|
Name |
Accession |
Description |
Interval |
E-value |
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
80-347 |
5.09e-84 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 268.31 E-value: 5.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 80 PSGRPSIGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQIDLADIAfdvtera 159
Cdd:COG1752 1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLF------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 160 elpqsrreDERYYINGLTLGFGAkgvkAPAGLVQGNRLQALLADWTAsvptNQPFDRLPIPYRAVATDLQTGQMVVLDHG 239
Cdd:COG1752 74 --------DLSLPRRLLRLDLGL----SPGGLLDGDPLRRLLERLLG----DRDFEDLPIPLAVVATDLETGREVVFDSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 240 SLPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDIGSPLRPLDalaSPADVMQQMVGILIRQ 319
Cdd:COG1752 138 PLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLRKLP---SLLDILGRALEIMFNS 214
|
250 260
....*....|....*....|....*...
gi 895892718 320 NvTSQRKQLHAEDVLLTPDLGTIAFTDF 347
Cdd:COG1752 215 I-LRRELALEPADILIEPDLSGISLLDF 241
|
|
| Pat_PNPLA6_PNPLA7_NTE1_like |
cd07205 |
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ... |
86-292 |
2.43e-62 |
|
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: 207.01 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSqidladiafdvteraelpqsR 165
Cdd:cd07205 1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAK--------------------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 166 REDERYYINGLTLGFgakgvkapAGLVQGNRLQALLADWTASVPtnqpFDRLPIPYRAVATDLQTGQMVVLDHGSLPLAI 245
Cdd:cd07205 61 RSTDLKALSDLTIPT--------AGLLRGDKFLELLDEYFGDRD----IEDLWIPFFIVATDLTSGKLVVFRSGSLVRAV 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 895892718 246 RASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDI 292
Cdd:cd07205 129 RASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRELGADIIIAVDL 175
|
|
| BamA |
COG4775 |
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis]; |
391-801 |
8.09e-55 |
|
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443807 [Multi-domain] Cd Length: 711 Bit Score: 201.47 E-value: 8.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 391 PPIRITSVDIRTNGGVPKRVVNDALHVRPGDLYDPQAVSKDLLALTTSGNFESV---TQQVISEGDENRLVIDAREKYWG 467
Cdd:COG4775 310 PRVYVDRIEIEGNTRTRDEVIRRELRLKEGDPFSREKLERSRRRLYRLGYFESVdveTEPGPSTPDQVDLVVDVKEKPTG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 468 PnfLLFGLGMSSSStdegGFRLHLGYRRPWLTESGLEFRADTTLGSDRQSARVELRQPLSASTGLYVAPYAEYQRRFANV 547
Cdd:COG4775 390 S--LSLGAGYSSDD----GFIGGASLSQRNLLGTGQELSLSLQLGSYSQSYSLSFTEPYFFGSPLSLGVSLFYRRRDASD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 548 YlddiklTQYRLQTERAGVDFGIPIRRLGDFRIGLAYAHGHASPdynvpadfgPNGEPTAFLFDGTNGRQLSARARLLID 627
Cdd:COG4775 464 Y------SSYDLKRTGGGLGLGYPLSEDLRLSLGYGYERTDISD---------VDSSPDYLPDQNGSSNTSSLGLGLTYD 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 628 QLDDPQFPRKGYFGELRVERSF-----------VSSEAQQYTEVFGKamvaqqfgrHSVNASIEAG--KSFGGVSPVNLL 694
Cdd:COG4775 529 TRDNPLFPTRGSYLSLSLEFAGpylggdleyykLSADARYYFPLGKK---------LVLALRAEAGylGGYGKDLPFFER 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 695 dFTLGGFQHLAAYAADQLN----GNALVYGQVTYMNQLMTFNASPVK-ALFVgasaELGNVWSLDSPVSAGPLKQSYSFF 769
Cdd:COG4775 600 -FYLGGFGSLRGYEENSLGprlgGNAYLLGSAELRFPLPLPPSAGLRgALFV----DAGNVWDSGDDFDLSDLRYSAGVG 674
|
410 420 430
....*....|....*....|....*....|....*..
gi 895892718 770 TSLTTSFGPLYVGVALA----PGGR-HNLYFQLGRTY 801
Cdd:COG4775 675 LRWDTPLGPLRLDYAYPldkePGDSgQRFHFSIGTRF 711
|
|
| PRK10279 |
PRK10279 |
patatin-like phospholipase RssA; |
86-311 |
1.64e-34 |
|
patatin-like phospholipase RssA;
Pssm-ID: 182352 [Multi-domain] Cd Length: 300 Bit Score: 133.68 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASgmpaedmqKRLSQIDLADIAF---DVTERAELP 162
Cdd:PRK10279 6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYAC--------DRLSALEDWVTSFsywDVLRLMDLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 163 QSRrederyyingltlgfgakgvkapAGLVQG----NRLQALLadwtasvpTNQPFDRLPIPYRAVATDLQTGQMVVLDH 238
Cdd:PRK10279 78 WQR-----------------------GGLLRGervfNQYREIM--------PETEIENCSRRFGAVATNLSTGRELWFTE 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 895892718 239 GSLPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDigsplrpldaLASPADVMQQ 311
Cdd:PRK10279 127 GDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPVSLTRALGADIVIAVD----------LQHDAHLMQQ 189
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
88-279 |
1.69e-32 |
|
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.
Pssm-ID: 396341 Cd Length: 190 Bit Score: 124.64 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQIDLADIAFDVTERAELPQSRRe 167
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSLLALL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 168 deRYYINGLTLGFGAKGVKAPAGLVQGNRLQALLADWTASVPTNQPFDRLPIPYRAVATDLQTGQMVVLDHGSLPLAIRA 247
Cdd:pfam01734 80 --RGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVLA 157
|
170 180 190
....*....|....*....|....*....|..
gi 895892718 248 SMAMPGLFAPAEINGRALVDGGLVSNLPVDTA 279
Cdd:pfam01734 158 SSALPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
|
|
| OM_YaeT |
TIGR03303 |
outer membrane protein assembly complex, YaeT protein; Members of this protein family are the ... |
419-779 |
3.53e-10 |
|
outer membrane protein assembly complex, YaeT protein; Members of this protein family are the YaeT protein of the YaeT/YfiO complex for assembling proteins into the outer membrane of Gram-negative bacteria. This protein is similar in sequence and function to a non-essential paralog, YtfM, that is also in the Omp85 family. Members of this family typically have five tandem copies of the surface antigen variable number repeat (pfam07244), followed by an outer membrane beta-barrel domain (pfam01103), while the YtfM family typically has a single pfam07244 repeat. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274514 [Multi-domain] Cd Length: 741 Bit Score: 63.75 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 419 PGDLYDPQAVSKDLLALTTSGNFESVTQQVISEGDENR--LVIDAREKYWGPnfLLFGLGMSSSStdegGFRLHLGYRRP 496
Cdd:TIGR03303 348 EGDWYSLSKIKRSKRRLERLGYFETVNIETVPVGSPDQvdLNVKVKEQPTGS--ISFGVGYGSSS----GLSFNASISER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 497 WLTESGLEFRADTTLGSDRQSARVELRQP------LSASTGLYvapYAEYQRRFANVYLddikltqYRLQTERAGVDFGI 570
Cdd:TIGR03303 422 NFLGTGNRLSLSANKSSLSTSYSLSFTDPyftddgVSLGFSIF---YSETDRNYKNFSD-------YKTKTYGGSINLGY 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 571 PIRRLGDFRIGLAYAHGHASPDYNVPADFGP-----NGEPTAFLFDgtngrqlsarARLLIDQLDDPQFPRKGYFGELRV 645
Cdd:TIGR03303 492 PITEYLRVSLGYGYEQNKIKDDSDSDSSASYfikeqGGKFIDSSLS----------YGWSYDTLDSGYFPTKGSIQRLSQ 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 646 ERSFVSSEAQQYTEVFgKAMVAQQFGRH-----SVNASIEAGKSFGGvSPVNLLD-FTLGGFQHLAAYAA------DQLN 713
Cdd:TIGR03303 562 EFAGPGGDLKYYKLTY-DSEYYIPLSKEddwvlSLRGRLGYGNGYGG-KDLPFYErFYAGGIGSVRGFESngigprDIND 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 714 GNALVYGqvtymNQLMTFNA---SPVK----------ALFVgasaELGNVWSLDSPVSAGPLKQS---YSFFTSLT--TS 775
Cdd:TIGR03303 640 SGDSIGG-----NAMATANVeliFPLPflpednglrgSVFF----DAGNVWGTDQKKEGDYSDDSslrASVGVGLRwiSP 710
|
....
gi 895892718 776 FGPL 779
Cdd:TIGR03303 711 MGPL 714
|
|
| Omp85 |
pfam01103 |
Omp85 superfamily domain; The Omp85 protein superfamily contains bacterial outer membrane ... |
501-779 |
3.86e-07 |
|
Omp85 superfamily domain; The Omp85 protein superfamily contains bacterial outer membrane proteins, which can function as protein translocases or as membrane protein assembly factors. The family includes the membrane bound beta barrel of proteins such as BamA and TamA from E. coli.
Pssm-ID: 460065 [Multi-domain] Cd Length: 319 Bit Score: 52.74 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 501 SGLEFRADTTLGSDRQSARVE------LRQPLSASTGLYvapyaeYQRRFANVYLDDikltQYRLQTERAGVDFGIPIRR 574
Cdd:pfam01103 5 RGQSLSVNASRGSYETSFSLSftdpyfLGDGVSLGGSLF------YNSYDSDRDSSD----SYRITTYGFSVSLGRPITE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 575 LGDFRIGLAYAHGHASPDYNVPADFgpngepTAFLFDGTNGRQLSARAR--LLIDQLDDPQFPRKGYFGELRVE------ 646
Cdd:pfam01103 75 NWSLSLGLGYQHNKILDESGSPNIR------NYYPSASGTGKSLTFSLSygWTYDTRDDGLFPTRGSYLKFNLEftgpfl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 647 ---RSFVSS--EAQQYTEVFGKAMVaqqfgrhSVNASIEAGKSFG-GVSPVNLLD-FTLGGFQHLAAYA----------A 709
Cdd:pfam01103 149 ggdVSYYKLtaDGSYYYPLGKDDSF-------VLSARVALGYLDGyGTKDLPFYErFYAGGSNSVRGFEyggigprdedG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 895892718 710 DQLNGNALVYGQVTYMNQLMTFNASPVK-ALFVGAsaelGNVWSLDSPVSAGP--------LKQSYSFFTSLTTSFGPL 779
Cdd:pfam01103 222 DALGGNSYVVASLELRFPLPFVPKQSVRgVLFFDA----GNVWNTGSTDPGSSrgarskagIRASVGVGLRWLSPLGPL 296
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
80-347 |
5.09e-84 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 268.31 E-value: 5.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 80 PSGRPSIGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQIDLADIAfdvtera 159
Cdd:COG1752 1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLF------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 160 elpqsrreDERYYINGLTLGFGAkgvkAPAGLVQGNRLQALLADWTAsvptNQPFDRLPIPYRAVATDLQTGQMVVLDHG 239
Cdd:COG1752 74 --------DLSLPRRLLRLDLGL----SPGGLLDGDPLRRLLERLLG----DRDFEDLPIPLAVVATDLETGREVVFDSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 240 SLPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDIGSPLRPLDalaSPADVMQQMVGILIRQ 319
Cdd:COG1752 138 PLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLRKLP---SLLDILGRALEIMFNS 214
|
250 260
....*....|....*....|....*...
gi 895892718 320 NvTSQRKQLHAEDVLLTPDLGTIAFTDF 347
Cdd:COG1752 215 I-LRRELALEPADILIEPDLSGISLLDF 241
|
|
| Pat_PNPLA6_PNPLA7_NTE1_like |
cd07205 |
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ... |
86-292 |
2.43e-62 |
|
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: 207.01 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSqidladiafdvteraelpqsR 165
Cdd:cd07205 1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAK--------------------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 166 REDERYYINGLTLGFgakgvkapAGLVQGNRLQALLADWTASVPtnqpFDRLPIPYRAVATDLQTGQMVVLDHGSLPLAI 245
Cdd:cd07205 61 RSTDLKALSDLTIPT--------AGLLRGDKFLELLDEYFGDRD----IEDLWIPFFIVATDLTSGKLVVFRSGSLVRAV 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 895892718 246 RASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDI 292
Cdd:cd07205 129 RASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRELGADIIIAVDL 175
|
|
| Pat_NTE_like_bacteria |
cd07228 |
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ... |
86-292 |
2.63e-58 |
|
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: 196.34 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQK--RLSQID---LADIAFdvterae 160
Cdd:cd07228 1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWvrSLSQRDvlrLLDLSA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 161 lpqSRrederyyingltlgfgakgvkapAGLVQGNRLQALLADWTASVPtnqpFDRLPIPYRAVATDLQTGQMVVLDHGS 240
Cdd:cd07228 74 ---SR-----------------------SGLLKGEKVLEYLREIMGGVT----IEELPIPFAAVATDLQTGKEVWFREGS 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 895892718 241 LPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDI 292
Cdd:cd07228 124 LIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVSVARALGADIVIAVDL 175
|
|
| BamA |
COG4775 |
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis]; |
391-801 |
8.09e-55 |
|
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443807 [Multi-domain] Cd Length: 711 Bit Score: 201.47 E-value: 8.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 391 PPIRITSVDIRTNGGVPKRVVNDALHVRPGDLYDPQAVSKDLLALTTSGNFESV---TQQVISEGDENRLVIDAREKYWG 467
Cdd:COG4775 310 PRVYVDRIEIEGNTRTRDEVIRRELRLKEGDPFSREKLERSRRRLYRLGYFESVdveTEPGPSTPDQVDLVVDVKEKPTG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 468 PnfLLFGLGMSSSStdegGFRLHLGYRRPWLTESGLEFRADTTLGSDRQSARVELRQPLSASTGLYVAPYAEYQRRFANV 547
Cdd:COG4775 390 S--LSLGAGYSSDD----GFIGGASLSQRNLLGTGQELSLSLQLGSYSQSYSLSFTEPYFFGSPLSLGVSLFYRRRDASD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 548 YlddiklTQYRLQTERAGVDFGIPIRRLGDFRIGLAYAHGHASPdynvpadfgPNGEPTAFLFDGTNGRQLSARARLLID 627
Cdd:COG4775 464 Y------SSYDLKRTGGGLGLGYPLSEDLRLSLGYGYERTDISD---------VDSSPDYLPDQNGSSNTSSLGLGLTYD 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 628 QLDDPQFPRKGYFGELRVERSF-----------VSSEAQQYTEVFGKamvaqqfgrHSVNASIEAG--KSFGGVSPVNLL 694
Cdd:COG4775 529 TRDNPLFPTRGSYLSLSLEFAGpylggdleyykLSADARYYFPLGKK---------LVLALRAEAGylGGYGKDLPFFER 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 695 dFTLGGFQHLAAYAADQLN----GNALVYGQVTYMNQLMTFNASPVK-ALFVgasaELGNVWSLDSPVSAGPLKQSYSFF 769
Cdd:COG4775 600 -FYLGGFGSLRGYEENSLGprlgGNAYLLGSAELRFPLPLPPSAGLRgALFV----DAGNVWDSGDDFDLSDLRYSAGVG 674
|
410 420 430
....*....|....*....|....*....|....*..
gi 895892718 770 TSLTTSFGPLYVGVALA----PGGR-HNLYFQLGRTY 801
Cdd:COG4775 675 LRWDTPLGPLRLDYAYPldkePGDSgQRFHFSIGTRF 711
|
|
| PRK10279 |
PRK10279 |
patatin-like phospholipase RssA; |
86-311 |
1.64e-34 |
|
patatin-like phospholipase RssA;
Pssm-ID: 182352 [Multi-domain] Cd Length: 300 Bit Score: 133.68 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASgmpaedmqKRLSQIDLADIAF---DVTERAELP 162
Cdd:PRK10279 6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYAC--------DRLSALEDWVTSFsywDVLRLMDLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 163 QSRrederyyingltlgfgakgvkapAGLVQG----NRLQALLadwtasvpTNQPFDRLPIPYRAVATDLQTGQMVVLDH 238
Cdd:PRK10279 78 WQR-----------------------GGLLRGervfNQYREIM--------PETEIENCSRRFGAVATNLSTGRELWFTE 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 895892718 239 GSLPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDigsplrpldaLASPADVMQQ 311
Cdd:PRK10279 127 GDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPVSLTRALGADIVIAVD----------LQHDAHLMQQ 189
|
|
| Pat_PNPLA6_PNPLA7 |
cd07225 |
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ... |
85-294 |
2.03e-34 |
|
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: 133.68 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 85 SIGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQI--DLADIAFDVTeraelp 162
Cdd:cd07225 15 SIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWakDMTSIWKKLL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 163 qsrreDERYYInglTLGFGAKGVKAPAGLVQGNRLqalladwtasvptnqpFDRLPIPYRAVATDLQTGQMVVLDHGSLP 242
Cdd:cd07225 89 -----DLTYPI---TSMFSGAAFNRSIHSIFGDKQ----------------IEDLWLPYFTITTDITASAMRVHTDGSLW 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 895892718 243 LAIRASMA----MPGLFAPAEinGRALVDGGLVSNLPVDTARRMGADVVIAVDIGS 294
Cdd:cd07225 145 RYVRASMSlsgyLPPLCDPKD--GHLLMDGGYINNLPADVARSMGAKTVIAIDVGS 198
|
|
| Pat_hypo_W_succinogenes_WS1459_like |
cd07210 |
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ... |
86-280 |
8.69e-34 |
|
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: 129.39 E-value: 8.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQIDLADIafdvteraelpqsr 165
Cdd:cd07210 1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELLLSLERKDF-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 166 rederyyingltlgFGAKGVKAPAGLVQGNRLQALLADwtaSVPTnQPFDRLPIPYRAVATDLQTGQMVVLDHGSLPLAI 245
Cdd:cd07210 67 --------------WMFWDPPLRGGLLSGDRFAALLRE---HLPP-DRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAV 128
|
170 180 190
....*....|....*....|....*....|....*
gi 895892718 246 RASMAMPGLFAPAEINGRALVDGGLVSNLPVDTAR 280
Cdd:cd07210 129 AASCAVPPLFQPVEIGGRPFVDGGVADRLPFDALR 163
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
88-279 |
1.69e-32 |
|
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.
Pssm-ID: 396341 Cd Length: 190 Bit Score: 124.64 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQIDLADIAFDVTERAELPQSRRe 167
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSLLALL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 168 deRYYINGLTLGFGAKGVKAPAGLVQGNRLQALLADWTASVPTNQPFDRLPIPYRAVATDLQTGQMVVLDHGSLPLAIRA 247
Cdd:pfam01734 80 --RGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVLA 157
|
170 180 190
....*....|....*....|....*....|..
gi 895892718 248 SMAMPGLFAPAEINGRALVDGGLVSNLPVDTA 279
Cdd:pfam01734 158 SSALPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
|
|
| Pat_ExoU_VipD_like |
cd07207 |
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ... |
88-278 |
4.01e-32 |
|
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: 123.54 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQIDLADIAFDVTeraelpqsrre 167
Cdd:cd07207 2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKETDFAKLLDSPV----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 168 deryyinglTLGFGAKGVKAPAGLVQGNRLQAL----LADWT----ASVPTNQPFDRLPIPYRAVATDLQTGQMVVLDHG 239
Cdd:cd07207 71 ---------GLLFLLPSLFKEGGLYKGDALEEWlrelLKEKTgnsfATSLLRDLDDDLGKDLKVVATDLTTGALVVFSAE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 895892718 240 SLP-----LAIRASMAMPGLFAPAEI-NGRALVDGGLVSNLPVDT 278
Cdd:cd07207 142 TTPdmpvaKAVRASMSIPFVFKPVRLaKGDVYVDGGVLDNYPVWL 186
|
|
| Pat_hypo_Ecoli_Z1214_like |
cd07209 |
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ... |
88-308 |
1.13e-29 |
|
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: 117.01 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMP--AEDMQKRLSQIDLADIafdvteraelpqsr 165
Cdd:cd07209 1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPeaVERLEKLWRELSREDV-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 166 rederyyingltlgfgakgvkapagLVQGNRLQALLADWTASVPTnqPFDRLPIpyraVATDLQTGQMVVLD---HGSLP 242
Cdd:cd07209 67 -------------------------FLRGLLDRALDFDTLRLLAI--LFAGLVI----VAVNVLTGEPVYFDdipDGILP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 895892718 243 LAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDIGSPLRPLDALASPADV 308
Cdd:cd07209 116 EHLLASAALPPFFPPVEIDGRYYWDGGVVDNTPLSPAIDLGADEIIVVSLSDKGRDDRKGTPPTTL 181
|
|
| Pat_Fungal_NTE1 |
cd07227 |
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ... |
85-294 |
3.67e-28 |
|
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: 114.51 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 85 SIGLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEDMQKRLSQI-----DLADIAFDVTera 159
Cdd:cd07227 10 AIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFagrmaSMWRFLSDVT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 160 eLPQSRREDERYYINGLTLGFGakgvkapaglvqgnrlqalladwtasvptNQPFDRLPIPYRAVATDLQTGQMVVLDHG 239
Cdd:cd07227 87 -YPFASYTTGHEFNRGIWKTFG-----------------------------NTHIEDFWIPFYANSTNITHSRMEIHSSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 895892718 240 SLPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAVDIGS 294
Cdd:cd07227 137 YAWRYIRASMSLAGLLPPLSDNGSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGS 191
|
|
| Patatin |
cd07198 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
88-290 |
5.49e-27 |
|
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: 108.20 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAEdmqkrlsqidLADIAFDVTERAELpqsRRE 167
Cdd:cd07198 1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLE----------EALLLLLRLSREVR---LRF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 168 DERYYINGLTLGFGAKgvkapaGLVQGNRLQALLADWtasvptnqpfdrlpIPYRAVATDLQTGQMVVLDH---GSLPLA 244
Cdd:cd07198 68 DGAFPPTGRLLGILRQ------PLLSALPDDAHEDAS--------------GKLFISLTRLTDGENVLVSDtskGELWSA 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 895892718 245 IRASMAMPGLFAP--AEINGRALVDGGLVSNLPVDtarRMGADVVIAV 290
Cdd:cd07198 128 VRASSSIPGYFGPvpLSFRGRRYGDGGLSNNLPVA---ELGNTINVSP 172
|
|
| YjjU |
COG4667 |
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; |
86-290 |
1.05e-21 |
|
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
Pssm-ID: 443704 [Multi-domain] Cd Length: 281 Bit Score: 96.00 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 86 IGLALSGGGARG-YAHlGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPaeDMQKRLsqidLADIAFDvteraelpqs 164
Cdd:COG4667 6 TALVLEGGGMRGiFTA-GVLDALLEEGIPFDLVIGVSAGALNGASYLSRQP--GRARRV----ITDYATD---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 165 rredeRYYINgltlgfgakgvkaPAGLVQGNRLqaLLADWT-ASVPTNQ-PFD-----RLPIPYRAVATDLQTGQMVVL- 236
Cdd:COG4667 69 -----PRFFS-------------LRNFLRGGNL--FDLDFLyDEIPNELlPFDfetfkASPREFYVVATNADTGEAEYFs 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 895892718 237 ---DHGSLPLAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGADVVIAV 290
Cdd:COG4667 129 kkdDDYDLLDALRASSALPLLYPPVEIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
|
|
| Pat_hypo_Ecoli_yjju_like |
cd07208 |
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ... |
88-288 |
3.93e-19 |
|
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: 88.05 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARG-YAhLGVLKVLEDNRI-PIDCIAGTSMGAVVGGLYASGMpaedmQKRlsqidladiAFDVTERAELpqsr 165
Cdd:cd07208 1 LVLEGGGMRGaYT-AGVLDAFLEAGIrPFDLVIGVSAGALNAASYLSGQ-----RGR---------ALRINTKYAT---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 166 reDERYyingltlgFGAKGVKAPAGLVQGNRLQALLADwtasvpTNQPFD-----RLPIPYRAVATDLQTGQMVVLDHGS 240
Cdd:cd07208 62 --DPRY--------LGLRSLLRTGNLFDLDFLYDELPD------GLDPFDfeafaASPARFYVVATDADTGEAVYFDKPD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 895892718 241 LP----LAIRASMAMPGLFAPAEINGRALVDGGLVSNLPVDTARRMGAD--VVI 288
Cdd:cd07208 126 ILddllDALRASSALPGLFPPVRIDGEPYVDGGLSDSIPVDKAIEDGADkiVVI 179
|
|
| TamA |
COG0729 |
Outer membrane translocation and assembly module TamA [Cell wall/membrane/envelope biogenesis]; ... |
391-798 |
5.84e-17 |
|
Outer membrane translocation and assembly module TamA [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440493 [Multi-domain] Cd Length: 574 Bit Score: 84.95 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 391 PPIRITSVDIRTNGGVPKRVVNDALHVRPGDLYDPQAVSKDLLALTTSGNFESVTQQVISEGDENR---LVIDAREKywG 467
Cdd:COG0729 185 PRYRFGEITVEGLSRVPEDFLRRLAPFKPGEPYSPDKLLELQQRLQSTGYFSSVRVTPDEDPAPDGtvpVTVTLTER--K 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 468 PNFLLFGLGMSsssTDEGgFRLHLGYRRPWLTESGLEFRADTTLGSDRQSARVELRQPLSASTGlyvapyaeyQRRFANV 547
Cdd:COG0729 263 RRRIGFGLGYS---TDTG-PRLSAGWEHRNLFGRGHRLRLELELSQPEQSLSADYRIPPLFPLG---------QYLSLGA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 548 YLDDIKLTQYRLQTERAGVDFGIPIRRLGDFRIGLAYAHGHASpdynvpadfgpNGEPTaflfdgTNGRQLSARARLLID 627
Cdd:COG0729 330 GLEREDTDDYDSRSLTLGAGRTRRLSDGWTRSLGLRLLYERFT-----------DGDDD------RTYTLLSPGLSWTRD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 628 QLDDPQFPRKGYF--GELRVERSFVSSEAqQYTEVFGKAMVAQQFG-RHSVNASIEAG----KSFGGVsPVNLLdFTLGG 700
Cdd:COG0729 393 RRDDPLDPTRGYRlsLELGPGSKLLGSDT-SFLRLYARGSWYRPLGeRHRLAGRAELGailgADFDDV-PPSLR-FFAGG 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 701 --------FQHLAAYAADQ--LNGNALVYGQVTYmNQLMTFNaspvkaLFVGASAELGNVWsldSPVSAGPLKQSYSFFT 770
Cdd:COG0729 470 dgsvrgygYQSLGPRDGDGdvIGGRSLAVGSLEY-RYRVTEN------WGLAVFVDAGNAF---NDFPFSDLKVGAGLGL 539
|
410 420 430
....*....|....*....|....*....|..
gi 895892718 771 SLTTSFGP--LYVGVALAPGGRHN--LYFQLG 798
Cdd:COG0729 540 RWYSPVGPirLDLAYPLNDRDDSSfrLYISLG 571
|
|
| OM_YaeT |
TIGR03303 |
outer membrane protein assembly complex, YaeT protein; Members of this protein family are the ... |
419-779 |
3.53e-10 |
|
outer membrane protein assembly complex, YaeT protein; Members of this protein family are the YaeT protein of the YaeT/YfiO complex for assembling proteins into the outer membrane of Gram-negative bacteria. This protein is similar in sequence and function to a non-essential paralog, YtfM, that is also in the Omp85 family. Members of this family typically have five tandem copies of the surface antigen variable number repeat (pfam07244), followed by an outer membrane beta-barrel domain (pfam01103), while the YtfM family typically has a single pfam07244 repeat. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274514 [Multi-domain] Cd Length: 741 Bit Score: 63.75 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 419 PGDLYDPQAVSKDLLALTTSGNFESVTQQVISEGDENR--LVIDAREKYWGPnfLLFGLGMSSSStdegGFRLHLGYRRP 496
Cdd:TIGR03303 348 EGDWYSLSKIKRSKRRLERLGYFETVNIETVPVGSPDQvdLNVKVKEQPTGS--ISFGVGYGSSS----GLSFNASISER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 497 WLTESGLEFRADTTLGSDRQSARVELRQP------LSASTGLYvapYAEYQRRFANVYLddikltqYRLQTERAGVDFGI 570
Cdd:TIGR03303 422 NFLGTGNRLSLSANKSSLSTSYSLSFTDPyftddgVSLGFSIF---YSETDRNYKNFSD-------YKTKTYGGSINLGY 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 571 PIRRLGDFRIGLAYAHGHASPDYNVPADFGP-----NGEPTAFLFDgtngrqlsarARLLIDQLDDPQFPRKGYFGELRV 645
Cdd:TIGR03303 492 PITEYLRVSLGYGYEQNKIKDDSDSDSSASYfikeqGGKFIDSSLS----------YGWSYDTLDSGYFPTKGSIQRLSQ 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 646 ERSFVSSEAQQYTEVFgKAMVAQQFGRH-----SVNASIEAGKSFGGvSPVNLLD-FTLGGFQHLAAYAA------DQLN 713
Cdd:TIGR03303 562 EFAGPGGDLKYYKLTY-DSEYYIPLSKEddwvlSLRGRLGYGNGYGG-KDLPFYErFYAGGIGSVRGFESngigprDIND 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 714 GNALVYGqvtymNQLMTFNA---SPVK----------ALFVgasaELGNVWSLDSPVSAGPLKQS---YSFFTSLT--TS 775
Cdd:TIGR03303 640 SGDSIGG-----NAMATANVeliFPLPflpednglrgSVFF----DAGNVWGTDQKKEGDYSDDSslrASVGVGLRwiSP 710
|
....
gi 895892718 776 FGPL 779
Cdd:TIGR03303 711 MGPL 714
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
88-281 |
3.59e-09 |
|
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: 58.50 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLED---NRIPI----DCIAGTSmgavVGGLYASGMpaedMQKRLSQIDLADIafdvterae 160
Cdd:cd07199 2 LSLDGGGIRGIIPAEILAELEKrlgKPSRIadlfDLIAGTS----TGGIIALGL----ALGRYSAEELVEL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 161 lpqsrrederyyingltlgFGAKGvkapaglvqgnrlqalladwtasvptNQPFDRLPIPyravATDLQTGQMVVL---- 236
Cdd:cd07199 65 -------------------YEELG--------------------------RKIFPRVLVT----AYDLSTGKPVVFsnyd 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 895892718 237 -----DHGSLPL--AIRASMAMPGLFAPAEI----NGRALVDGGLVSNLPVDTARR 281
Cdd:cd07199 96 aeepdDDDDFKLwdVARATSAAPTYFPPAVIesggDEGAFVDGGVAANNPALLALA 151
|
|
| Pat_PLPL |
cd07232 |
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ... |
87-137 |
1.05e-07 |
|
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: 54.96 E-value: 1.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 895892718 87 GLALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAE 137
Cdd:cd07232 69 ALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLCTRTDEE 119
|
|
| Omp85 |
pfam01103 |
Omp85 superfamily domain; The Omp85 protein superfamily contains bacterial outer membrane ... |
501-779 |
3.86e-07 |
|
Omp85 superfamily domain; The Omp85 protein superfamily contains bacterial outer membrane proteins, which can function as protein translocases or as membrane protein assembly factors. The family includes the membrane bound beta barrel of proteins such as BamA and TamA from E. coli.
Pssm-ID: 460065 [Multi-domain] Cd Length: 319 Bit Score: 52.74 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 501 SGLEFRADTTLGSDRQSARVE------LRQPLSASTGLYvapyaeYQRRFANVYLDDikltQYRLQTERAGVDFGIPIRR 574
Cdd:pfam01103 5 RGQSLSVNASRGSYETSFSLSftdpyfLGDGVSLGGSLF------YNSYDSDRDSSD----SYRITTYGFSVSLGRPITE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 575 LGDFRIGLAYAHGHASPDYNVPADFgpngepTAFLFDGTNGRQLSARAR--LLIDQLDDPQFPRKGYFGELRVE------ 646
Cdd:pfam01103 75 NWSLSLGLGYQHNKILDESGSPNIR------NYYPSASGTGKSLTFSLSygWTYDTRDDGLFPTRGSYLKFNLEftgpfl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 647 ---RSFVSS--EAQQYTEVFGKAMVaqqfgrhSVNASIEAGKSFG-GVSPVNLLD-FTLGGFQHLAAYA----------A 709
Cdd:pfam01103 149 ggdVSYYKLtaDGSYYYPLGKDDSF-------VLSARVALGYLDGyGTKDLPFYErFYAGGSNSVRGFEyggigprdedG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 895892718 710 DQLNGNALVYGQVTYMNQLMTFNASPVK-ALFVGAsaelGNVWSLDSPVSAGP--------LKQSYSFFTSLTTSFGPL 779
Cdd:pfam01103 222 DALGGNSYVVASLELRFPLPFVPKQSVRgVLFFDA----GNVWNTGSTDPGSSrgarskagIRASVGVGLRWLSPLGPL 296
|
|
| Omp85_2 |
pfam19143 |
OMP85 superfamily; This entry represents the membrane spanning beta barrel domain of various ... |
599-701 |
1.12e-06 |
|
OMP85 superfamily; This entry represents the membrane spanning beta barrel domain of various Omp85 superfamily related proteins that have often have POTRA and Patatin domains. This family contains mainly flavobacterial proteins.
Pssm-ID: 465981 Cd Length: 351 Bit Score: 51.31 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 599 FGPNGEPTAFLFDGTNgrQLSARARLLIDQLDDPQFPRKGYF--GELRVerSFVSSEaqqYTEVF-------GKAMVAQQ 669
Cdd:pfam19143 142 LGENNNPEETVFENSN--YFSAFGYLKLDTYDNKYFPTKGFYfdGDFHW--YLFSSD---YNNDFeefsiakADIGYAFT 214
|
90 100 110
....*....|....*....|....*....|...
gi 895892718 670 FGRH-SVNASIEAGKSFGGvSPVNLLDFTLGGF 701
Cdd:pfam19143 215 FFDKlSFNLETEGGFKIGN-SSVPSFDFVLGGY 246
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
88-299 |
4.68e-06 |
|
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 subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
Pssm-ID: 132856 [Multi-domain] Cd Length: 344 Bit Score: 49.41 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 88 LALSGGGARGYAHLGVLKVLED-----NRIP-------IDCIAGTSMGAVVGGLYASGMPAEDMqKRLSQIDLADIaFDV 155
Cdd:cd07217 4 LALDGGGIRGLLSVEILGRIEKdlrthLDDPefrlgdyFDFVGGTSTGSIIAACIALGMSVTDL-LSFYTLNGVNM-FDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 156 TERAELPQSRREDERYYINGLTLGFGAKGVKAPAGlvqGNRLQALLADWTASVPTNQP--FDRLPIPY------RAVATD 227
Cdd:cd07217 82 AWLAQRLFLNKLYNQYDPTNLGKKLNTVFPETTLG---DDTLRTLLMIVTRNATTGSPwpVCNNPEAKyndsdrSDCNLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 228 LQTGQMVvldhgslplaiRASMAMPGLFAP-----AEINGRALVDGGLVS-NLP------VDTAR------RMGADVVIA 289
Cdd:cd07217 159 LPLWQLV-----------RASTAAPTFFPPevvsiAPGTAFVFVDGGVTTyNNPafqaflMATAKpyklnwEVGADNLLL 227
|
250
....*....|
gi 895892718 290 VDIGSPLRPL 299
Cdd:cd07217 228 VSVGTGFAPE 237
|
|
| Pat_TGL3-4-5_SDP1 |
cd07206 |
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ... |
82-132 |
2.27e-05 |
|
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: 47.21 E-value: 2.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 895892718 82 GRPSigLALSGGGARGYAHLGVLKVL-EDNRIPiDCIAGTSMGAVVGGLYAS 132
Cdd:cd07206 68 GRTA--LMLSGGASLGLFHLGVVKALwEQDLLP-RVISGSSAGAIVAALLGT 116
|
|
| Patatin_and_cPLA2 |
cd01819 |
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
88-132 |
5.91e-05 |
|
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.
Pssm-ID: 132836 [Multi-domain] Cd Length: 155 Bit Score: 43.94 E-value: 5.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 895892718 88 LALSGGGARGYAHLGVLKVLeDNRIPIDC---IAGTSMGAVVGGLYAS 132
Cdd:cd01819 1 LSFSGGGFRGMYHAGVLSAL-AERGLLDCvtyLAGTSGGAWVAATLYP 47
|
|
| POTRA |
pfam07244 |
Surface antigen variable number repeat; This family is found primarily in bacterial surface ... |
394-464 |
3.26e-04 |
|
Surface antigen variable number repeat; This family is found primarily in bacterial surface antigens, normally as variable number repeats at the N-terminus. The C-terminus of these proteins is normally represented by pfam01103. The alignment centres on a -GY- or -GF- motif. Some members of this family are found in the mitochondria. It is predicted to have a mixed alpha/beta secondary structure.
Pssm-ID: 462121 [Multi-domain] Cd Length: 78 Bit Score: 40.02 E-value: 3.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 895892718 394 RITSVDIRTNGGVPKRVVNDALHVRPGDLYDPQAVSKDLLALTT----SGNFE-SVTQQVISEGDENR--LVIDAREK 464
Cdd:pfam07244 1 KIGDINFEGNKKTKDEELRRLLGLKEGDVYNREKLEEDKEALKDrygrLGYFDaSVSTNVEIDDEVNTvdLTFNVDEG 78
|
|
| Pat_SDP1-like |
cd07231 |
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ... |
88-158 |
3.72e-04 |
|
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: 43.59 E-value: 3.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 895892718 88 LALSGGGARGYAHLGVLKVLEDNRIPIDCIAGTSMGAVVGGLYASGMPAE--DMQKRLsqidLADI----AFDVTER 158
Cdd:cd07231 71 LLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEElqSFFRAL----LGDLtfqeAYDRTGR 143
|
|
| BamA |
COG4775 |
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis]; |
395-464 |
3.87e-04 |
|
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443807 [Multi-domain] Cd Length: 711 Bit Score: 43.93 E-value: 3.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 395 ITSVDIRTNGGVPKRVVNDALHVRPGDLYDPQAVSKDLLALTTSGNFESVtqQVISEGdeNRLVIDAREK 464
Cdd:COG4775 1 IKDIRVEGLQRVEAGTVLSYLPLRVGDTFDDEKLDEAIKALYATGLFSDV--RIEREG--VVLVVKVKER 66
|
|
| OM_YaeT |
TIGR03303 |
outer membrane protein assembly complex, YaeT protein; Members of this protein family are the ... |
399-464 |
1.04e-03 |
|
outer membrane protein assembly complex, YaeT protein; Members of this protein family are the YaeT protein of the YaeT/YfiO complex for assembling proteins into the outer membrane of Gram-negative bacteria. This protein is similar in sequence and function to a non-essential paralog, YtfM, that is also in the Omp85 family. Members of this family typically have five tandem copies of the surface antigen variable number repeat (pfam07244), followed by an outer membrane beta-barrel domain (pfam01103), while the YtfM family typically has a single pfam07244 repeat. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274514 [Multi-domain] Cd Length: 741 Bit Score: 42.57 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895892718 399 DIRTNGGvpKRVVNDA----LHVRPGDLYDPQAVSKDLLALTTSGNFESVtqQVISEGdeNRLVIDAREK 464
Cdd:TIGR03303 5 DIRVEGL--QRVSEGTvlnyLPVKVGDTISDEKIDEAIKALYATGYFEDV--KIEREG--GVLVIKVKER 68
|
|
| Pat_TGL4-5_like |
cd07230 |
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ... |
83-126 |
6.73e-03 |
|
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.
Pssm-ID: 132868 Cd Length: 421 Bit Score: 39.51 E-value: 6.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 895892718 83 RPSIG---LALSGGGARGYAHLGVLKVL-EDNRIP-IdcIAGTSMGAVV 126
Cdd:cd07230 68 RKNFGrtaLLLSGGGTFGMFHIGVLKALfEANLLPrI--ISGSSAGSIV 114
|
|
|