|
Name |
Accession |
Description |
Interval |
E-value |
| SGNH_hydrolase_like_1 |
cd01832 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
27-205 |
2.30e-35 |
|
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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.
Pssm-ID: 238870 Cd Length: 185 Bit Score: 123.53 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 27 SYLALGDSYTIGESIEVED----SYPNQLKEKIDIIDS---LKIIAKTGWTTDE-LIDTLNNSNLKQYDIVSLLIGVNNQ 98
Cdd:cd01832 1 RYVALGDSITEGVGDPVPDggyrGWADRLAAALAAADPgieYANLAVRGRRTAQiLAEQLPAALALRPDLVTLLAGGNDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 99 FR-GYSIDNYKVEFENLLAktiRYSNNKKNVFVLSIPDYGV-TPFGQSRGKekiynEINAYNDINRIISEKYNVMYFNIT 176
Cdd:cd01832 81 LRpGTDPDTYRADLEEAVR---RLRAAGARVVVFTIPDPAVlEPFRRRVRA-----RLAAYNAVIRAVAARYGAVHVDLW 152
|
170 180
....*....|....*....|....*....
gi 1251812611 177 DISRRAenDLTLLANDKLHPSEKMYAEWV 205
Cdd:cd01832 153 EHPEFA--DPRLWASDRLHPSAAGHARLA 179
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
19-208 |
2.22e-27 |
|
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: 102.80 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 19 KDYSRPSLSYLALGDSYTIGESIEVEDSYPNQLKEKIDIIDsLKII--AKTGWTTDELIDTLNNSNLK-QYDIVSLLIGV 95
Cdd:COG2755 2 KAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAAD-VRVVnaGISGATTADLLARLDRDLLAlKPDLVVIELGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 96 NNQFRGY--SIDNYKVEFENLLAKTIRYSNNKKnVFVLSIPdygvtPFgqsRGKEKIYNEINAYNDINRIISEKYNVMYF 173
Cdd:COG2755 81 NDLLRGLgvSPEEFRANLEALIDRLRAAGPGAR-VVLVTPP-----PR---LRPNYLNERIEAYNAAIRELAAEYGVPLV 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1251812611 174 NITDISRRAENDLTLLANDKLHPSEKMYAEWVNLM 208
Cdd:COG2755 152 DLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAV 186
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
30-202 |
6.54e-19 |
|
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: 80.28 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 30 ALGDSYTIGESIE-VEDSYPNQLKEKID---IIDSLKIIAKTGWTTDELIDT-LNNSNLKQYDIVSLLIGVNNQFRGYSI 104
Cdd:pfam13472 1 ALGDSITAGYGATgGDRSYPGWLARLLArrlGADVVNNLGISGATTRLDLLErLDDVLRLKPDLVVILLGTNDLGRGVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 105 DNYKVEFENLLAKTIRYSNNKKnvfVLSIPDYGVTPFGQSRGKEkIYNEINAYNDINRIISEKYNVMYFNITDISRRAEN 184
Cdd:pfam13472 81 ARAAANLEALIDALRAAGPDAR---VLLIGPLPVGPPPPLDERR-LNARIAEYNAAIREVAAERGVPYVDLWDALRDDGG 156
|
170
....*....|....*....
gi 1251812611 185 DL-TLLANDKLHPSEKMYA 202
Cdd:pfam13472 157 WLpDLLADDGLHPNAAGYR 175
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SGNH_hydrolase_like_1 |
cd01832 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
27-205 |
2.30e-35 |
|
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. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.
Pssm-ID: 238870 Cd Length: 185 Bit Score: 123.53 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 27 SYLALGDSYTIGESIEVED----SYPNQLKEKIDIIDS---LKIIAKTGWTTDE-LIDTLNNSNLKQYDIVSLLIGVNNQ 98
Cdd:cd01832 1 RYVALGDSITEGVGDPVPDggyrGWADRLAAALAAADPgieYANLAVRGRRTAQiLAEQLPAALALRPDLVTLLAGGNDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 99 FR-GYSIDNYKVEFENLLAktiRYSNNKKNVFVLSIPDYGV-TPFGQSRGKekiynEINAYNDINRIISEKYNVMYFNIT 176
Cdd:cd01832 81 LRpGTDPDTYRADLEEAVR---RLRAAGARVVVFTIPDPAVlEPFRRRVRA-----RLAAYNAVIRAVAARYGAVHVDLW 152
|
170 180
....*....|....*....|....*....
gi 1251812611 177 DISRRAenDLTLLANDKLHPSEKMYAEWV 205
Cdd:cd01832 153 EHPEFA--DPRLWASDRLHPSAAGHARLA 179
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
19-208 |
2.22e-27 |
|
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: 102.80 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 19 KDYSRPSLSYLALGDSYTIGESIEVEDSYPNQLKEKIDIIDsLKII--AKTGWTTDELIDTLNNSNLK-QYDIVSLLIGV 95
Cdd:COG2755 2 KAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAAD-VRVVnaGISGATTADLLARLDRDLLAlKPDLVVIELGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 96 NNQFRGY--SIDNYKVEFENLLAKTIRYSNNKKnVFVLSIPdygvtPFgqsRGKEKIYNEINAYNDINRIISEKYNVMYF 173
Cdd:COG2755 81 NDLLRGLgvSPEEFRANLEALIDRLRAAGPGAR-VVLVTPP-----PR---LRPNYLNERIEAYNAAIRELAAEYGVPLV 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1251812611 174 NITDISRRAENDLTLLANDKLHPSEKMYAEWVNLM 208
Cdd:COG2755 152 DLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAV 186
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
30-202 |
6.54e-19 |
|
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: 80.28 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 30 ALGDSYTIGESIE-VEDSYPNQLKEKID---IIDSLKIIAKTGWTTDELIDT-LNNSNLKQYDIVSLLIGVNNQFRGYSI 104
Cdd:pfam13472 1 ALGDSITAGYGATgGDRSYPGWLARLLArrlGADVVNNLGISGATTRLDLLErLDDVLRLKPDLVVILLGTNDLGRGVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 105 DNYKVEFENLLAKTIRYSNNKKnvfVLSIPDYGVTPFGQSRGKEkIYNEINAYNDINRIISEKYNVMYFNITDISRRAEN 184
Cdd:pfam13472 81 ARAAANLEALIDALRAAGPDAR---VLLIGPLPVGPPPPLDERR-LNARIAEYNAAIREVAAERGVPYVDLWDALRDDGG 156
|
170
....*....|....*....
gi 1251812611 185 DL-TLLANDKLHPSEKMYA 202
Cdd:pfam13472 157 WLpDLLADDGLHPNAAGYR 175
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
28-208 |
3.85e-12 |
|
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: 62.43 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 28 YLALGDSYTIGESIEVEDSYP----NQLKEKIDIIDSLKIIAKTGWTTDELIDTLNNS---NLKQYDIVSLLIGVNNQFR 100
Cdd:cd00229 1 ILVIGDSITAGYGASSGSTFYslllYLLLLAGGPGVEVINLGVSGATTADALRRLGLRlalLKDKPDLVIIELGTNDLGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 101 G--YSIDNYKVEFENLLaKTIRYSNNKKNVFVLSIPDYGVTPFGQSRGKEKiYNEINAynDINRIISEKYNVMYFNITDI 178
Cdd:cd00229 81 GgdTSIDEFKANLEELL-DALRERAPGAKVILITPPPPPPREGLLGRALPR-YNEAIK--AVAAENPAPSGVDLVDLAAL 156
|
170 180 190
....*....|....*....|....*....|
gi 1251812611 179 SRRAENDLtlLANDKLHPSEKMYAEWVNLM 208
Cdd:cd00229 157 LGDEDKSL--YSPDGIHPNPAGHKLIAEAL 184
|
|
| SGNH_hydrolase_YpmR_like |
cd04506 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
28-201 |
8.77e-10 |
|
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: 56.10 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 28 YLALGDSYTIGESIEVEDSY-----PNQLKEKIDIIDSLKIIAKTGWTTDELIDTLNNS----NLKQYDIVSLLIGVNNQ 98
Cdd:cd04506 2 IVALGDSLTEGVGDETGKGGyvgrlDKLIETKTVKKVTVQNFGVSGDRSDQLLKRLKTKkvqkELKKADVITITIGGNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 99 FRGYSIDN--------------YKVEFENLLaKTIRYSNNKKNVFVLSIpdYgvTPFGQSRGKEKIYNE-INAYNDINRI 163
Cdd:cd04506 82 MQVLEKNFlsldvedfkkaeetYQNNLKKIF-KEIRKLNPDAPIFLVGL--Y--NPFYVYFPNITEINDiVNDWNEASQK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1251812611 164 ISEKYNVMYF-NITDISRRAENDLtLLANDKLHPSEKMY 201
Cdd:cd04506 157 LASQYKNAYFvPIFDLFSDGQNKY-LLTSDHFHPNDKGY 194
|
|
| FeeA_FeeB_like |
cd01836 |
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ... |
24-214 |
2.79e-08 |
|
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: 51.88 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 24 PSLSYLALGDSYTIG---ESIE--VEDSYPNQLKEKIDIIDSLKIIAKTGWTTDELIDTLNNSNLKQYDIVSLLIGVNNQ 98
Cdd:cd01836 1 PPLRLLVLGDSTAAGvgvETQDqaLAGQLARGLAAITGRGVRWRLFAKTGATSADLLRQLAPLPETRFDVAVISIGVNDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 99 FRGYSIDNYKVEFENLLaKTIRYSNNKKNVFVLSIPDYGVTP--------FGQSRGkeKIYNEINAyndinRIISEKYNV 170
Cdd:cd01836 81 THLTSIARWRKQLAELV-DALRAKFPGARVVVTAVPPLGRFPalpqplrwLLGRRA--RLLNRALE-----RLASEAPRV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1251812611 171 MYFNITDISRRAendltLLANDKLHPSEKMYAEWVNLMKLQILD 214
Cdd:cd01836 153 TLLPATGPLFPA-----LFASDGFHPSAAGYAVWAEALAPAIAA 191
|
|
| sialate_O-acetylesterase_like2 |
cd01828 |
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ... |
68-209 |
1.79e-06 |
|
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: 46.50 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 68 GWTTDELIDTLNNSNLKQYDIVSLLIGVNNQFRGYSIDNYKVEFENLLAKTIRYSNNKKnVFVLSIPdygvtPFGQsrgK 147
Cdd:cd01828 31 GDTTRGLLARLDEDVALQPKAIFIMIGINDLAQGTSDEDIVANYRTILEKLRKHFPNIK-IVVQSIL-----PVGE---L 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251812611 148 EKIYNE-INAYNDINRIISEKYNVMYFNI----TDISRRAENDLTllaNDKLHPSEKMYAEWVNLMK 209
Cdd:cd01828 102 KSIPNEqIEELNRQLAQLAQQEGVTFLDLwavfTNADGDLKNEFT---TDGLHLNAKGYAVWAAALQ 165
|
|
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
29-205 |
1.13e-05 |
|
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: 44.04 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 29 LALGDSYTIGESIEVEDSYPNQLKEKIDIID-SLKII--AKTGWTTDELIDTLNNSnLKQY--DIVSLLIGVNNQFRGYS 103
Cdd:cd01822 4 LALGDSLTAGYGLPPEEGWPALLQKRLDARGiDVTVInaGVSGDTTAGGLARLPAL-LAQHkpDLVILELGGNDGLRGIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 104 IDnykvEFENLLAKTIRYSNNKK-NVFVLSI---PDYGvtpfgqsrgkeKIYNEinAYNDINRIISEKYNV--MYFNITD 177
Cdd:cd01822 83 PD----QTRANLRQMIETAQARGaPVLLVGMqapPNYG-----------PRYTR--RFAAIYPELAEEYGVplVPFFLEG 145
|
170 180 190
....*....|....*....|....*....|.
gi 1251812611 178 ISRRAEndltLLANDKLHPSEKMY---AEWV 205
Cdd:cd01822 146 VAGDPE----LMQSDGIHPNAEGQpiiAENV 172
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
28-208 |
1.87e-05 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 44.10 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 28 YLALGDSYT--IGESIEVEDSYPNQLK----EKIDIIDSLKII----AKTGWTTDELIDTL--------NNSNLKQYDIV 89
Cdd:pfam00657 1 IVAFGDSLTdgGGDGPGGRFSWGDLLAdflaRKLGVPGSGYNHganfAIGGATIEDLPIQLeqllrlisDVKDQAKPDLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 90 SLLIGVNNQFRGYSIDNYKVEF-----ENLLAKTIRYSNNKKNVFVLSIPDYGVTPFgqsRGKEKIYNEINAY--NDINR 162
Cdd:pfam00657 81 TIFIGANDLCNFLSSPARSKKRvpdllDELRANLPQLGLGARKFWVHGLGPLGCTPP---KGCYELYNALAEEynERLNE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251812611 163 IIS------EKYNVMYFNITD----ISRRAENDLTllaNDKLHPSEKMYAEWVNLM 208
Cdd:pfam00657 158 LVNslaaaaEDANVVYVDIYGfedpTDPCCGIGLE---PDGLHPSEKGYKAVAEAI 210
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
47-198 |
1.16e-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: 238872 Cd Length: 191 Bit Score: 41.51 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 47 YPNQlkeKIDIIDSlkiiaktGWTTDELIDTLNNSNL----KQYDIVSLLIGVNNQFRGY----SIDNYKVEFENLLAKT 118
Cdd:cd01834 29 YPEL---KLTFRNL-------GWSGDTVSDLAARRDRdvlpAKPDVVSIMFGINDSFRGFddpvGLEKFKTNLRRLIDRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 119 IRYSNNKKnvFVLsipdygVTPF-----GQSRGKEKIYNE-INAYNDINRIISEKYNV----MYFNITDISRRAENdlTL 188
Cdd:cd01834 99 KNKESAPR--IVL------VSPIayeanEDPLPDGAEYNAnLAAYADAVRELAAENGVafvdLFTPMKEAFQKAGE--AV 168
|
170
....*....|
gi 1251812611 189 LANDKLHPSE 198
Cdd:cd01834 169 LTVDGVHPNE 178
|
|
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
68-204 |
7.58e-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: 38.76 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251812611 68 GWTTDElIDTLNNSNLKQY--DIVSLLIGVNNQFRGYSIDNYKVEFENLLAKTIRYSNNKKnVFVLSIPdygvtPFGQSR 145
Cdd:cd01833 22 GYLIDQ-IAAAAADWVLAAkpDVVLLHLGTNDLVLNRDPDTAPDRLRALIDQMRAANPDVK-IIVATLI-----PTTDAS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251812611 146 GKekiyNEINAYND-INRIISEKYNV--------MYFNITDISRRAendltllanDKLHPS----EKMYAEW 204
Cdd:cd01833 95 GN----ARIAEYNAaIPGVVADLRTAgspvvlvdMSTGYTTADDLY---------DGLHPNdqgyKKMADAW 153
|
|
| |
