|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_SDP1-like |
cd07231 |
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ... |
163-570 |
0e+00 |
|
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.
Pssm-ID: 132869 Cd Length: 323 Bit Score: 584.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 163 MRADLVRNLGNMCNPELHKGRLHVPRLIKEYIDEVSTQLRMVCDMDTEELSLEEKLSFMHETRHAYGRTALLLSGGASLG 242
Cdd:cd07231 1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 243 AFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQSFFegswhalqffdqmggifttvkrvmtqgavheirhl 322
Cdd:cd07231 81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 323 qwklRNLTNNLTFQEAYDITGRILGITVCSLRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGEIVP 402
Cdd:cd07231 126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 403 YHPPFNLdpeegsASVRRWRDGSLEMDLPMIQLKELFNVNHFIVSQANPHIAPFLRMKefvracggrfaaklaqlaemev 482
Cdd:cd07231 202 YHPPGKV------SSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK---------------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 483 khrcnqvlelglplrevaSLFAQEWEGDVTIVMPATFSQYLKIIQNPSNVEIQKAANQGRRCTWEKLAVIKANFGIELAL 562
Cdd:cd07231 254 ------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGIELTL 315
|
....*...
gi 15230231 563 DECVTVLN 570
Cdd:cd07231 316 DECVAELR 323
|
|
| DUF3336 |
pfam11815 |
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ... |
97-226 |
2.66e-43 |
|
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. This family is found in bacteria and eukaryotes. This presumed domain is typically between 143 to 227 amino acids in length.
Pssm-ID: 432096 Cd Length: 139 Bit Score: 153.07 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 97 YRRKFWRNMMRAALTYEEWSHAAKMLDKET-----PKVNETDLFDVELVSNKLDELKHRRHEGSLRDIIFCMRADLVRNL 171
Cdd:pfam11815 6 GRRKRLRKKLRNAKSYEEWKEAAKELDELLgndewKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLKRNF 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15230231 172 GNMCNPELHK-GRLHVPRLIKEYIDEVSTQLRMVCdmDTEELSLEEKLSFMHETRH 226
Cdd:pfam11815 86 AGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLA--ESPSLSLEEKLEFFKETRK 139
|
|
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
230-391 |
2.19e-19 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 88.81 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 230 RTALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGT-RSWPELQSFFEgSWHALQFFD-QMGGIFTTV 307
Cdd:COG1752 6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWR-SLDRRDLFDlSLPRRLLRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 308 KRVMTQGAVHEIRHLQWKLRNLTNNLTFQEAyditGRILGITVCSLRKHEPprclnyltsphVV-----IWSAVTASCAF 382
Cdd:COG1752 85 DLGLSPGGLLDGDPLRRLLERLLGDRDFEDL----PIPLAVVATDLETGRE-----------VVfdsgpLADAVRASAAI 149
|
....*....
gi 15230231 383 PGLFEAQEL 391
Cdd:COG1752 150 PGVFPPVEI 158
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
233-391 |
5.00e-17 |
|
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: 79.96 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWP-ELQSFFEGSWHAL---QFFDQMGGIFTTVK 308
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPeEIEDLLLELDLNLflsLIRKRALSLLALLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 309 RVMTQGAVHEIRHLQWKLRNLTNNLTFQEAYDITGRI--------LGITVCSLRKHEPPRcLNYLTSPHVVIWSAVTASC 380
Cdd:pfam01734 81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralLTVISTALGTRARIL-LPDDLDDDEDLADAVLASS 159
|
170
....*....|.
gi 15230231 381 AFPGLFEAQEL 391
Cdd:pfam01734 160 ALPGVFPPVRL 170
|
|
| PRK10279 |
PRK10279 |
patatin-like phospholipase RssA; |
233-386 |
1.11e-06 |
|
patatin-like phospholipase RssA;
Pssm-ID: 182352 [Multi-domain] Cd Length: 300 Bit Score: 51.25 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQ----SFfeGSWHALQFFD---QMGG--- 302
Cdd:PRK10279 8 LALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEdwvtSF--SYWDVLRLMDlswQRGGllr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 303 ---IFTTVKRVMTqgaVHEIRHLQWKLRNLTNNLTfqeaydiTGRILGITVCSLRKhepprclnyltsphvviwsAVTAS 379
Cdd:PRK10279 86 gerVFNQYREIMP---ETEIENCSRRFGAVATNLS-------TGRELWFTEGDLHL-------------------AIRAS 136
|
....*..
gi 15230231 380 CAFPGLF 386
Cdd:PRK10279 137 CSMPGLM 143
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_SDP1-like |
cd07231 |
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ... |
163-570 |
0e+00 |
|
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.
Pssm-ID: 132869 Cd Length: 323 Bit Score: 584.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 163 MRADLVRNLGNMCNPELHKGRLHVPRLIKEYIDEVSTQLRMVCDMDTEELSLEEKLSFMHETRHAYGRTALLLSGGASLG 242
Cdd:cd07231 1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 243 AFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQSFFegswhalqffdqmggifttvkrvmtqgavheirhl 322
Cdd:cd07231 81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 323 qwklRNLTNNLTFQEAYDITGRILGITVCSLRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGEIVP 402
Cdd:cd07231 126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 403 YHPPFNLdpeegsASVRRWRDGSLEMDLPMIQLKELFNVNHFIVSQANPHIAPFLRMKefvracggrfaaklaqlaemev 482
Cdd:cd07231 202 YHPPGKV------SSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK---------------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 483 khrcnqvlelglplrevaSLFAQEWEGDVTIVMPATFSQYLKIIQNPSNVEIQKAANQGRRCTWEKLAVIKANFGIELAL 562
Cdd:cd07231 254 ------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGIELTL 315
|
....*...
gi 15230231 563 DECVTVLN 570
Cdd:cd07231 316 DECVAELR 323
|
|
| Pat_TGL3-4-5_SDP1 |
cd07206 |
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ... |
163-564 |
3.34e-143 |
|
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: 423.16 E-value: 3.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 163 MRADLVRNLGNMCNPELHKGRLHVPR-LIKEYIDEVSTQLRMVCDMDTEELSLEEKLSFMHETRHAYGRTALLLSGGASL 241
Cdd:cd07206 1 LREGLHGNLGNMGNPSLYRHAYFGTKhLIEDYIEEVDLSLEYLALLDTKELSVEEKLDFFRRARHAFGRTALMLSGGASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 242 GAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELqsffegswhalqffdqmggifttvkrvmtqgavheirh 321
Cdd:cd07206 81 GLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL-------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 322 lqwklrnlTNNLTFQEAYDITGRILGITVCSLRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGEIV 401
Cdd:cd07206 123 --------IGDLTFQEAYERTGRIINITVAPAEPHQNSRLLNALTSPNVLIWSAVLASCAVPGVFPPVMLMAKNRDGEIV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 402 PYHPPfnldpeegsasvRRWRDGSLEMDLPMIQLKELFNVNHFIVSQANPHIAPFLrmkefvracggrfaaklaqlaeme 481
Cdd:cd07206 195 PYLPG------------RKWVDGSVSDDLPAKRLARLYNVNHFIVSQTNPHVVPFL------------------------ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 482 vkhrcnqvlelglplrevaslfaQEWEGDVTIVMPATFSQYLKIIQNPSNVEIQKAANQGRRCTWEKLAVIKANFGIELA 561
Cdd:cd07206 239 -----------------------QEYSGDITIIPPFSFSNPLKLLSNPSEDELQRLILEGERATWPKIEMIRTQTRISRT 295
|
...
gi 15230231 562 LDE 564
Cdd:cd07206 296 LEE 298
|
|
| Pat_TGL4-5_like |
cd07230 |
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ... |
159-569 |
1.67e-118 |
|
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: 364.24 E-value: 1.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 159 IIFCMRADLVRNLGNMCNPELHKgRLHV--PRLIKEYIDEVSTQLRMVCDMDTEELSLEEKLSFMHETRHAYGRTALLLS 236
Cdd:cd07230 1 LLYLIRTTLSRDLGNMGNVNLYR-HSHVgtKKLIERYITEALLTLEYLVDDDEDGLEDRYLLGMLLQTRKNFGRTALLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 237 GGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPE----LQSFFEGSWHALQFFDQMGGIFTTVKRVMT 312
Cdd:cd07230 80 GGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEipelLEEFPYGDFNVFEDPDQEENVLQKLSRFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 313 QGAVHEIRHLQWKLRNLTNNLTFQEAYDITGRILGITVCSLRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELM 392
Cdd:cd07230 160 YGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 393 AKD-RTGEIVPYHPpfnldpeegsaSVRRWRDGSLEMDLPMIQLKELFNVNHFIVSQANPHIAPFLR---------MKEF 462
Cdd:cd07230 240 EKDpKTGEIVPWNP-----------SSVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKksescvggeVEDE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 463 VRACGGRFAAKLAQLAEMEVKHRCNQVLELGL---PLREVASLFAQEWEGDVTIVMPATFSQYLKIIQNPSNVEIQKAAN 539
Cdd:cd07230 309 LSARFKRWLNNVTDLAKDEVLHRLQLLSELGIfpnLLTKLRSVLSQKYSGDITILPELNYSDFPKILKNPTPEFMLDACL 388
|
410 420 430
....*....|....*....|....*....|
gi 15230231 540 QGRRCTWEKLAVIKANFGIELALDECVTVL 569
Cdd:cd07230 389 RGERATWPKLSRIRNHCAIELALDKAIQYL 418
|
|
| Pat_PLPL |
cd07232 |
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ... |
189-565 |
2.29e-94 |
|
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: 300.72 E-value: 2.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 189 LIKEYIDEVSTQLRMVcdMDTEELSLEEKLSFMHETRHAYGRTALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVG 268
Cdd:cd07232 28 LVEEYIDEVEACLKYL--RESSQLDLEEKRRLFKRLSTNYGRTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 269 SVMCAVVGTRS--------WPELQSFFEGSWhalqffdqmGGIFTTVKRVMTQGA----VHEIRHLQWKLRNltnNLTFQ 336
Cdd:cd07232 106 SLVAALLCTRTdeelkqllVPELARKITACE---------PPWLVWIPRWLKTGArfdsVEWARTCCWFTRG---SMTFE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 337 EAYDITGRILGITVCSLRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGEIVPYHPPfnldpeeGSa 416
Cdd:cd07232 174 EAYERTGRILNISVVPADPHSPTILLNYLTSPNCTIWSAVLASAAVPGILNPVVLMMKDPDGTLIPPFSF-------GS- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 417 svrRWRDGSLEMDLPMIQLKELFNVNHFIVSQANPHIAPFL--------RMKEFVRAC---GGRFAAKLAQLAEMEVKHR 485
Cdd:cd07232 246 ---KWKDGSLRTDIPLKALNTLFNVNFSIVSQVNPHINLFFfssrgsvgRPVSHRKGRgwrGGFLLSALEQYLKLDIKKW 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 486 CNQVLELGL---PLREVAS-LFAQEWEGDVTIVMPATFSQYLKIIQNPSNVEIQKAANQGRRCTWEKLAVIKANFGIELA 561
Cdd:cd07232 323 LKVLRDLELlprPLGQDWSqIFLQDFSGTITIWPRSTLSDFLRILSDPTPEDLERMIHEGQQAAFPKLHFIKNRMRIEKA 402
|
....
gi 15230231 562 LDEC 565
Cdd:cd07232 403 IEDG 406
|
|
| Pat_TGL3_like |
cd07229 |
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ... |
154-569 |
1.03e-76 |
|
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG lipase activity of the lipid particle. Triacylglycerol (TAG) lipases are also necessary for the mobilization of TAG stored in lipid particles. TGL3 contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes. This family includes Tgl3p from Saccharomyces cerevisiae.
Pssm-ID: 132867 Cd Length: 391 Bit Score: 253.38 E-value: 1.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 154 GSLRDIIFCMRADLVRNLGNMCNPELH-KGRLHVPRLIKEYIDEVSTQLRMVCD-----MDTEELSLEEKLSFMHETRHA 227
Cdd:cd07229 1 GDILTLLNLLRSGLVRNLGNITSPKLFtRAYAGTKLLIEEYITEVAECLEYVTAlqtspMHSKGFSSQAKLDFFHDTRQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 228 YGRTALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQSFFEGSWHALQFFDQMGG----- 302
Cdd:cd07229 81 FGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDGDGIDLSAFNRLRGkkslg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 303 ---------IFTTVKRVMTQGAVHEIRHLQWKLRNLTNNLTFQEAYDITGRILGITVCSLRKHEPPRCLNYLTSPHVVIW 373
Cdd:cd07229 161 ysgygwlgtLGRRIQRLLREGYFLDVKVLEEFVRANLGDLTFEEAYARTGRVLNITVAPSAVSGSPNLLNYLTAPNVLIW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 374 SAVTAS-CAFPGLFEAQELMAKDRTGEIVPYhppfnldPEEGSASVRRWRDGSL-EMDLPMIQLKELFNVNHFIVSQANP 451
Cdd:cd07229 241 SAALASnASSAALYRSVTLLCKDETGSIVPW-------PPVQVLFFRSWRGANYsERESPLARLSELFNVNHFIVSQARP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 452 HIAPFLRmkefvracggrfaaklaqlaemevkhrcnQVLELGLPLREvaslfaqewegdVTIVMPATFSQYLKIIQNPSN 531
Cdd:cd07229 314 YLAPFLS-----------------------------SDLHENIPGPN------------ITLVPELSFSDFLRLFQNPTT 352
|
410 420 430
....*....|....*....|....*....|....*...
gi 15230231 532 VEIQKAANQGRRCTWEKLAVIKANFGIELALDECVTVL 569
Cdd:cd07229 353 DEIQYWILKGERGVWPALAALRVRCAVEFELDDGYQVL 390
|
|
| DUF3336 |
pfam11815 |
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ... |
97-226 |
2.66e-43 |
|
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. This family is found in bacteria and eukaryotes. This presumed domain is typically between 143 to 227 amino acids in length.
Pssm-ID: 432096 Cd Length: 139 Bit Score: 153.07 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 97 YRRKFWRNMMRAALTYEEWSHAAKMLDKET-----PKVNETDLFDVELVSNKLDELKHRRHEGSLRDIIFCMRADLVRNL 171
Cdd:pfam11815 6 GRRKRLRKKLRNAKSYEEWKEAAKELDELLgndewKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLKRNF 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15230231 172 GNMCNPELHK-GRLHVPRLIKEYIDEVSTQLRMVCdmDTEELSLEEKLSFMHETRH 226
Cdd:pfam11815 86 AGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLA--ESPSLSLEEKLEFFKETRK 139
|
|
| Patatin |
cd07198 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
233-443 |
1.44e-34 |
|
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: 129.77 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQSFFEgswhalqffdqmggifttvkrvmt 312
Cdd:cd07198 1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLL------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 313 qgavheirhlqwKLRNLTNNLTFQEAYDITGRILGITVCSLRK-----------HEPPRCLNYLTSPHVV---------I 372
Cdd:cd07198 57 ------------LRLSREVRLRFDGAFPPTGRLLGILRQPLLSalpddahedasGKLFISLTRLTDGENVlvsdtskgeL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230231 373 WSAVTASCAFPGLFEAQELMAKDrtgeivpyhppfnldpeegsasvRRWRDGSLEMDLPMIQLKELFNVNH 443
Cdd:cd07198 125 WSAVRASSSIPGYFGPVPLSFRG-----------------------RRYGDGGLSNNLPVAELGNTINVSP 172
|
|
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
230-391 |
2.19e-19 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 88.81 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 230 RTALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGT-RSWPELQSFFEgSWHALQFFD-QMGGIFTTV 307
Cdd:COG1752 6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWR-SLDRRDLFDlSLPRRLLRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 308 KRVMTQGAVHEIRHLQWKLRNLTNNLTFQEAyditGRILGITVCSLRKHEPprclnyltsphVV-----IWSAVTASCAF 382
Cdd:COG1752 85 DLGLSPGGLLDGDPLRRLLERLLGDRDFEDL----PIPLAVVATDLETGRE-----------VVfdsgpLADAVRASAAI 149
|
....*....
gi 15230231 383 PGLFEAQEL 391
Cdd:COG1752 150 PGVFPPVEI 158
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
233-391 |
5.00e-17 |
|
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: 79.96 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWP-ELQSFFEGSWHAL---QFFDQMGGIFTTVK 308
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPeEIEDLLLELDLNLflsLIRKRALSLLALLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 309 RVMTQGAVHEIRHLQWKLRNLTNNLTFQEAYDITGRI--------LGITVCSLRKHEPPRcLNYLTSPHVVIWSAVTASC 380
Cdd:pfam01734 81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralLTVISTALGTRARIL-LPDDLDDDEDLADAVLASS 159
|
170
....*....|.
gi 15230231 381 AFPGLFEAQEL 391
Cdd:pfam01734 160 ALPGVFPPVRL 170
|
|
| Pat_ExoU_VipD_like |
cd07207 |
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ... |
233-395 |
4.57e-13 |
|
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: 68.46 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVV--GTRSwPELQSFFEGSwHALQFFDQMGGIFTTVKRV 310
Cdd:cd07207 2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLalGYSA-ADIKDILKET-DFAKLLDSPVGLLFLLPSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 311 MTQG-------AVHEIRH-LQWKLRNLTNNLTFQEAYDITGRILGITVCSLRKHEPPRcLNYLTSPHVVIWSAVTASCAF 382
Cdd:cd07207 80 FKEGglykgdaLEEWLRElLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVV-FSAETTPDMPVAKAVRASMSI 158
|
170
....*....|...
gi 15230231 383 PGLFEAQELMAKD 395
Cdd:cd07207 159 PFVFKPVRLAKGD 171
|
|
| Pat_PNPLA6_PNPLA7_NTE1_like |
cd07205 |
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ... |
231-386 |
8.64e-12 |
|
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: 64.49 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 231 TALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGT-RSWPELQSFFEGSWHALQFFDQM----GGIFT 305
Cdd:cd07205 1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAgYSPEEIEERAKLRSTDLKALSDLtiptAGLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 306 T---VKRVMT-QGAVHeIRHLQWKLRNLTNNLtfqeaydITGRILGITVCSLrkhepprclnyltsphvviWSAVTASCA 381
Cdd:cd07205 81 GdkfLELLDEyFGDRD-IEDLWIPFFIVATDL-------TSGKLVVFRSGSL-------------------VRAVRASMS 133
|
....*
gi 15230231 382 FPGLF 386
Cdd:cd07205 134 IPGIF 138
|
|
| Pat_hypo_Ecoli_Z1214_like |
cd07209 |
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ... |
233-391 |
5.98e-10 |
|
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: 60.00 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVG---TRSWPELQSFfegsWHALQFFDqmggifttvkr 309
Cdd:cd07209 1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAggdPEAVERLEKL----WRELSRED----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 310 VMTQGAVHEIRhlqwklrnltnNLTFQEAYDITGRILGITVCSLRKHEPPRCLNyltSPHVVIWSAVTASCAFPGLFEAQ 389
Cdd:cd07209 66 VFLRGLLDRAL-----------DFDTLRLLAILFAGLVIVAVNVLTGEPVYFDD---IPDGILPEHLLASAALPPFFPPV 131
|
..
gi 15230231 390 EL 391
Cdd:cd07209 132 EI 133
|
|
| Pat_hypo_W_succinogenes_WS1459_like |
cd07210 |
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ... |
231-391 |
5.37e-07 |
|
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: 51.19 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 231 TALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSS----VGSVMCAVVGTRSWPELQSFFEGSWhALQFFDQM--GGIF 304
Cdd:cd07210 1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSagalVGGLFASGISPDEMAELLLSLERKD-FWMFWDPPlrGGLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 305 TtvkrvmtqgavheirhlqwklrnLTNNLTFqeayditgrilgitvcsLRKHEPPRCLNYLTSP-HVVIWS--------- 374
Cdd:cd07210 80 S-----------------------GDRFAAL-----------------LREHLPPDRFEELRIPlAVSVVDltsretlll 119
|
170 180
....*....|....*....|....
gi 15230231 375 -------AVTASCAFPGLFEAQEL 391
Cdd:cd07210 120 segdlaeAVAASCAVPPLFQPVEI 143
|
|
| PRK10279 |
PRK10279 |
patatin-like phospholipase RssA; |
233-386 |
1.11e-06 |
|
patatin-like phospholipase RssA;
Pssm-ID: 182352 [Multi-domain] Cd Length: 300 Bit Score: 51.25 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQ----SFfeGSWHALQFFD---QMGG--- 302
Cdd:PRK10279 8 LALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEdwvtSF--SYWDVLRLMDlswQRGGllr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 303 ---IFTTVKRVMTqgaVHEIRHLQWKLRNLTNNLTfqeaydiTGRILGITVCSLRKhepprclnyltsphvviwsAVTAS 379
Cdd:PRK10279 86 gerVFNQYREIMP---ETEIENCSRRFGAVATNLS-------TGRELWFTEGDLHL-------------------AIRAS 136
|
....*..
gi 15230231 380 CAFPGLF 386
Cdd:PRK10279 137 CSMPGLM 143
|
|
| Pat_NTE_like_bacteria |
cd07228 |
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ... |
232-390 |
5.32e-05 |
|
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: 44.57 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 232 ALLLSGGASLGAFHLGVVKTLVEHKLLPRIIAGSSVGSVMCAVVGTRSWPELQSFF--EGSWHALQFFDqmggifttvKR 309
Cdd:cd07228 2 GLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVrsLSQRDVLRLLD---------LS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230231 310 VMTQGAVHEIRHLQWkLRNLTNNLTFQEAyditGRILGITVCSLRKHEPPrclnYLTSPHVViwSAVTASCAFPGLFEAQ 389
Cdd:cd07228 73 ASRSGLLKGEKVLEY-LREIMGGVTIEEL----PIPFAAVATDLQTGKEV----WFREGSLI--DAIRASISIPGIFAPV 141
|
.
gi 15230231 390 E 390
Cdd:cd07228 142 E 142
|
|
| Patatin_and_cPLA2 |
cd01819 |
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
233-275 |
2.43e-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: 39.32 E-value: 2.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15230231 233 LLLSGGASLGAFHLGVVKTLVEHKLL--PRIIAGSSVGSVMCAVV 275
Cdd:cd01819 1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAATL 45
|
|
| |
