLASSALPGVFPPVRLDGELYVDGGLVDNVPVEAAL 190
 
Name Accession Description Interval E-value
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 10-214 1.03e-60

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 192.49  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  10 DLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVTRLAEMmrsiDYPKFLDRnligHVPL 89
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKET----DFAKLLDS----PVGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  90 IGGGLSLLLSDGVYRGAYLEQLLGGLLADLGVHTFGDLRTGEAPEQFAWSLVVTASDLSRRRLVRipwdldSYGIHPDDF 169
Cdd:cd07207   73 LFLLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVV------FSAETTPDM 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 339298588 170 SVARAVHASSAIPFVFEPVR-VRGATWVDGGLLSNFPVALFDRTDA 214
Cdd:cd07207  147 PVAKAVRASMSIPFVFKPVRlAKGDVYVDGGVLDNYPVWLFDGWEL 192
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 8-306 3.20e-45

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 154.68  E-value: 3.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   8 RVDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAalqtAGEPVTRLAEMMRSIDYPKFLDRNLIGHV 87
Cdd:COG1752    6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYA----AGYSADELEELWRSLDRRDLFDLSLPRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  88 PLIgggLSLLLSDGVYRGAYLEQllgGLLADLGVHTFGDLRTgeapeqfawSLVVTASDLSRRRLVRIpwdldsygihpD 167
Cdd:COG1752   82 LRL---DLGLSPGGLLDGDPLRR---LLERLLGDRDFEDLPI---------PLAVVATDLETGREVVF-----------D 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588 168 DFSVARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFDRTDAEprwPTFGIRLSARPGIPPTrpvqgPVSLGIAA 247
Cdd:COG1752  136 SGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGAD---RVIAVDLNPPLRKLPS-----LLDILGRA 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 339298588 248 IETLVSNQDNAYIdDPCTVRRTIFVPAHDVSPIDFDitaeQREALYQRGFQAGQKFLAN 306
Cdd:COG1752  208 LEIMFNSILRREL-ALEPADILIEPDLSGISLLDFS----RAEELIEAGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 11-210 5.72e-32

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 118.10  E-value: 5.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   11 LVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVtrlaEMMRSIDYPKFLDRNLIGHVPLI 90
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIE----DLLLELDLNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   91 GGGLSLLLSDGVYRGAYLEQLLGGLLADLGVHTFGDLRTGEAPEQFAWSLVVTASDLSRRRLVRIPWDLDsygihpDDFS 170
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLD------DDED 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 339298588  171 VARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFD 210
Cdd:pfam01734 151 LADAVLASSALPGVFPPVRLDGELYVDGGLVDNVPVEAAL 190
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 11-216 9.66e-22

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 90.30  E-value: 9.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  11 LVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVTRLAEMMRSIdypKFLDRNLIGHVPLI 90
Cdd:cd07205    3 LALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDL---KALSDLTIPTAGLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  91 ggglslllsdgvyRGAYLEQLLGglladlgvHTFGDLRTgeapEQFAWSLVVTASDLSRRRLVripwdldsygIHpDDFS 170
Cdd:cd07205   80 -------------RGDKFLELLD--------EYFGDRDI----EDLWIPFFIVATDLTSGKLV----------VF-RSGS 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 339298588 171 VARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFDRTDAEP 216
Cdd:cd07205  124 LVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRELGADI 169
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 11-206 9.72e-22

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 91.20  E-value: 9.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  11 LVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAalQTAGEPVTRLAEMMRSIDYPKFLDRNLIGHVPLi 90
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIA--GGDPEAVERLEKLWRELSREDVFLRGLLDRALD- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  91 ggglslllsdgvyrgayleqllgglladlgVHTFGDLRTGEAPeqfawsLVVTASDLSRRRLVRIpwDLDSYGIHPDdfs 170
Cdd:cd07209   78 ------------------------------FDTLRLLAILFAG------LVIVAVNVLTGEPVYF--DDIPDGILPE--- 116

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 339298588 171 varAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPV 206
Cdd:cd07209  117 ---HLLASAALPPFFPPVEIDGRYYWDGGVVDNTPL 149
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 11-207 8.81e-18

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 79.31  E-value: 8.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  11 LVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAALQTAGEPVTRLAEMMRSIDYpkfldRNLIGHVPLi 90
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRL-----RFDGAFPPT- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  91 ggglslllsdgvyrGAYLeqllgglladlgvhtfGDLRTGEAPEQFAwSLVVTASDLSRRRLVRIPWDLDSYGIHPDDFS 170
Cdd:cd07198   75 --------------GRLL----------------GILRQPLLSALPD-DAHEDASGKLFISLTRLTDGENVLVSDTSKGE 123

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 339298588 171 VARAVHASSAIPFVFEPV--RVRGATWVDGGLLSNFPVA 207
Cdd:cd07198  124 LWSAVRASSSIPGYFGPVplSFRGRRYGDGGLSNNLPVA 162
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 11-300 1.77e-17

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 80.73  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  11 LVCEGGGVRGIGLVGAVDALADAGYR-FPRVAGSSAGAIVASLVAALQT--AGEPVTRLAEMMRSIDYPKFL-DRNLIGh 86
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRpFDLVIGVSAGALNAASYLSGQRgrALRINTKYATDPRYLGLRSLLrTGNLFD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  87 vpliggglsllLSDGVYRGAYLEQllgglladlgvhTFgDLRTGEApeqFAWSLVVTASDLSRRRlvRIPWDLDsyGIHP 166
Cdd:cd07208   80 -----------LDFLYDELPDGLD------------PF-DFEAFAA---SPARFYVVATDADTGE--AVYFDKP--DILD 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588 167 DDFsvaRAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFDRTDAE--------PRwptfGIRLSARPGIPPTRPVQ 238
Cdd:cd07208  129 DLL---DALRASSALPGLFPPVRIDGEPYVDGGLSDSIPVDKAIEDGADkivviltrPR----GYRKKPSKSSPLAKLLY 201

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339298588 239 gpvSLGIAAIETLVSNQD--NAYIDDpctVRR-----TIFVPAHD----VSPIDFDItaEQREALYQRGFQAG 300
Cdd:cd07208  202 ---RKYPNLVEALLRRHSryNETLEF---IRRleaegKIFVIAPEkplkVSRLERDP--EKLEALYDLGYEDA 266
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 9-232 8.58e-17

Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 77.77  E-value: 8.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   9 VDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAalqtAGEPVTRLAEMMRSIDYPKFL-DRNLIGHV 87
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFA----SGISPDEMAELLLSLERKDFWmFWDPPLRG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  88 PLIGGGLSLllsdgvyrgAYLEQllggllaDLGVHTFGDLRTgeapeqfawSLVVTASDLSRRRLVripwdLDSYGihpd 167
Cdd:cd07210   77 GLLSGDRFA---------ALLRE-------HLPPDRFEELRI---------PLAVSVVDLTSRETL-----LLSEG---- 122

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339298588 168 dfSVARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVALFdrtdAEPRWPTFGIRLSARPGIP 232
Cdd:cd07210  123 --DLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPFDAL----RPEIERILYHHVAPRRPWE 181
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
6-308 1.83e-13

Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 69.42  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   6 TARVDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAI-VASLVaalqtAGEPVTRLAEMMRSIDYPKFLD-RNL 83
Cdd:COG4667    3 MMKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALnGASYL-----SRQPGRARRVITDYATDPRFFSlRNF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  84 IGHVPLIGGGlslllsdgvyrgayleqllgglladlgvHTFGDLRTGEAP---EQFAWS---LVVTASDLSRRRLVripw 157
Cdd:COG4667   78 LRGGNLFDLD----------------------------FLYDEIPNELLPfdfETFKASpreFYVVATNADTGEAE---- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588 158 DLDSYGIHPDDFsvaRAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPV--AL---FDRTDAeprwptfgIRlsarpgip 232
Cdd:COG4667  126 YFSKKDDDYDLL---DALRASSALPLLYPPVEIDGKRYLDGGVADSIPVreAIrdgADKIVV--------IL-------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588 233 pTRPVQ---GPVSLGI----------AAIETLVS-----NQDNAYIDD-PCTVRRTIFVPAHD--VSPIDFDItaEQREA 291
Cdd:COG4667  187 -TRPRGyrkKPSKFKRllrrlyrkypKLVEALLNrheryNETLEFIEQlEKEGKIFVIRPPKPltVSRLERDP--EKLRA 263

                        330
                 ....*....|....*..
gi 339298588 292 LYQRGFQAGQKFLANWN 308
Cdd:COG4667  264 LYELGYEDARKFLAELK 280
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 9-208 1.66e-07

Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 50.35  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   9 VDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAAlqtaGEPVtRLAEMMRSIDYPKF---LDRNLig 85
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAA----GHLD-ALEEWVRSLSQRDVlrlLDLSA-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  86 hvpliggglsllLSDGVYRGAYLEQLLGGLladlgvhtFGDLRTGEAPEQFAwslvVTASDLSRRRLVRIpwdldSYGih 165
Cdd:cd07228   74 ------------SRSGLLKGEKVLEYLREI--------MGGVTIEELPIPFA----AVATDLQTGKEVWF-----REG-- 122

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 339298588 166 pddfSVARAVHASSAIPFVFEPVRVRGATWVDGGLLSNFPVAL 208
Cdd:cd07228  123 ----SLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVSV 161
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 11-208 2.68e-07

Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 50.79  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  11 LVCEGGGVRGI----------GLVGAVDALADagyRFPRVAGSSAGAIVASLVAALQ-TAGEPVTRLAEMMRSIdypkfl 79
Cdd:cd07199    2 LSLDGGGIRGIipaeilaeleKRLGKPSRIAD---LFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKI------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  80 drnlighvpliggglslllsdgvyrgayleqllgglladlgvhtFGdlrtgeapeqfawSLVVTASDLSRRRLVRIPWDL 159
Cdd:cd07199   73 --------------------------------------------FP-------------RVLVTAYDLSTGKPVVFSNYD 95

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 339298588 160 DSYGIHPDDFSVARAVHASSAIPFVFEPVRVRGATW----VDGGLLSNFPVAL 208
Cdd:cd07199   96 AEEPDDDDDFKLWDVARATSAAPTYFPPAVIESGGDegafVDGGVAANNPALL 148
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 1-208 2.98e-06

Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 47.98  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588   1 MALVSTARVdLVCEGGGVRGIGLVGAVDALADA-----GYRFPRVAGSSAGAIVASLVAALQTAGEpvtrlaemMRSIdy 75
Cdd:COG3621    1 MSANKPFRI-LSLDGGGIRGLIPARILAELEERlgkplAEYFDLIAGTSTGGIIALGLAAGYSAEE--------ILDL-- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  76 pkFLDrnligHVPLIGGGLSLLLSDGV-------YRGAYLEQLLGglladlgvHTFGDLRTGEAPEqfawSLVVTASDLS 148
Cdd:COG3621   70 --YEE-----EGKEIFPKSRWRKLLSLrglfgpkYDSEGLEKVLK--------EYFGDTTLGDLKT----PVLIPSYDLD 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339298588 149 RRRlvriPWDLDSY---GIHPDDFSVARAVHASSAIPFVFEPVRVRGATW-----VDGGLLSNFPVAL 208
Cdd:COG3621  131 NGK----PVFFKSPhakFDRDRDFLLVDVARATSAAPTYFPPAQIKNLTGegyalIDGGVFANNPALC 194
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 11-54 2.70e-05

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 43.56  E-value: 2.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 339298588  11 LVCEGGGVRGIGLVGAVDALADAGYRFP--RVAGSSAGAIVASLVA 54
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLLDCvtYLAGTSGGAWVAATLY 46
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 11-54 4.69e-04

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 41.43  E-value: 4.69e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 339298588  11 LVCEGGGVRGIGLVGAVDALADAGYrFPRV-AGSSAGAIVASLVA 54
Cdd:cd07206   72 LMLSGGASLGLFHLGVVKALWEQDL-LPRViSGSSAGAIVAALLG 115
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 9-54 9.19e-04

Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This family includes NTE1 from fungi.


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 40.17  E-value: 9.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 339298588   9 VDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVA 54
Cdd:cd07227   11 IGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYA 56
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 8-80 1.09e-03

Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologous to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.


Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 40.08  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339298588   8 RVDLVCEGGGVRGIGLVGAVDALADAGYRFPRVAGSSAGAIVASLVAA---LQTAGEPVTRLAEMMRSIdYPKFLD 80
Cdd:cd07225   15 SIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEernISRMKQRAREWAKDMTSI-WKKLLD 89
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 15-212 1.67e-03

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 39.26  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  15 GGGVRGIGLVGAVDALADAGYRF----PRVAGSSAGAIVASLVAALQTAGEPVTRLAEMMRSIDY----PKFLDRNLIGH 86
Cdd:cd07204    6 GCGFLGIYHVGVASALREHAPRLlqnaRRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRrslgPLHPSFNLLKI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339298588  87 VpliggglslllsdgvyrgayLEQLLGGLLADLGVHTFGDLRtgeapeqfawslvVTASDLSRRRLVRIpwdldsygihp 166
Cdd:cd07204   86 L--------------------RQGLEKILPDDAHELASGRLH-------------ISLTRVSDGENVLV----------- 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 339298588 167 DDFS----VARAVHASSAIPFV--FEPVRVRGATWVDGGLLSNFPVALFDRT 212
Cdd:cd07204  122 SEFDskeeLIQALVCSCFIPFYcgLIPPKFRGVRYIDGGLSDNLPILDDENT 173
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 8-78 9.63e-03

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


Pssm-ID: 132868  Cd Length: 421  Bit Score: 37.59  E-value: 9.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339298588   8 RVDLVCEGGGVRGIGLVGAVDALADAGYrFPRV-AGSSAGAIVASlVAALQTAGEpvtrLAEMMRSIDYPKF 78
Cdd:cd07230   73 RTALLLSGGGTFGMFHIGVLKALFEANL-LPRIiSGSSAGSIVAA-ILCTHTDEE----IPELLEEFPYGDF 138
 
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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