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Conserved domains on  [gi|658754231|ref|WP_029772994|]
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MULTISPECIES: patatin family protein [Pseudoalteromonas]

Protein Classification

patatin family protein( domain architecture ID 11468705)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
18-315 1.50e-102

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


:

Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 302.47  E-value: 1.50e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  18 PKVALIAEGGGQRGIFTAGVLDAWLEQNYdPFDLFIGTSAGSQNLTSYLARQKGYAKRLIRGLSRNKRFFQLGRGLMGKH 97
Cdd:COG4667    4 MKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLRGGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  98 IVDLDWYFEKTTEVNRALDFKTAKTSlgERELLITATNARDRKAYYLSPTGEGKQWRDLLKASSALPFLYKqGVKLtpwl 177
Cdd:COG4667   83 LFDLDFLYDEIPNELLPFDFETFKAS--PREFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP-PVEI---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 178 gtkaaneahlaaeqsSEDFYLDGGLAAPLPVREAYNRGARKIVVIRTVDEHFQAQTAWVQKLRTFACASgyCPKTLDYLI 257
Cdd:COG4667  156 ---------------DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLYRK--YPKLVEALL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658754231 258 QHEQAYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAGRAYL 315
Cdd:COG4667  219 NRHERYNETLEFIEQLEKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFL 276
 
Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
18-315 1.50e-102

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 302.47  E-value: 1.50e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  18 PKVALIAEGGGQRGIFTAGVLDAWLEQNYdPFDLFIGTSAGSQNLTSYLARQKGYAKRLIRGLSRNKRFFQLGRGLMGKH 97
Cdd:COG4667    4 MKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLRGGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  98 IVDLDWYFEKTTEVNRALDFKTAKTSlgERELLITATNARDRKAYYLSPTGEGKQWRDLLKASSALPFLYKqGVKLtpwl 177
Cdd:COG4667   83 LFDLDFLYDEIPNELLPFDFETFKAS--PREFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP-PVEI---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 178 gtkaaneahlaaeqsSEDFYLDGGLAAPLPVREAYNRGARKIVVIRTVDEHFQAQTAWVQKLRTFACASgyCPKTLDYLI 257
Cdd:COG4667  156 ---------------DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLYRK--YPKLVEALL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658754231 258 QHEQAYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAGRAYL 315
Cdd:COG4667  219 NRHERYNETLEFIEQLEKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFL 276
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
22-311 3.53e-80

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: 244.83  E-value: 3.53e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  22 LIAEGGGQRGIFTAGVLDAWLEQNYDPFDLFIGTSAGSQNLTSYLARQKGYAKRLIRGLSRNKRFFQLGRGLMGKHIVDL 101
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRSLLRTGNLFDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 102 DWYFEKTTEVNRALDFKTAKTSLgeRELLITATNARDRKAYYLSPTGEGKQWRDLLKASSALPFLYKQGvkltpwlgtka 181
Cdd:cd07208   81 DFLYDELPDGLDPFDFEAFAASP--ARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFPPV----------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 182 aneahlaaeQSSEDFYLDGGLAAPLPVREAYNRGARKIVVIRTVDEHFQAQTAWVQKLRTFACASgyCPKTLDYLIQHEQ 261
Cdd:cd07208  148 ---------RIDGEPYVDGGLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSSPLAKLLYRK--YPNLVEALLRRHS 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 658754231 262 AYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAG 311
Cdd:cd07208  217 RYNETLEFIRRLEAEGKIFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA 266
DUF6363 pfam19890
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ...
249-320 2.43e-18

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: 77.95  E-value: 2.43e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658754231  249 CPKTLDYLIQHEQAYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAGRAYLKSQNA 320
Cdd:pfam19890   1 YPKLVDALLKRYESYNETLDFIENPEKEGKAFVIRPEKPLKSSRLESDPEKLEADYELGYEDGRRFLEELKE 72
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
26-58 9.36e-03

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 37.48  E-value: 9.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 658754231  26 GGGQRGIFTAGVLdAWLEQNY-----DPFDLFIGTSAG 58
Cdd:NF041079   8 GGGYRGLYTASVL-AELEEQFgrpiaDHFDLICGTSIG 44
 
Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
18-315 1.50e-102

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 302.47  E-value: 1.50e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  18 PKVALIAEGGGQRGIFTAGVLDAWLEQNYdPFDLFIGTSAGSQNLTSYLARQKGYAKRLIRGLSRNKRFFQLGRGLMGKH 97
Cdd:COG4667    4 MKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLRGGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  98 IVDLDWYFEKTTEVNRALDFKTAKTSlgERELLITATNARDRKAYYLSPTGEGKQWRDLLKASSALPFLYKqGVKLtpwl 177
Cdd:COG4667   83 LFDLDFLYDEIPNELLPFDFETFKAS--PREFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP-PVEI---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 178 gtkaaneahlaaeqsSEDFYLDGGLAAPLPVREAYNRGARKIVVIRTVDEHFQAQTAWVQKLRTFACASgyCPKTLDYLI 257
Cdd:COG4667  156 ---------------DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLYRK--YPKLVEALL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658754231 258 QHEQAYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAGRAYL 315
Cdd:COG4667  219 NRHERYNETLEFIEQLEKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFL 276
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
22-311 3.53e-80

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: 244.83  E-value: 3.53e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  22 LIAEGGGQRGIFTAGVLDAWLEQNYDPFDLFIGTSAGSQNLTSYLARQKGYAKRLIRGLSRNKRFFQLGRGLMGKHIVDL 101
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRSLLRTGNLFDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 102 DWYFEKTTEVNRALDFKTAKTSLgeRELLITATNARDRKAYYLSPTGEGKQWRDLLKASSALPFLYKQGvkltpwlgtka 181
Cdd:cd07208   81 DFLYDELPDGLDPFDFEAFAASP--ARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFPPV----------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 182 aneahlaaeQSSEDFYLDGGLAAPLPVREAYNRGARKIVVIRTVDEHFQAQTAWVQKLRTFACASgyCPKTLDYLIQHEQ 261
Cdd:cd07208  148 ---------RIDGEPYVDGGLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSSPLAKLLYRK--YPNLVEALLRRHS 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 658754231 262 AYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAG 311
Cdd:cd07208  217 RYNETLEFIRRLEAEGKIFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA 266
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
15-222 7.75e-24

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 98.05  E-value: 7.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  15 TAQPKVALIAEGGGQRGIFTAGVLDAWLEQNYdPFDLFIGTSAGSQNLTSYLArqkGYAKRLIRGLSRNKRFFQLGRGLM 94
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGI-PPDVIAGTSAGAIVGALYAA---GYSADELEELWRSLDRRDLFDLSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  95 GKHIVDLDWYFE-----KTTEVNRALDFKTAKTSLGE--RELLITATNARDRKAYYLSpTGEGkqwRDLLKASSALPFLY 167
Cdd:COG1752   78 PRRLLRLDLGLSpggllDGDPLRRLLERLLGDRDFEDlpIPLAVVATDLETGREVVFD-SGPL---ADAVRASAAIPGVF 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 658754231 168 KqgvkltpwlgtkaaneahlaAEQSSEDFYLDGGLAAPLPVREAYNRGARKIVVI 222
Cdd:COG1752  154 P--------------------PVEIDGRLYVDGGVVNNLPVDPARALGADRVIAV 188
DUF6363 pfam19890
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ...
249-320 2.43e-18

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: 77.95  E-value: 2.43e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658754231  249 CPKTLDYLIQHEQAYLDELTFIANPPSDVEIIQIFADEKLHSKLLGSSNDDLRFDHKLGVKAGRAYLKSQNA 320
Cdd:pfam19890   1 YPKLVDALLKRYESYNETLDFIENPEKEGKAFVIRPEKPLKSSRLESDPEKLEADYELGYEDGRRFLEELKE 72
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
22-227 2.91e-15

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: 73.48  E-value: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  22 LIAEGGGQRGIFTAGVLDAwLEQNYDPFDLFIGTSAGSQNLTSYLARQKGYAKRLI---RGLSRNKRFFqlgRGLMGkhi 98
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKA-LAEAGIEPDIISGTSIGAINGALIAGGDPEAVERLEklwRELSREDVFL---RGLLD--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  99 vdldwyfekttevnRALDFKTAKTS-LGERELLITATNARDRKAYYLSPTGEGKQwRDLLKASSALPfLYKQGVKLtpwl 177
Cdd:cd07209   74 --------------RALDFDTLRLLaILFAGLVIVAVNVLTGEPVYFDDIPDGIL-PEHLLASAALP-PFFPPVEI---- 133
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 658754231 178 gtkaaneahlaaeqsSEDFYLDGGLAAPLPVREAYNRGARKIVVIRTVDE 227
Cdd:cd07209  134 ---------------DGRYYWDGGVVDNTPLSPAIDLGADEIIVVSLSDK 168
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
22-208 4.81e-15

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: 71.99  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  22 LIAEGGGQRGIFTAGVLDAWLEQNYdPFDLFIGTSAGSQNLTSYLARQKGY-AKRLIRGLSRNKRFFQLGRGLMGKHIVD 100
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGP-LIDIIAGTSAGAIVAALLASGRDLEeALLLLLRLSREVRLRFDGAFPPTGRLLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231 101 LDWYFEkttevnrALDFKTAKTSLGERELLITATNARDRKAYYLSPTGEGKQWRDLLkASSALPFLYKQGVkltpwlgtk 180
Cdd:cd07198   80 ILRQPL-------LSALPDDAHEDASGKLFISLTRLTDGENVLVSDTSKGELWSAVR-ASSSIPGYFGPVP--------- 142
                        170       180
                 ....*....|....*....|....*...
gi 658754231 181 aaneahlaaEQSSEDFYLDGGLAAPLPV 208
Cdd:cd07198  143 ---------LSFRGRRYGDGGLSNNLPV 161
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
25-212 6.76e-14

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: 69.18  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231   25 EGGGQRGIFTAGVLDAwLEQNYDPFDLFIGTSAGSQNLTSY-LARQKGYAKRLIRGLSRNKRFFQLGRGLMGKHIVDLDW 103
Cdd:pfam01734   4 SGGGARGAYHLGVLKA-LGEAGIRFDVISGTSAGAINAALLaLGRDPEEIEDLLLELDLNLFLSLIRKRALSLLALLRGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  104 YFEKT--------TEVNRALDFKTAKTSLGERELLITATNARDRKAYYLSPTGEGKQ-----------WRDLLKASSALP 164
Cdd:pfam01734  83 IGEGGlfdgdalrELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARIllpddldddedLADAVLASSALP 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 658754231  165 FLYKQgVKLTPwlgtkaaneahlaaeqsseDFYLDGGLAAPLPVREAY 212
Cdd:pfam01734 163 GVFPP-VRLDG-------------------ELYVDGGLVDNVPVEAAL 190
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
20-220 9.09e-08

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: 51.39  E-value: 9.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  20 VALIAEGGGQRGIFTAGVLDAwLEQNYDPFDLFIGTSAGSqnL------TSYLARQKGYAKRLIRGLSRNKRFFQLGRGL 93
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKA-LEEAGIPIDIVSGTSAGA--IvgalyaAGYSPEEIEERAKLRSTDLKALSDLTIPTAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  94 MGKHIVdLDWYFEKTTevnRALDFKTAKTslgerELLITATNARDRKAYYLSptgEGKQWRDlLKASSALPFLYKQgVKL 173
Cdd:cd07205   78 LLRGDK-FLELLDEYF---GDRDIEDLWI-----PFFIVATDLTSGKLVVFR---SGSLVRA-VRASMSIPGIFPP-VKI 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 658754231 174 tpwlgtkaaneahlaaeqsSEDFYLDGGLAAPLPVREAYNRGARKIV 220
Cdd:cd07205  144 -------------------DGQLLVDGGVLNNLPVDVLRELGADIII 171
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
26-222 1.43e-06

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 49.13  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  26 GGGQRGIFTAGVLDAwLEQNYDP-----FDLFIGTSAGSQnLTSYLArqKGYAKRLIRGLSRN-------KRFFQLGRGL 93
Cdd:COG3621   14 GGGIRGLIPARILAE-LEERLGKplaeyFDLIAGTSTGGI-IALGLA--AGYSAEEILDLYEEegkeifpKSRWRKLLSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  94 MGkhivdldWYFEK--TTEVNRALDFKTAKTSLGE--RELLITATNARDRKAYYL-SPTGEGKQWRDLL-----KASSAL 163
Cdd:COG3621   90 RG-------LFGPKydSEGLEKVLKEYFGDTTLGDlkTPVLIPSYDLDNGKPVFFkSPHAKFDRDRDFLlvdvaRATSAA 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658754231 164 PFLYKqgvkltpwlgtkaanEAHLAAEQSSEDFYLDGGLAAPLPV-------REAYNRGARKIVVI 222
Cdd:COG3621  163 PTYFP---------------PAQIKNLTGEGYALIDGGVFANNPAlcalaeaLKLLGPDLDDILVL 213
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
20-222 4.45e-06

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: 47.49  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  20 VALIAEGGGQRGIFTAGVLDAwLEQNYDPFDLFIGTSAGSQNLTSYlARQKGyakrLIRGLSRNKRFfqLGR-GLMGKHI 98
Cdd:cd07227   11 IGLVLGGGGARGISHIGILQA-LEEAGIPIDAIGGTSIGSFVGGLY-AREAD----LVPIFGRAKKF--AGRmASMWRFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  99 VDLDWYFEKTT---EVNRALdFKT-AKTSLGE--RELLITATNARDRKAYYLSptgEGKQWRdLLKASSALPFLykqgvk 172
Cdd:cd07227   83 SDVTYPFASYTtghEFNRGI-WKTfGNTHIEDfwIPFYANSTNITHSRMEIHS---SGYAWR-YIRASMSLAGL------ 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 658754231 173 LTPWLgtkaaneahlaaeqSSEDFYLDGGLAAPLPVREAYNRGARKIVVI 222
Cdd:cd07227  152 LPPLS--------------DNGSMLLDGGYMDNLPVSPMRSLGIRDIFAV 187
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
26-222 5.49e-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: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  26 GGGQRGIFTAGVLDAwLE---QNYDP----FDLFIGTSAGSqnltsylarqkgyakrLI-RGLSRnkrffqlgRGLMGKH 97
Cdd:cd07199    6 GGGIRGIIPAEILAE-LEkrlGKPSRiadlFDLIAGTSTGG----------------IIaLGLAL--------GRYSAEE 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658754231  98 IVDLdwYFEKTTEVnraldFKTaktslgereLLITATNARDRKAYYLS-----PTGEGKQW--RDLLKASSALPFLYKqg 170
Cdd:cd07199   61 LVEL--YEELGRKI-----FPR---------VLVTAYDLSTGKPVVFSnydaeEPDDDDDFklWDVARATSAAPTYFP-- 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 658754231 171 vkltpwlgtkaaneAHLAAEQSSEDFYLDGGLAAPLPVREAY-------NRGARKIVVI 222
Cdd:cd07199  123 --------------PAVIESGGDEGAFVDGGVAANNPALLALaealrllAPDKDDILVL 167
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
22-59 2.23e-03

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: 38.17  E-value: 2.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 658754231  22 LIAEGGGQRGIFTAGVLDAWLEQN-YDPFDLFIGTSAGS 59
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGlLDCVTYLAGTSGGA 39
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
26-58 9.36e-03

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 37.48  E-value: 9.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 658754231  26 GGGQRGIFTAGVLdAWLEQNY-----DPFDLFIGTSAG 58
Cdd:NF041079   8 GGGYRGLYTASVL-AELEEQFgrpiaDHFDLICGTSIG 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.
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