|
Name |
Accession |
Description |
Interval |
E-value |
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
29-203 |
7.47e-87 |
|
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.
Pssm-ID: 238860 [Multi-domain] Cd Length: 177 Bit Score: 253.97 E-value: 7.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 29 NLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKGLDVTIANAGVSGDTTTAGLARVDWSVPD-GTDGVILELGANDALRGI 107
Cdd:cd01822 2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGIDVTVINAGVSGDTTAGGLARLPALLAQhKPDLVILELGGNDGLRGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 108 PPEESEKNLDQMITRLKARGIAVLLAGIIAPPNMGADYAARFNPIYQKLSEKHKLPLYAFFLDGVALEAGLKLEDGMHPN 187
Cdd:cd01822 82 PPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHPN 161
|
170
....*....|....*.
gi 1672690050 188 AKGVDVMVEKMEPAVT 203
Cdd:cd01822 162 AEGQPIIAENVWPALE 177
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
21-202 |
5.91e-46 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 150.56 E-value: 5.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 21 TAANARTINLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKglDVTIANAGVSGDTTTAGLARVDWSVPDG-TDGVILELG 99
Cdd:COG2755 2 KAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAA--DVRVVNAGISGATTADLLARLDRDLLALkPDLVVIELG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 100 ANDALRGI--PPEESEKNLDQMITRLKARG--IAVLLAGI--IAPPNMGADYAARFNPIYQKLSEKHKLPLYAFF--LDG 171
Cdd:COG2755 80 TNDLLRGLgvSPEEFRANLEALIDRLRAAGpgARVVLVTPppRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYaaLRD 159
|
170 180 190
....*....|....*....|....*....|.
gi 1672690050 172 VALEAGLKLEDGMHPNAKGVDVMVEKMEPAV 202
Cdd:COG2755 160 AGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
|
|
| PRK10528 |
PRK10528 |
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional |
18-204 |
3.98e-38 |
|
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
Pssm-ID: 182521 Cd Length: 191 Bit Score: 130.65 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 18 ILATAANARTINLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKGldvTIANAGVSGDTTTAGLARV---------DWsvp 88
Cdd:PRK10528 1 VLLTFRAAAADTLLILGDSLSAGYRMPASAAWPALLNDKWQSKT---SVVNASISGDTSQQGLARLpallkqhqpRW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 89 dgtdgVILELGANDALRGIPPEESEKNLDQMITRLKARGIAVLLAGIIAPPNMGADYAARFNPIYQKLSEKHKLPLYAFF 168
Cdd:PRK10528 75 -----VLVELGGNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1672690050 169 LDGVALEAGLKLEDGMHPNAKG----VDVMVEKMEPAVTN 204
Cdd:PRK10528 150 MEEVYLKPQWMQDDGIHPNRDAqpfiADWMAKQLQPLVNH 189
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
33-190 |
4.16e-27 |
|
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.
Pssm-ID: 463889 Cd Length: 176 Bit Score: 101.85 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 33 FGDSLMAGYQLPLGD-GFPEKLQAALKAKGLDVTIANAGVSGDTTTAGLA-RVDWSVPDGTDGVILELGANDALRGIPPE 110
Cdd:pfam13472 2 LGDSITAGYGATGGDrSYPGWLARLLARRLGADVVNNLGISGATTRLDLLeRLDDVLRLKPDLVVILLGTNDLGRGVSAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 111 ESEKNLDQMITRLKARG--IAVLLAGIIAP-------PNMGADYAARFNPIYQKLSEKHKLP---LYAFFLDGVALEAGL 178
Cdd:pfam13472 82 RAAANLEALIDALRAAGpdARVLLIGPLPVgppppldERRLNARIAEYNAAIREVAAERGVPyvdLWDALRDDGGWLPDL 161
|
170
....*....|..
gi 1672690050 179 KLEDGMHPNAKG 190
Cdd:pfam13472 162 LADDGLHPNAAG 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
29-203 |
7.47e-87 |
|
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.
Pssm-ID: 238860 [Multi-domain] Cd Length: 177 Bit Score: 253.97 E-value: 7.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 29 NLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKGLDVTIANAGVSGDTTTAGLARVDWSVPD-GTDGVILELGANDALRGI 107
Cdd:cd01822 2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGIDVTVINAGVSGDTTAGGLARLPALLAQhKPDLVILELGGNDGLRGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 108 PPEESEKNLDQMITRLKARGIAVLLAGIIAPPNMGADYAARFNPIYQKLSEKHKLPLYAFFLDGVALEAGLKLEDGMHPN 187
Cdd:cd01822 82 PPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHPN 161
|
170
....*....|....*.
gi 1672690050 188 AKGVDVMVEKMEPAVT 203
Cdd:cd01822 162 AEGQPIIAENVWPALE 177
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
21-202 |
5.91e-46 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 150.56 E-value: 5.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 21 TAANARTINLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKglDVTIANAGVSGDTTTAGLARVDWSVPDG-TDGVILELG 99
Cdd:COG2755 2 KAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAA--DVRVVNAGISGATTADLLARLDRDLLALkPDLVVIELG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 100 ANDALRGI--PPEESEKNLDQMITRLKARG--IAVLLAGI--IAPPNMGADYAARFNPIYQKLSEKHKLPLYAFF--LDG 171
Cdd:COG2755 80 TNDLLRGLgvSPEEFRANLEALIDRLRAAGpgARVVLVTPppRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYaaLRD 159
|
170 180 190
....*....|....*....|....*....|.
gi 1672690050 172 VALEAGLKLEDGMHPNAKGVDVMVEKMEPAV 202
Cdd:COG2755 160 AGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
|
|
| PRK10528 |
PRK10528 |
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional |
18-204 |
3.98e-38 |
|
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
Pssm-ID: 182521 Cd Length: 191 Bit Score: 130.65 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 18 ILATAANARTINLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKGldvTIANAGVSGDTTTAGLARV---------DWsvp 88
Cdd:PRK10528 1 VLLTFRAAAADTLLILGDSLSAGYRMPASAAWPALLNDKWQSKT---SVVNASISGDTSQQGLARLpallkqhqpRW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 89 dgtdgVILELGANDALRGIPPEESEKNLDQMITRLKARGIAVLLAGIIAPPNMGADYAARFNPIYQKLSEKHKLPLYAFF 168
Cdd:PRK10528 75 -----VLVELGGNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1672690050 169 LDGVALEAGLKLEDGMHPNAKG----VDVMVEKMEPAVTN 204
Cdd:PRK10528 150 MEEVYLKPQWMQDDGIHPNRDAqpfiADWMAKQLQPLVNH 189
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
33-190 |
4.16e-27 |
|
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.
Pssm-ID: 463889 Cd Length: 176 Bit Score: 101.85 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 33 FGDSLMAGYQLPLGD-GFPEKLQAALKAKGLDVTIANAGVSGDTTTAGLA-RVDWSVPDGTDGVILELGANDALRGIPPE 110
Cdd:pfam13472 2 LGDSITAGYGATGGDrSYPGWLARLLARRLGADVVNNLGISGATTRLDLLeRLDDVLRLKPDLVVILLGTNDLGRGVSAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 111 ESEKNLDQMITRLKARG--IAVLLAGIIAP-------PNMGADYAARFNPIYQKLSEKHKLP---LYAFFLDGVALEAGL 178
Cdd:pfam13472 82 RAAANLEALIDALRAAGpdARVLLIGPLPVgppppldERRLNARIAEYNAAIREVAAERGVPyvdLWDALRDDGGWLPDL 161
|
170
....*....|..
gi 1672690050 179 KLEDGMHPNAKG 190
Cdd:pfam13472 162 LADDGLHPNAAG 173
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
30-201 |
2.06e-24 |
|
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 238141 [Multi-domain] Cd Length: 187 Bit Score: 95.17 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 30 LVGFGDSLMAGYQLPLGDGFP-EKLQAALKAKGLDVTIANAGVSGDTTTAGLARVDWS---VPDGTDGVILELGANDALR 105
Cdd:cd00229 1 ILVIGDSITAGYGASSGSTFYsLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRlalLKDKPDLVIIELGTNDLGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 106 GI--PPEESEKNLDQMITRLKAR--GIAVLLAGIIAPPNMGADYAA---RFNPIYQKLSEKHKLPLYAFFLDGVALEAGL 178
Cdd:cd00229 81 GGdtSIDEFKANLEELLDALRERapGAKVILITPPPPPPREGLLGRalpRYNEAIKAVAAENPAPSGVDLVDLAALLGDE 160
|
170 180
....*....|....*....|....*..
gi 1672690050 179 KLE----DGMHPNAKGVDVMVEKMEPA 201
Cdd:cd00229 161 DKSlyspDGIHPNPAGHKLIAEALASA 187
|
|
| SGNH_hydrolase_like_4 |
cd04501 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
28-194 |
1.90e-16 |
|
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 239945 Cd Length: 183 Bit Score: 73.90 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 28 INLVGFGDSLMAGYqlplGDGfPEKLQAALKAKGLDVTIANAGVSGDTTTAGLARVDWSV-PDGTDGVILELGANDALRG 106
Cdd:cd04501 1 MRVVCLGDSITYGY----PVG-PEASWVNLLAEFLGKEVINRGINGDTTSQMLVRFYEDViALKPAVVIIMGGTNDIIVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 107 IPPEESEKNLDQMITRLKARGIAVLLaGIIAPPNM------GADYA---ARFNPIYQKLSEKHKLPLYAFF-----LDGV 172
Cdd:cd04501 76 TSLEMIKDNIRSMVELAEANGIKVIL-ASPLPVDDypwkpqWLRPAnklKSLNRWLKDYARENGLLFLDFYsplldERNV 154
|
170 180
....*....|....*....|..
gi 1672690050 173 ALEAGLkLEDGMHPNAKGVDVM 194
Cdd:cd04501 155 GLKPGL-LTDGLHPSREGYRVM 175
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
30-198 |
6.72e-15 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 70.29 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 30 LVGFGDSLMAGY-QLPLGDGFPEKLQAALKAKGLDV------TIANAGVSGDTT------TAGLARVDWSVPDGTDG--V 94
Cdd:pfam00657 1 IVAFGDSLTDGGgDGPGGRFSWGDLLADFLARKLGVpgsgynHGANFAIGGATIedlpiqLEQLLRLISDVKDQAKPdlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 95 ILELGANDALRG-IPPEESEKNLDQMITRLK---------ARGIAVLLAGII--APP--------NMGADYAARFNPIYQ 154
Cdd:pfam00657 81 TIFIGANDLCNFlSSPARSKKRVPDLLDELRanlpqlglgARKFWVHGLGPLgcTPPkgcyelynALAEEYNERLNELVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1672690050 155 KLSEKHK------LPLYAFFLDGVALEAGLKLEDGMHPNAKGVDVMVEKM 198
Cdd:pfam00657 161 SLAAAAEdanvvyVDIYGFEDPTDPCCGIGLEPDGLHPSEKGYKAVAEAI 210
|
|
| sialate_O-acetylesterase_like2 |
cd01828 |
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ... |
29-202 |
1.02e-12 |
|
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238866 Cd Length: 169 Bit Score: 63.45 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 29 NLVGFGDSLMAGYqlPLGDGFPeklqaalkakglDVTIANAGVSGDTTTAGLARVDWSVPDGTDGVILELGANDALRGIP 108
Cdd:cd01828 1 ALVFLGDSLTEGG--PWALLFP------------DVKVANRGISGDTTRGLLARLDEDVALQPKAIFIMIGINDLAQGTS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 109 PEESEKNLDQMITRLKA--RGIAVLLAGIiaPPnMGADyAARFNPIYQKLSEkhKLPLYA-----FFLDGVAL--EAGLK 179
Cdd:cd01828 67 DEDIVANYRTILEKLRKhfPNIKIVVQSI--LP-VGEL-KSIPNEQIEELNR--QLAQLAqqegvTFLDLWAVftNADGD 140
|
170 180
....*....|....*....|....*...
gi 1672690050 180 LE-----DGMHPNAKGVDVMVEKMEPAV 202
Cdd:cd01828 141 LKnefttDGLHLNAKGYAVWAAALQPYL 168
|
|
| FeeA_FeeB_like |
cd01836 |
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ... |
33-202 |
5.17e-12 |
|
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238874 Cd Length: 191 Bit Score: 61.90 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 33 FGDSLMAGYQ-LPLGDGFPEKLQAALKAK-GLDVTIANAGVSGDTTTAGLARVDWSVPDGTDGVILELGANDALRGIPPE 110
Cdd:cd01836 8 LGDSTAAGVGvETQDQALAGQLARGLAAItGRGVRWRLFAKTGATSADLLRQLAPLPETRFDVAVISIGVNDVTHLTSIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 111 ESEKNLDQMITRLKAR--GIAVLLAGIiapPNMG-------------ADYAARFNPIYQKL-SEKHKLPLYAffLDGVAL 174
Cdd:cd01836 88 RWRKQLAELVDALRAKfpGARVVVTAV---PPLGrfpalpqplrwllGRRARLLNRALERLaSEAPRVTLLP--ATGPLF 162
|
170 180
....*....|....*....|....*...
gi 1672690050 175 EAGLKlEDGMHPNAKGVDVMVEKMEPAV 202
Cdd:cd01836 163 PALFA-SDGFHPSAAGYAVWAEALAPAI 189
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
28-194 |
6.88e-12 |
|
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238872 Cd Length: 191 Bit Score: 61.93 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 28 INLVGFGDSLMAGYQLPlgDGFPEKLQAALKakGLDVTIANAGVSGDTTTAGLARVD-WSVPDGTDGVILELGANDALRG 106
Cdd:cd01834 2 DRIVFIGNSITDRGGYV--GYVETYLAARYP--ELKLTFRNLGWSGDTVSDLAARRDrDVLPAKPDVVSIMFGINDSFRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 107 IP----PEESEKNLDQMITRLKARGIA---VLLAGIIAPPNM-----GADYAAR---FNPIYQKLSEKHKL---PLYAFF 168
Cdd:cd01834 78 FDdpvgLEKFKTNLRRLIDRLKNKESApriVLVSPIAYEANEdplpdGAEYNANlaaYADAVRELAAENGVafvDLFTPM 157
|
170 180
....*....|....*....|....*..
gi 1672690050 169 LDGV-ALEAGLKLEDGMHPNAKGVDVM 194
Cdd:cd01834 158 KEAFqKAGEAVLTVDGVHPNEAGHRAL 184
|
|
| Isoamyl_acetate_hydrolase_like |
cd01838 |
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ... |
30-198 |
7.25e-11 |
|
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
Pssm-ID: 238876 Cd Length: 199 Bit Score: 59.19 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 30 LVGFGDSLMagyQLPLGDGFPEkLQAALK---AKGLDVTiaNAGVSGDTTTAGLARVDWSVP----DGTDGVILELGAND 102
Cdd:cd01838 2 IVLFGDSIT---QFSFDQGEFG-FGAALAdvySRKLDVI--NRGFSGYNTRWALKVLPKIFLeeklAQPDLVTIFFGAND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 103 AL-----RGIPPEESEKNLDQMITRLKAR--GIAVLLagiIAPP--NMGADYAARFNPIYQKLSEKHKLPLYAFFLDGVA 173
Cdd:cd01838 76 AAlpgqpQHVPLDEYKENLRKIVSHLKSLspKTKVIL---ITPPpvDEEAWEKSLEDGGSQPGRTNELLKQYAEACVEVA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1672690050 174 LEAGLK------------------LEDGMHPNAKGVDVMVEKM 198
Cdd:cd01838 153 EELGVPvidlwtamqeeagwleslLTDGLHFSSKGYELLFEEI 195
|
|
| COG2845 |
COG2845 |
Peptidoglycan O-acetyltransferase, SGNH hydrolase family [Cell wall/membrane/envelope ... |
6-170 |
2.71e-09 |
|
Peptidoglycan O-acetyltransferase, SGNH hydrolase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442093 Cd Length: 229 Bit Score: 54.93 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 6 AALQFTVIAVSLILATAANARTInLVgFGDSLMAGyqlpLGDGfpekLQAALKAKgLDVTIANAGVSGdtttAGLAR--- 82
Cdd:COG2845 2 STSRLVRLLLLLLLAKLPDADRV-LV-IGDSLAQG----LAPG----LQRALADQ-PGIRVINLSKQS----TGLVRpdf 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 83 VDWS-------VPDGTDGVILELGANDAlRGIPP-------------EESEKNLDQMITRLKARGIAVLLAGiiaPPNMG 142
Cdd:COG2845 67 FDWPktirellAEEKPDVVVVMLGANDR-QDIRDgggrlkfgspeweEEYRRRVDALLRALRAHGVPVIWVG---LPPMR 142
|
170 180 190
....*....|....*....|....*....|....*
gi 1672690050 143 A----DYAARFNPIYQKLSEKHK---LPLYAFFLD 170
Cdd:COG2845 143 SprlsADMAYLNDIYREEAEKAGvifVDTWDGFVD 177
|
|
| SGNH_hydrolase_like_3 |
cd01835 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
28-190 |
5.72e-09 |
|
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238873 Cd Length: 193 Bit Score: 53.88 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 28 INLVGFGDSLMAGYQLPLGDGFPEKLQAALKAKGLDVTIANAGVSGDTTTAGLAR--VDWS---VPDGTDGVILELGAND 102
Cdd:cd01835 2 KRLIVVGDSLVYGWGDPEGGGWVGRLRARWMNLGDDPVLYNLGVRGDGSEDVAARwrAEWSrrgELNVPNRLVLSVGLND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 103 ALRG------IPPEESEKNLDQMITRLKaRGIAVLLAGIiaPP---------NMG-ADYAARFNPIYQKLSEKHkLPLYA 166
Cdd:cd01835 82 TARGgrkrpqLSARAFLFGLNQLLEEAK-RLVPVLVVGP--TPvdeakmpysNRRiARLETAFAEVCLRRDVPF-LDTFT 157
|
170 180
....*....|....*....|....
gi 1672690050 167 FFLDGVALEAGLKLEDGMHPNAKG 190
Cdd:cd01835 158 PLLNHPQWRRELAATDGIHPNAAG 181
|
|
| XynE_like |
cd01830 |
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ... |
30-194 |
1.14e-07 |
|
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238868 Cd Length: 204 Bit Score: 50.32 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 30 LVGFGDSLMAGYQLPLG------DGFPEKLQAALKAKGLDVtiANAGVSGDTTTA------GLARVD---WSVPdGTDGV 94
Cdd:cd01830 2 VVALGDSITDGRGSTPDannrwpDLLAARLAARAGTRGIAV--LNAGIGGNRLLAdglgpsALARFDrdvLSQP-GVRTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 95 ILELGANDaLRGIPPEESEKNLD---------QMITRLKARGIAVLLAGIiaPPNMGADYAARFN-PIYQKLSE------ 158
Cdd:cd01830 79 IILEGVND-IGASGTDFAAAPVTaeeliagyrQLIRRAHARGIKVIGATI--TPFEGSGYYTPAReATRQAVNEwirtsg 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1672690050 159 --KHKLPLYAFFLDGV---ALEAGLKLEDGMHPNAKGVDVM 194
Cdd:cd01830 156 afDAVVDFDAALRDPAdpsRLRPAYDSGDHLHPNDAGYQAM 196
|
|
| SGNH_arylesterase_like |
cd01839 |
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ... |
33-203 |
2.63e-07 |
|
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238877 Cd Length: 208 Bit Score: 49.19 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 33 FGDSLMAGY------QLPLGDGFPEKLQAALKAKGLDVTIANAGVSGDTTTA---------GLARVDWSVPDGT--DGVI 95
Cdd:cd01839 5 FGDSNTWGIipdtggRYPFEDRWPGVLEKALGANGENVRVIEDGLPGRTTVLddpffpgrnGLTYLPQALESHSplDLVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 96 LELGANDALR--GIPPEESEKNLDQMI----TRLKARGIAVLLAGIIAPPNM-------------GADYAARFNPIYQKL 156
Cdd:cd01839 85 IMLGTNDLKSyfNLSAAEIAQGLGALVdiirTAPIEPGMPAPKILIVAPPPIrtpkgslagkfagAEEKSKGLADAYRAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1672690050 157 SEKHKlplyAFFLDG--VALEAGLkleDGMHPNAKGVDVMVEKMEPAVT 203
Cdd:cd01839 165 AEELG----CHFFDAgsVGSTSPV---DGVHLDADQHAALGQALASVIR 206
|
|
| SGNH_hydrolase_peri1 |
cd01825 |
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ... |
33-198 |
7.59e-05 |
|
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238863 Cd Length: 189 Bit Score: 41.88 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 33 FGDSLMAGyqlplgDGFPEKLQAALKakgldVTIANAGVSGDTTTaglarvDWSVPDGT-----------DGVILELGAN 101
Cdd:cd01825 5 LGDSHIAG------DFFTDVLRGLLG-----VIYDNLGVNGASAS------LLLKWDAEflqaqlaalppDLVILSYGTN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 102 DALR-GIPPEESEKNLDQMITRLKARGIAVLLAgIIAPPN-------MGADYAARFNPIYQKLSE---KHKLP---LYAf 167
Cdd:cd01825 68 EAFNkQLNASEYRQQLREFIKRLRQILPNASIL-LVGPPDslqktgaGRWRTPPGLDAVIAAQRRvakEEGIAfwdLYA- 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 1672690050 168 FLDGVA-----LEAGLKLEDGMHPNAKGVDVMVEKM 198
Cdd:cd01825 146 AMGGEGgiwqwAEPGLARKDYVHLTPRGYERLANLL 181
|
|
| SGNH_hydrolase_YpmR_like |
cd04506 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
29-197 |
1.07e-04 |
|
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. This subfamily contains sequences similar to Bacillus YpmR.
Pssm-ID: 239947 Cd Length: 204 Bit Score: 41.46 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 29 NLVGFGDSLMAGYQLPLGDGFPEKLQAALKAK--GLDVTIANAGVSGDTTTAGLARVDWS-VPDG---TDGVILELGAND 102
Cdd:cd04506 1 KIVALGDSLTEGVGDETGKGGYVGRLDKLIETktVKKVTVQNFGVSGDRSDQLLKRLKTKkVQKElkkADVITITIGGND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 103 ALRGI-------------PPEES-EKNLDQMITRLKARG--IAVLLAGIIAP-----PNMGA--DYAARFNPIYQKLSEK 159
Cdd:cd04506 81 LMQVLeknflsldvedfkKAEETyQNNLKKIFKEIRKLNpdAPIFLVGLYNPfyvyfPNITEinDIVNDWNEASQKLASQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1672690050 160 HK----LPLYAFFLDGValEAGLKLEDGMHPNAKGVDVMVEK 197
Cdd:cd04506 161 YKnayfVPIFDLFSDGQ--NKYLLTSDHFHPNDKGYQLIADR 200
|
|
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
68-194 |
1.62e-04 |
|
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238871 Cd Length: 157 Bit Score: 40.68 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672690050 68 NAGVSGDTTT--AGLArVDWSVPDGTDGVILELGANDALRGIPPEESEKNLDQMITRLKA--RGIAVLLAGII-APPNMG 142
Cdd:cd01833 17 HEGHSGYLIDqiAAAA-ADWVLAAKPDVVLLHLGTNDLVLNRDPDTAPDRLRALIDQMRAanPDVKIIVATLIpTTDASG 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1672690050 143 ADYAARFNPIYQKLSEKH---KLPLYafFLD-GVALEAGLKLEDGMHPNAKGVDVM 194
Cdd:cd01833 96 NARIAEYNAAIPGVVADLrtaGSPVV--LVDmSTGYTTADDLYDGLHPNDQGYKKM 149
|
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