NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515200991|ref|WP_016809136|]
View 

patatin family protein [Klebsiella oxytoca]

Protein Classification

patatin family protein( domain architecture ID 11468705)

patatin family protein similar to Escherichia coli YjjU; the family includes putative phospholipases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
20-303 5.29e-129

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


:

Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 370.65  E-value: 5.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  20 FQPGRLALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMRFVR 99
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 100 GGNLIDLDWLVDSTAKK-MPLAMAYAedrFAQGKEFWMCACRGDDYTPNYFSPTQ--QTWLDLIRASSAIPGFYRsGVML 176
Cdd:COG4667   80 GGNLFDLDFLYDEIPNElLPFDFETF---KASPREFYVVATNADTGEAEYFSKKDddYDLLDALRASSALPLLYP-PVEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 177 DGVSYLDGGVSDAIPVQEAARRGAQTIVVIRTVPSQMYYTPQWFKRMERWLGeSSLQPFVNLVQHHETTYRSTQEFIEKP 256
Cdd:COG4667  156 DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLY-RKYPKLVEALLNRHERYNETLEFIEQL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 515200991 257 PGKLRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCGRYFLATVGK 303
Cdd:COG4667  235 EKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELKA 281
 
Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
20-303 5.29e-129

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 370.65  E-value: 5.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  20 FQPGRLALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMRFVR 99
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 100 GGNLIDLDWLVDSTAKK-MPLAMAYAedrFAQGKEFWMCACRGDDYTPNYFSPTQ--QTWLDLIRASSAIPGFYRsGVML 176
Cdd:COG4667   80 GGNLFDLDFLYDEIPNElLPFDFETF---KASPREFYVVATNADTGEAEYFSKKDddYDLLDALRASSALPLLYP-PVEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 177 DGVSYLDGGVSDAIPVQEAARRGAQTIVVIRTVPSQMYYTPQWFKRMERWLGeSSLQPFVNLVQHHETTYRSTQEFIEKP 256
Cdd:COG4667  156 DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLY-RKYPKLVEALLNRHERYNETLEFIEQL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 515200991 257 PGKLRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCGRYFLATVGK 303
Cdd:COG4667  235 EKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELKA 281
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 27-294 8.78e-88

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: 265.24  E-value: 8.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAGFNPFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMRFVRGGNLIDL 106
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRSLLRTGNLFDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 107 DWLVDSTAKKM-PLAMayaeDRFAQ-GKEFWMCACRGDDYTPNYFSPTQ--QTWLDLIRASSAIPGFYRsGVMLDGVSYL 182
Cdd:cd07208   81 DFLYDELPDGLdPFDF----EAFAAsPARFYVVATDADTGEAVYFDKPDilDDLLDALRASSALPGLFP-PVRIDGEPYV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 183 DGGVSDAIPVQEAARRGAQTIVVIRTVPSQMYYTPQWFKrmerWLGESSLQPFVNLVQ---HHETTYRSTQEFIEKPPGK 259
Cdd:cd07208  156 DGGLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSS----PLAKLLYRKYPNLVEallRRHSRYNETLEFIRRLEAE 231

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 515200991 260 LRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCG 294
Cdd:cd07208  232 GKIFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA 266
DUF6363 pfam19890
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ...
 232-305 3.70e-26

Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. This domain is found at the C-terminal of patatin-like proteins from bacteria. There is a conserved tyrosine residue and a conserved FxxxPP sequence motif.


Pssm-ID: 466223 [Multi-domain]  Cd Length: 75  Bit Score: 99.53  E-value: 3.70e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515200991  232 LQPFVNLVQHHETTYRSTQEFIEKPPGKLRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCGRYFLATVGKLL 305
Cdd:pfam19890   1 YPKLVDALLKRYESYNETLDFIENPEKEGKAFVIRPEKPLKSSRLESDPEKLEADYELGYEDGRRFLEELKEFL 74
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
25-63 5.00e-03

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 38.25  E-value: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 515200991  25 LALvcEGGGQRGIFTAGVLDEFMRAgFN-P----FDMLFGTSAG 63
Cdd:NF041079   4 LSL--SGGGYRGLYTASVLAELEEQ-FGrPiadhFDLICGTSIG 44
 
Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
20-303 5.29e-129

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 370.65  E-value: 5.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  20 FQPGRLALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMRFVR 99
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 100 GGNLIDLDWLVDSTAKK-MPLAMAYAedrFAQGKEFWMCACRGDDYTPNYFSPTQ--QTWLDLIRASSAIPGFYRsGVML 176
Cdd:COG4667   80 GGNLFDLDFLYDEIPNElLPFDFETF---KASPREFYVVATNADTGEAEYFSKKDddYDLLDALRASSALPLLYP-PVEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 177 DGVSYLDGGVSDAIPVQEAARRGAQTIVVIRTVPSQMYYTPQWFKRMERWLGeSSLQPFVNLVQHHETTYRSTQEFIEKP 256
Cdd:COG4667  156 DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLY-RKYPKLVEALLNRHERYNETLEFIEQL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 515200991 257 PGKLRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCGRYFLATVGK 303
Cdd:COG4667  235 EKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELKA 281
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 27-294 8.78e-88

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: 265.24  E-value: 8.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAGFNPFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMRFVRGGNLIDL 106
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRSLLRTGNLFDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 107 DWLVDSTAKKM-PLAMayaeDRFAQ-GKEFWMCACRGDDYTPNYFSPTQ--QTWLDLIRASSAIPGFYRsGVMLDGVSYL 182
Cdd:cd07208   81 DFLYDELPDGLdPFDF----EAFAAsPARFYVVATDADTGEAVYFDKPDilDDLLDALRASSALPGLFP-PVRIDGEPYV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 183 DGGVSDAIPVQEAARRGAQTIVVIRTVPSQMYYTPQWFKrmerWLGESSLQPFVNLVQ---HHETTYRSTQEFIEKPPGK 259
Cdd:cd07208  156 DGGLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSS----PLAKLLYRKYPNLVEallRRHSRYNETLEFIRRLEAE 231

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 515200991 260 LRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCG 294
Cdd:cd07208  232 GKIFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA 266
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 27-205 6.05e-39

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: 136.32  E-value: 6.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAGFNPfDMLFGTSAGAQNVSAYLCNQPGYARK-VITRYTTAREFFDPMRFVRGGNLID 105
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLI-DIIAGTSAGAIVAALLASGRDLEEALlLLLRLSREVRLRFDGAFPPTGRLLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 106 LDWLVDSTAKKmplAMAYaedRFAQGKEFWMCACRGDDYTPNYFSPTQQTWLDLIRASSAIPGFYRSG-VMLDGVSYLDG 184
Cdd:cd07198   80 ILRQPLLSALP---DDAH---EDASGKLFISLTRLTDGENVLVSDTSKGELWSAVRASSSIPGYFGPVpLSFRGRRYGDG 153

                        170       180
                 ....*....|....*....|.
gi 515200991 185 GVSDAIPVQEAarrgAQTIVV 205
Cdd:cd07198  154 GLSNNLPVAEL----GNTINV 170
DUF6363 pfam19890
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ...
 232-305 3.70e-26

Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. This domain is found at the C-terminal of patatin-like proteins from bacteria. There is a conserved tyrosine residue and a conserved FxxxPP sequence motif.


Pssm-ID: 466223 [Multi-domain]  Cd Length: 75  Bit Score: 99.53  E-value: 3.70e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515200991  232 LQPFVNLVQHHETTYRSTQEFIEKPPGKLRILEIYPQKPLKSMALGSRLPALLEDYKTGRQCGRYFLATVGKLL 305
Cdd:pfam19890   1 YPKLVDALLKRYESYNETLDFIENPEKEGKAFVIRPEKPLKSSRLESDPEKLEADYELGYEDGRRFLEELKEFL 74
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 22-210 9.68e-26

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 103.83  E-value: 9.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  22 PGRLALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPmRFVRGG 101
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGI-PPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDL-SLPRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 102 NLIDLDWLVDSTAKKMPLAMAYAE----DRFAQ-GKEFWMCACRGDDYTPNYFS--PTqqtwLDLIRASSAIPGFYRSgV 174
Cdd:COG1752   82 LRLDLGLSPGGLLDGDPLRRLLERllgdRDFEDlPIPLAVVATDLETGREVVFDsgPL----ADAVRASAAIPGVFPP-V 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515200991 175 MLDGVSYLDGGVSDAIPVQEAARRGAQTIVVIRTVP 210
Cdd:COG1752  157 EIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNP 192
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 27-195 1.40e-21

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: 90.75  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991   27 LVCEGGGQRGIFTAGVLDEFMRAGFNpFDMLFGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMR------FVRG 100
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-FDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralslLALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  101 GNLIDLDWLVDSTAKKMPLAMAYAEDRFAQGKEFWMCACRGD------------DYTPNYFSPTQQT----WLDLIRASS 164
Cdd:pfam01734  80 RGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVAlralltvistalGTRARILLPDDLDddedLADAVLASS 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 515200991  165 AIPGFYrSGVMLDGVSYLDGGVSDAIPVQEA 195
Cdd:pfam01734 160 ALPGVF-PPVRLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 27-210 2.85e-19

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: 85.04  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAYLCNQPGYARKvitryttAREFFDPMR----FVRGGn 102
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGI-EPDIISGTSIGAINGALIAGGDPEAVER-------LEKLWRELSredvFLRGL- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 103 lidLDWLVD-STAKKMPLAmayaedrfaqgkEFWMCACRGDDYTPN--YFS--PTQQTwLDLIRASSAIPGFYRSgVMLD 177
Cdd:cd07209   72 ---LDRALDfDTLRLLAIL------------FAGLVIVAVNVLTGEpvYFDdiPDGIL-PEHLLASAALPPFFPP-VEID 134

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515200991 178 GVSYLDGGVSDAIPVQEAARRGAQTIVVIRTVP 210
Cdd:cd07209  135 GRYYWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 25-204 2.30e-13

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: 67.57  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  25 LALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQnVSAYLC--NQPGYARKVITRYTTAREFFDPMRFVRGGn 102
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGI-PIDIVSGTSAGAI-VGALYAagYSPEEIEERAKLRSTDLKALSDLTIPTAG- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 103 LIDLD---WLVDSTAKKM-------PLAMAyAEDrFAQGKE--FWmcacRGDDYTPnyfsptqqtwldlIRASSAIPGFY 170
Cdd:cd07205   78 LLRGDkflELLDEYFGDRdiedlwiPFFIV-ATD-LTSGKLvvFR----SGSLVRA-------------VRASMSIPGIF 138

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515200991 171 rSGVMLDGVSYLDGGVSDAIPVQEAARRGAQTIV 204
Cdd:cd07205  139 -PPVKIDGQLLVDGGVLNNLPVDVLRELGADIII 171
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 25-211 3.35e-10

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: 59.28  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  25 LALVCEGGGQRGIFTAGVLDEFMRAGFNPFDMLfGTSAGAQNVSAYLCNQPGYARKVITRYTTAREFFDPMRFVRGGNLI 104
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAIS-GTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFWDPPLRGGLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 105 DLDWLVDSTAKKMPlamayaEDRFAQgkefwmcaCRGDDYTPNYFSPTQQTWL-------DLIRASSAIPGFYRSgVMLD 177
Cdd:cd07210   80 SGDRFAALLREHLP------PDRFEE--------LRIPLAVSVVDLTSRETLLlsegdlaEAVAASCAVPPLFQP-VEIG 144

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515200991 178 GVSYLDGGVSDAIPVQEAARRGaQTIVVIRTVPS 211
Cdd:cd07210  145 GRPFVDGGVADRLPFDALRPEI-ERILYHHVAPR 177
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 27-192 9.39e-09

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: 54.59  E-value: 9.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQnVSAYLCNqpGYARKVITRYTTAREFFDPM----------- 95
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGI-LKKRVAGTSAGAI-TAALLAL--GYSAADIKDILKETDFAKLLdspvgllfllp 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  96 RFVRGGNLID----LDWLVDSTAKKM-------PLAMAYAEdrfaQGKEFWMCACRGDDYTPNYFSPTQQTWLDL---IR 161
Cdd:cd07207   78 SLFKEGGLYKgdalEEWLRELLKEKTgnsfatsLLRDLDDD----LGKDLKVVATDLTTGALVVFSAETTPDMPVakaVR 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 515200991 162 ASSAIPGFYRSGVMLDGVSYLDGGVSDAIPV 192
Cdd:cd07207  154 ASMSIPFVFKPVRLAKGDVYVDGGVLDNYPV 184
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 25-255 1.32e-07

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: 52.11  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  25 LALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAylcnqpgYARK--VITRYTTAREFFDPM----RFv 98
Cdd:cd07227   11 IGLVLGGGGARGISHIGILQALEEAGI-PIDAIGGTSIGSFVGGL-------YAREadLVPIFGRAKKFAGRMasmwRF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  99 rggnLIDLDWlvdstakkmPLAMAYAEDRFAQG----------KEFWM---CACRGDDYTPNYFSPTQQTWlDLIRASSA 165
Cdd:cd07227   82 ----LSDVTY---------PFASYTTGHEFNRGiwktfgnthiEDFWIpfyANSTNITHSRMEIHSSGYAW-RYIRASMS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 166 IPGFY----RSGVMLdgvsyLDGGVSDAIPVQEAARRGAQTIVVIrTVPSQMYYTPQ--------WFKRMERWLGESSLQ 233
Cdd:cd07227  148 LAGLLpplsDNGSML-----LDGGYMDNLPVSPMRSLGIRDIFAV-DVGSVDDRTPMdygdsvsgVWIFFNRWNPFSSRP 221

                        250       260
                 ....*....|....*....|...
gi 515200991 234 PFVNLVQ-HHETTYRSTQEFIEK 255
Cdd:cd07227  222 NVPSMAEiQSRLTYVSSVKTLEK 244
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 31-186 2.17e-06

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 48.75  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  31 GGGQRGIFTAGVLDEFMRAGFNP----FDMLFGTSAGAQNVSAYLCnqpGY-ARKVITRYTT-AREFFDPMRFVRggnLI 104
Cdd:COG3621   14 GGGIRGLIPARILAELEERLGKPlaeyFDLIAGTSTGGIIALGLAA---GYsAEEILDLYEEeGKEIFPKSRWRK---LL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 105 DLDWLV----DSTAKKMPLAMAYAEDRFAQG-KEFWMCACRGDDYTPNYFS--PTQQTW------LDLIRASSAIPGFYR 171
Cdd:COG3621   88 SLRGLFgpkyDSEGLEKVLKEYFGDTTLGDLkTPVLIPSYDLDNGKPVFFKspHAKFDRdrdfllVDVARATSAAPTYFP 167

                        170
                 ....*....|....*....
gi 515200991 172 ----SGVMLDGVSYLDGGV 186
Cdd:COG3621  168 paqiKNLTGEGYALIDGGV 186
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 26-204 6.37e-06

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: 46.11  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  26 ALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQNVSAYLCnqpGYARKVITRYTTAReffdpMRFVRGgnLID 105
Cdd:cd07228    2 GLALGSGGARGWAHIGVLRALEEEGI-EIDIIAGSSIGALVGALYAA---GHLDALEEWVRSLS-----QRDVLR--LLD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 106 LDW----LVDSTAKKMPLAMAYAEDRFAQ-GKEFWMCAC---RGddytpnyfsptQQTWL------DLIRASSAIPGFYR 171
Cdd:cd07228   71 LSAsrsgLLKGEKVLEYLREIMGGVTIEElPIPFAAVATdlqTG-----------KEVWFregsliDAIRASISIPGIFA 139

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515200991 172 SgVMLDGVSYLDGGVSDAIPVQEAARRGAQTIV 204
Cdd:cd07228  140 P-VEHNGRLLVDGGVVNPIPVSVARALGADIVI 171
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 27-204 1.43e-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: 44.71  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAG-FNPFDMLFGTSAGAQnVSAYLCNqPGYARKVITRyTTAREFFDPMRFVRGGNLID 105
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGlLDCVTYLAGTSGGAW-VAATLYP-PSSSLDNKPR-QSLEEALSGKLWVSFTPVTA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991 106 LDWLVDSTAKKMplamaYAEDR--FAQGkeFWmcacrgddytPNYFSPtqqtwldlirassaIPGFY----RSGVMLDGV 179
Cdd:cd01819   78 GENVLVSRFVSK-----EELIRalFASG--SW----------PSYFGL--------------IPPAElytsKSNLKEKGV 126

                        170       180
                 ....*....|....*....|....*..
gi 515200991 180 SYLDGGVSDA--IPVQEAARRGAQTIV 204
Cdd:cd01819  127 RLVDGGVSNNlpAPVLLRPGRGVTLTI 153
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 27-186 6.51e-05

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: 43.86  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  27 LVCEGGGQRGIFTAGVLDEFMRAGFNP------FDMLFGTSAGAqnVSAYLCNQPGY-ARKVITRYTT-AREFFDPMrFV 98
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKRLGKPsriadlFDLIAGTSTGG--IIALGLALGRYsAEELVELYEElGRKIFPRV-LV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  99 RGGNLIDLDWLVDSTAKkmplamayAEDRfaqgkefwmcaCRGDDYTPnyfsptqqtWlDLIRASSAIPGF---YRSGVM 175
Cdd:cd07199   79 TAYDLSTGKPVVFSNYD--------AEEP-----------DDDDDFKL---------W-DVARATSAAPTYfppAVIESG 129

                        170
                 ....*....|.
gi 515200991 176 LDGVSYLDGGV 186
Cdd:cd07199  130 GDEGAFVDGGV 140
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 31-205 1.66e-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: 39.64  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  31 GGGQRGIFTAGVLDEFMRAGfnPF-----DMLFGTSAGAQNVSAYLCNQP-GYARKVITRYTTA---REF------FDPM 95
Cdd:cd07204    6 GCGFLGIYHVGVASALREHA--PRllqnaRRIAGASAGAIVAAVVLCGVSmEEACSFILKVVSEarrRSLgplhpsFNLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  96 RFVRGGnLIDLdwLVDSTAKKMPLAMAYAEDRFAQGKEFWMcacrgDDYTPNYfsptqqtwlDLIRA---SSAIPGFyrS 172
Cdd:cd07204   84 KILRQG-LEKI--LPDDAHELASGRLHISLTRVSDGENVLV-----SEFDSKE---------ELIQAlvcSCFIPFY--C 144

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515200991 173 G---VMLDGVSYLDGGVSDAIPVQEAarrgAQTIVV 205
Cdd:cd07204  145 GlipPKFRGVRYIDGGLSDNLPILDD----ENTITV 176
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 23-194 2.19e-03

Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. 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 been found also in vertebrates.


Pssm-ID: 132870  Cd Length: 407  Bit Score: 39.56  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  23 GRLALVCEGGGQRGIFTAGVLDEFMRAGFNPfDMLFGTSAGAQnVSAYLCNQPGYARKVITRYTTAREF---FDPM---- 95
Cdd:cd07232   66 GRTALCLSGGAAFAYYHFGVVKALLDADLLP-NVISGTSGGSL-VAALLCTRTDEELKQLLVPELARKItacEPPWlvwi 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515200991  96 -RFVRGGNLID-LDWLVDS---TAKKMPLAMAYAEdrfaQGKEFWMCACRGDDYTP----NYF-SPTQQTWLDLIrASSA 165
Cdd:cd07232  144 pRWLKTGARFDsVEWARTCcwfTRGSMTFEEAYER----TGRILNISVVPADPHSPtillNYLtSPNCTIWSAVL-ASAA 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515200991 166 IPGFYRSGVML-------------DGVSYLDGGVSDAIPVQE 194
Cdd:cd07232  219 VPGILNPVVLMmkdpdgtlippfsFGSKWKDGSLRTDIPLKA 260
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 24-95 4.76e-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: 38.54  E-value: 4.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515200991  24 RLALVCEGGGQRGIFTAGVLDEFMRAGFnPFDMLFGTSAGAQnVSAYLCNQpgyaRKVITRYTTAREFFDPM 95
Cdd:cd07225   15 SIALVLGGGGARGCAHIGVIKALEEAGI-PVDMVGGTSIGAF-IGALYAEE----RNISRMKQRAREWAKDM 80
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
25-63 5.00e-03

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 38.25  E-value: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 515200991  25 LALvcEGGGQRGIFTAGVLDEFMRAgFN-P----FDMLFGTSAG 63
Cdd:NF041079   4 LSL--SGGGYRGLYTASVLAELEEQ-FGrPiadhFDLICGTSIG 44
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH