|
Name |
Accession |
Description |
Interval |
E-value |
| Rhamnogalacturan_acetylesterase_like |
cd01821 |
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ... |
25-234 |
6.35e-85 |
|
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
Pssm-ID: 238859 Cd Length: 198 Bit Score: 251.36 E-value: 6.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 25 INVFMAGDSTMSIKEvKDYPETGWGMPFQYFFNDQVQVINLAKNGRSTRTFKSEGRWQMIMDEIKPGDYVIIQFGHNDQs 104
Cdd:cd01821 1 PTIFLAGDSTVADYD-PGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRSFRDEGRWDAILKLIKPGDYVLIQFGHNDQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 105 KQKVDRYT-SVPDFKANLLGFIKDVREKQAHPLLMTPITRRYFNEDGTIKETHPLYADAVRDVAKQTKVDFIDMEAITKR 183
Cdd:cd01821 79 KPKDPEYTePYTTYKEYLRRYIAEARAKGATPILVTPVTRRTFDEGGKVEDTLGDYPAAMRELAAEEGVPLIDLNAASRA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053177521 184 YFQALGDDGSALRFmhiapdlhpnyPLGVTDDTHLNQLGATEVAQLVLTEL 234
Cdd:cd01821 159 LYEAIGPEKSKKYF-----------PEGPGDNTHFSEKGADVVARLVAEEL 198
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
18-235 |
8.68e-33 |
|
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: 118.21 E-value: 8.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 18 TAQADEQINVFMAGDSTMSikEVKDYPETGWGMPFQ-YFFNDQVQVINLAKNGRSTRTFKSegRWQMIMDEIKPgDYVII 96
Cdd:COG2755 2 KAAAGKPLRIVALGDSITA--GYGASRERGWPALLArRLAAADVRVVNAGISGATTADLLA--RLDRDLLALKP-DLVVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 97 QFGHNDQskqKVDRYTSVPDFKANLLGFIKDVREK--QAHPLLMTPITRRYFNEdgtIKETHPLYADAVRDVAKQTKVDF 174
Cdd:COG2755 77 ELGTNDL---LRGLGVSPEEFRANLEALIDRLRAAgpGARVVLVTPPPRLRPNY---LNERIEAYNAAIRELAAEYGVPL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053177521 175 IDMeaitkryFQALGDDGSALRFMhiapdlhpnyplgVTDDTHLNQLGATEVAQLVLTELK 235
Cdd:COG2755 151 VDL-------YAALRDAGDLPDLL-------------TADGLHPNAAGYRLIAEAVLPALK 191
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
62-207 |
1.55e-13 |
|
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: 66.80 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 62 VINLAKNGRSTRtFKSEGRWQMImDEIKPgDYVIIQFGHNDqskqkVDRYTSVPDFKANLLGFIKDVREKQAHPLLMT-- 139
Cdd:pfam13472 36 VNNLGISGATTR-LDLLERLDDV-LRLKP-DLVVILLGTND-----LGRGVSAARAAANLEALIDALRAAGPDARVLLig 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 140 --PITRRYFNEDGTIKETHPLYADAVRDVAKQTKVDFIDMeaitkryFQALGDDGSALRFMHIAPDLHPN 207
Cdd:pfam13472 108 plPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDL-------WDALRDDGGWLPDLLADDGLHPN 170
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rhamnogalacturan_acetylesterase_like |
cd01821 |
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ... |
25-234 |
6.35e-85 |
|
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
Pssm-ID: 238859 Cd Length: 198 Bit Score: 251.36 E-value: 6.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 25 INVFMAGDSTMSIKEvKDYPETGWGMPFQYFFNDQVQVINLAKNGRSTRTFKSEGRWQMIMDEIKPGDYVIIQFGHNDQs 104
Cdd:cd01821 1 PTIFLAGDSTVADYD-PGAPQAGWGQALPQYLDTGITVVNHAKGGRSSRSFRDEGRWDAILKLIKPGDYVLIQFGHNDQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 105 KQKVDRYT-SVPDFKANLLGFIKDVREKQAHPLLMTPITRRYFNEDGTIKETHPLYADAVRDVAKQTKVDFIDMEAITKR 183
Cdd:cd01821 79 KPKDPEYTePYTTYKEYLRRYIAEARAKGATPILVTPVTRRTFDEGGKVEDTLGDYPAAMRELAAEEGVPLIDLNAASRA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1053177521 184 YFQALGDDGSALRFmhiapdlhpnyPLGVTDDTHLNQLGATEVAQLVLTEL 234
Cdd:cd01821 159 LYEAIGPEKSKKYF-----------PEGPGDNTHFSEKGADVVARLVAEEL 198
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
18-235 |
8.68e-33 |
|
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: 118.21 E-value: 8.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 18 TAQADEQINVFMAGDSTMSikEVKDYPETGWGMPFQ-YFFNDQVQVINLAKNGRSTRTFKSegRWQMIMDEIKPgDYVII 96
Cdd:COG2755 2 KAAAGKPLRIVALGDSITA--GYGASRERGWPALLArRLAAADVRVVNAGISGATTADLLA--RLDRDLLALKP-DLVVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 97 QFGHNDQskqKVDRYTSVPDFKANLLGFIKDVREK--QAHPLLMTPITRRYFNEdgtIKETHPLYADAVRDVAKQTKVDF 174
Cdd:COG2755 77 ELGTNDL---LRGLGVSPEEFRANLEALIDRLRAAgpGARVVLVTPPPRLRPNY---LNERIEAYNAAIRELAAEYGVPL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053177521 175 IDMeaitkryFQALGDDGSALRFMhiapdlhpnyplgVTDDTHLNQLGATEVAQLVLTELK 235
Cdd:COG2755 151 VDL-------YAALRDAGDLPDLL-------------TADGLHPNAAGYRLIAEAVLPALK 191
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
62-207 |
1.55e-13 |
|
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: 66.80 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 62 VINLAKNGRSTRtFKSEGRWQMImDEIKPgDYVIIQFGHNDqskqkVDRYTSVPDFKANLLGFIKDVREKQAHPLLMT-- 139
Cdd:pfam13472 36 VNNLGISGATTR-LDLLERLDDV-LRLKP-DLVVILLGTND-----LGRGVSAARAAANLEALIDALRAAGPDARVLLig 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 140 --PITRRYFNEDGTIKETHPLYADAVRDVAKQTKVDFIDMeaitkryFQALGDDGSALRFMHIAPDLHPN 207
Cdd:pfam13472 108 plPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDL-------WDALRDDGGWLPDLLADDGLHPN 170
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
27-231 |
9.26e-13 |
|
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: 64.74 E-value: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 27 VFMAGDSTMSIKEVKDYPETGWGMPF--QYFFNDQVQVINLAKNGRSTRTFKSEGRWQMIMDEIKPgDYVIIQFGHNDQS 104
Cdd:cd00229 1 ILVIGDSITAGYGASSGSTFYSLLLYllLLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKP-DLVIIELGTNDLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 105 KqkvDRYTSVPDFKANLLGFIKDVRE--KQAHPLLMTPITRryFNEDGTIKETHPLYADAVRDVAKQ----TKVDFIDME 178
Cdd:cd00229 80 R---GGDTSIDEFKANLEELLDALREraPGAKVILITPPPP--PPREGLLGRALPRYNEAIKAVAAEnpapSGVDLVDLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1053177521 179 AITKRYFQALGDDgsalrfmhiapdlhpnyplgvtDDTHLNQLGATEVAQLVL 231
Cdd:cd00229 155 ALLGDEDKSLYSP----------------------DGIHPNPAGHKLIAEALA 185
|
|
| SGNH_hydrolase_peri1 |
cd01825 |
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ... |
60-236 |
1.94e-11 |
|
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: 61.14 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 60 VQVINLAKNGRSTRTFKSEGRwQMIMDEIKPGDY--VIIQFGHNDQSKQKVDRytsvPDFKANLLGFIKDVRE--KQAHP 135
Cdd:cd01825 25 VIYDNLGVNGASASLLLKWDA-EFLQAQLAALPPdlVILSYGTNEAFNKQLNA----SEYRQQLREFIKRLRQilPNASI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 136 LLMTPITRRYFNEDGTIKETHPLYA--DAVRDVAKQTKVDFIDMeaitkryFQALGDDGSALRFMhiapdlhpNYPLGVT 213
Cdd:cd01825 100 LLVGPPDSLQKTGAGRWRTPPGLDAviAAQRRVAKEEGIAFWDL-------YAAMGGEGGIWQWA--------EPGLARK 164
|
170 180
....*....|....*....|...
gi 1053177521 214 DDTHLNQLGATEVAQLVLTELKK 236
Cdd:cd01825 165 DYVHLTPRGYERLANLLYEALLK 187
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
59-231 |
1.19e-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: 238872 Cd Length: 191 Bit Score: 56.15 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 59 QVQVINLAKNGRSTRTFKseGRWQMIMDEIKPgDYVIIQFGHNDqSKQKVDRYTSVPDFKANLLGFIKDVREKQAHP--L 136
Cdd:cd01834 33 KLTFRNLGWSGDTVSDLA--ARRDRDVLPAKP-DVVSIMFGIND-SFRGFDDPVGLEKFKTNLRRLIDRLKNKESAPriV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 137 LMTPITRRYFNEDGTIKETH----PLYADAVRDVAKQTKVDFIDMEAITKRYFQAlgddgsalrfmhiapdlHPNYPLGv 212
Cdd:cd01834 109 LVSPIAYEANEDPLPDGAEYnanlAAYADAVRELAAENGVAFVDLFTPMKEAFQK-----------------AGEAVLT- 170
|
170
....*....|....*....
gi 1053177521 213 TDDTHLNQLGATEVAQLVL 231
Cdd:cd01834 171 VDGVHPNEAGHRALARLWL 189
|
|
| Isoamyl_acetate_hydrolase_like |
cd01838 |
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ... |
45-234 |
3.29e-07 |
|
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: 49.56 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 45 ETGWGMPFQYFFNDQVQVINLAKNGRSTRTFKSegRWQMIMDEIKPG--DYVIIQFGHNDQSKQKVDRYTSVPDFKANL- 121
Cdd:cd01838 18 EFGFGAALADVYSRKLDVINRGFSGYNTRWALK--VLPKIFLEEKLAqpDLVTIFFGANDAALPGQPQHVPLDEYKENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 122 --LGFIKDVREKQaHPLLMTP-------ITRRYFNEDGTI---KETHPLYADAVRDVAKQTKVDFIDMeaitkryFQALG 189
Cdd:cd01838 96 kiVSHLKSLSPKT-KVILITPppvdeeaWEKSLEDGGSQPgrtNELLKQYAEACVEVAEELGVPVIDL-------WTAMQ 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1053177521 190 DDGSALRFMhiapdlhpnyplgVTDDTHLNQLGATEVAQLVLTEL 234
Cdd:cd01838 168 EEAGWLESL-------------LTDGLHFSSKGYELLFEEIVKVI 199
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
27-230 |
4.11e-07 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 49.11 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 27 VFMAGDSTMSIKEVKDYPETGWGMPFQYFFNDQVQV--------INLAKNGRSTRTFKSEGRwQMI-----MDEIKPGDY 93
Cdd:pfam00657 1 IVAFGDSLTDGGGDGPGGRFSWGDLLADFLARKLGVpgsgynhgANFAIGGATIEDLPIQLE-QLLrlisdVKDQAKPDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 94 VIIQFGHNDQSKQKVDRYTSVPDFKANLLGFIKDVREKQ----------AHPLLMTPITRRY--FNEDGTikethpLYAD 161
Cdd:pfam00657 80 VTIFIGANDLCNFLSSPARSKKRVPDLLDELRANLPQLGlgarkfwvhgLGPLGCTPPKGCYelYNALAE------EYNE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053177521 162 AVRDVAKQTKVDFIDMEAItkryfqalgddgsalrFMHIAPDLHPNYPL----GVTDDTHLNQLGATEVAQLV 230
Cdd:pfam00657 154 RLNELVNSLAAAAEDANVV----------------YVDIYGFEDPTDPCcgigLEPDGLHPSEKGYKAVAEAI 210
|
|
| sialate_O-acetylesterase_like1 |
cd01827 |
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ... |
36-230 |
1.21e-04 |
|
sialate O-acetylesterase_like family 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: 238865 Cd Length: 188 Bit Score: 41.66 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 36 SIKEVKDYPETG-WGMPFQYFFNDQVQVINLaknGRSTRTFKSEGRWQ-MIMDEIKP-----GDYVIIQFGHNDqSKQKV 108
Cdd:cd01827 9 SITEGAGLRAYDsYPSPLAQMLGDGYEVGNF---GKSARTVLNKGDHPyMNEERYKNalafnPNIVIIKLGTND-AKPQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 109 DRYTSvpDFKANLLGFIKDVREKQAHP--LLMTPITR-----RYFNEDGTIKETHPlyadAVRDVAKQTKVDFIDmeait 181
Cdd:cd01827 85 WKYKD--DFKKDYETMIDSFQALPSKPkiYICYPIPAyygdgGFINDNIIKKEIQP----MIDKIAKKLNLKLID----- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1053177521 182 kryfqalgddgsalrfMHIAPDLHPNYplgVTDDTHLNQLGATEVAQLV 230
Cdd:cd01827 154 ----------------LHTPLKGKPEL---VPDWVHPNEKGAYILAKVV 183
|
|
| Endoglucanase_E_like |
cd01831 |
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ... |
92-208 |
1.51e-04 |
|
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pssm-ID: 238869 Cd Length: 169 Bit Score: 41.18 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 92 DYVIIQFGHNDQSKqkvDRYTSVPDFKANLLGFIKDVREK--QAHPLLMTpiTRRYFNEDGTIKETHpLYADAVRDvAKQ 169
Cdd:cd01831 57 DLVVINLGTNDFST---GNNPPGEDFTNAYVEFIEELRKRypDAPIVLML--GPMLFGPYGTEEEIK-RVAEAFKD-QKS 129
|
90 100 110
....*....|....*....|....*....|....*....
gi 1053177521 170 TKVDFIDMEAITKRYFqalgddgsalrfmhIAPDLHPNY 208
Cdd:cd01831 130 KKVHYFDTPGILQHND--------------IGCDWHPTV 154
|
|
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
60-207 |
1.94e-04 |
|
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: 40.96 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 60 VQVINLAKNGRSTrtfkSEG--RWQMIMDEIKPgDYVIIQFGHND----QSKQKVdrytsvpdfKANLLGFIKDVREKQA 133
Cdd:cd01822 37 VTVINAGVSGDTT----AGGlaRLPALLAQHKP-DLVILELGGNDglrgIPPDQT---------RANLRQMIETAQARGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 134 HPLLM-----TPITRRYFnedgtiKETHPLYadavRDVAKQTKV----DFIDMEAITKRYFQalgDDGsalrfmhiapdL 204
Cdd:cd01822 103 PVLLVgmqapPNYGPRYT------RRFAAIY----PELAEEYGVplvpFFLEGVAGDPELMQ---SDG-----------I 158
|
...
gi 1053177521 205 HPN 207
Cdd:cd01822 159 HPN 161
|
|
| SGNH_hydrolase_like_3 |
cd01835 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
94-231 |
2.43e-04 |
|
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: 40.78 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053177521 94 VIIQFGHNDQSKQKVDRYTSVPDFKANLLGFIkDVREKQAHPLL---MTPI---TRRYFNEDGTikethpLYADAVRDVA 167
Cdd:cd01835 73 LVLSVGLNDTARGGRKRPQLSARAFLFGLNQL-LEEAKRLVPVLvvgPTPVdeaKMPYSNRRIA------RLETAFAEVC 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053177521 168 KQTKVDFIDMeaitkryFQALGDDGSALRfmHIAPdlhpnyplgvTDDTHLNQLGATEVAQLVL 231
Cdd:cd01835 146 LRRDVPFLDT-------FTPLLNHPQWRR--ELAA----------TDGIHPNAAGYGWLAWLVL 190
|
|
| |
