|
Name |
Accession |
Description |
Interval |
E-value |
| XynE_like |
cd01830 |
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ... |
230-432 |
5.15e-110 |
|
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: 322.27 E-value: 5.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 230 SLVIIGNSITDGRGSGTNRQNRWPDILAERLIKNPPTSNTGVLNQGIGGNCVLRECLGPPAIERFDRDVLGQHGVRWLII 309
Cdd:cd01830 1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 310 LHGVNDIGQTGTKEEADQV-AEELIAAYERMIADAHAAGILVYGATILPFGNSFYYTEPGEAARQKVNEWIRSGGWFDAV 388
Cdd:cd01830 81 LEGVNDIGASGTDFAAAPVtAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1711019391 389 IDFDRLMRDPDDPRLLLKEFHTGDFLHPNEAGYRMMGDAVDLKL 432
Cdd:cd01830 161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
224-428 |
1.05e-35 |
|
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: 130.15 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 224 AQATAGSLVIIGNSITDGRGSGtnRQNRWPDILAERLIKNPPTsntgVLNQGIGGNCVLReclgppAIERFDRDVLgQHG 303
Cdd:COG2755 4 AAGKPLRIVALGDSITAGYGAS--RERGWPALLARRLAAADVR----VVNAGISGATTAD------LLARLDRDLL-ALK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 304 VRWLIILHGVNDIGQTGTKEeadqvAEELIAAYERMIADAHAAG--ILVYGATILPFGNSfyytEPGEAARQKVNEWIRS 381
Cdd:COG2755 71 PDLVVIELGTNDLLRGLGVS-----PEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRP----NYLNERIEAYNAAIRE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1711019391 382 ----GGWfdAVIDFDRLMRDPDDprllLKEFHTGDFLHPNEAGYRMMGDAV 428
Cdd:COG2755 142 laaeYGV--PLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
233-422 |
1.01e-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: 108.40 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 233 IIGNSITDGRGSgTNRQNRWPDILAERLIKNPPtsNTGVLNQGIGGNCVLRECLgppaiERFDRdvLGQHGVRWLIILHG 312
Cdd:pfam13472 1 ALGDSITAGYGA-TGGDRSYPGWLARLLARRLG--ADVVNNLGISGATTRLDLL-----ERLDD--VLRLKPDLVVILLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 313 VNDIGQTGTKEEADqvaeeliAAYERMIADAHAAG---ILVYGATILPFGNSFYYTEPGEAARQKVNEWIRS--GGWFDA 387
Cdd:pfam13472 71 TNDLGRGVSAARAA-------ANLEALIDALRAAGpdaRVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREvaAERGVP 143
|
170 180 190
....*....|....*....|....*....|....*
gi 1711019391 388 VIDFDRLMRDPDDPrllLKEFHTGDFLHPNEAGYR 422
Cdd:pfam13472 144 YVDLWDALRDDGGW---LPDLLADDGLHPNAAGYR 175
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| XynE_like |
cd01830 |
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ... |
230-432 |
5.15e-110 |
|
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: 322.27 E-value: 5.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 230 SLVIIGNSITDGRGSGTNRQNRWPDILAERLIKNPPTSNTGVLNQGIGGNCVLRECLGPPAIERFDRDVLGQHGVRWLII 309
Cdd:cd01830 1 SVVALGDSITDGRGSTPDANNRWPDLLAARLAARAGTRGIAVLNAGIGGNRLLADGLGPSALARFDRDVLSQPGVRTVII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 310 LHGVNDIGQTGTKEEADQV-AEELIAAYERMIADAHAAGILVYGATILPFGNSFYYTEPGEAARQKVNEWIRSGGWFDAV 388
Cdd:cd01830 81 LEGVNDIGASGTDFAAAPVtAEELIAGYRQLIRRAHARGIKVIGATITPFEGSGYYTPAREATRQAVNEWIRTSGAFDAV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1711019391 389 IDFDRLMRDPDDPRLLLKEFHTGDFLHPNEAGYRMMGDAVDLKL 432
Cdd:cd01830 161 VDFDAALRDPADPSRLRPAYDSGDHLHPNDAGYQAMADAVDLDL 204
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
224-428 |
1.05e-35 |
|
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: 130.15 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 224 AQATAGSLVIIGNSITDGRGSGtnRQNRWPDILAERLIKNPPTsntgVLNQGIGGNCVLReclgppAIERFDRDVLgQHG 303
Cdd:COG2755 4 AAGKPLRIVALGDSITAGYGAS--RERGWPALLARRLAAADVR----VVNAGISGATTAD------LLARLDRDLL-ALK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 304 VRWLIILHGVNDIGQTGTKEeadqvAEELIAAYERMIADAHAAG--ILVYGATILPFGNSfyytEPGEAARQKVNEWIRS 381
Cdd:COG2755 71 PDLVVIELGTNDLLRGLGVS-----PEEFRANLEALIDRLRAAGpgARVVLVTPPPRLRP----NYLNERIEAYNAAIRE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1711019391 382 ----GGWfdAVIDFDRLMRDPDDprllLKEFHTGDFLHPNEAGYRMMGDAV 428
Cdd:COG2755 142 laaeYGV--PLVDLYAALRDAGD----LPDLLTADGLHPNAAGYRLIAEAV 186
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
233-422 |
1.01e-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: 108.40 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 233 IIGNSITDGRGSgTNRQNRWPDILAERLIKNPPtsNTGVLNQGIGGNCVLRECLgppaiERFDRdvLGQHGVRWLIILHG 312
Cdd:pfam13472 1 ALGDSITAGYGA-TGGDRSYPGWLARLLARRLG--ADVVNNLGISGATTRLDLL-----ERLDD--VLRLKPDLVVILLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 313 VNDIGQTGTKEEADqvaeeliAAYERMIADAHAAG---ILVYGATILPFGNSFYYTEPGEAARQKVNEWIRS--GGWFDA 387
Cdd:pfam13472 71 TNDLGRGVSAARAA-------ANLEALIDALRAAGpdaRVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREvaAERGVP 143
|
170 180 190
....*....|....*....|....*....|....*
gi 1711019391 388 VIDFDRLMRDPDDPrllLKEFHTGDFLHPNEAGYR 422
Cdd:pfam13472 144 YVDLWDALRDDGGW---LPDLLADDGLHPNAAGYR 175
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
231-428 |
1.40e-23 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 98.03 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 231 LVIIGNSITDGRGSGTNRQNRWPDILAERLIKN---PPTSNTGVLNQGIGGNCVLRECLGPPAIERFDRDVLGQHGVRWL 307
Cdd:pfam00657 1 IVAFGDSLTDGGGDGPGGRFSWGDLLADFLARKlgvPGSGYNHGANFAIGGATIEDLPIQLEQLLRLISDVKDQAKPDLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 308 IILHGVNDIGQTG-----TKEEADQVAEELIAAYERMiaDAHAAGILVYGATIL----PFGNSFYYTEPGEAARQKVNEW 378
Cdd:pfam00657 81 TIFIGANDLCNFLssparSKKRVPDLLDELRANLPQL--GLGARKFWVHGLGPLgctpPKGCYELYNALAEEYNERLNEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1711019391 379 IRSGGWF---DAVIDFDrlMRDPDDPRLLLKEFHTG-DFLHPNEAGYRMMGDAV 428
Cdd:pfam00657 159 VNSLAAAaedANVVYVD--IYGFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
|
|
| SGNH_hydrolase_like_4 |
cd04501 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
231-432 |
5.18e-20 |
|
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: 87.00 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 231 LVIIGNSITDGRGSGTnrQNRWPDILAErliknppTSNTGVLNQGIGGNcVLRECLgppaiERFDRDVLGQHGvRWLIIL 310
Cdd:cd04501 3 VVCLGDSITYGYPVGP--EASWVNLLAE-------FLGKEVINRGINGD-TTSQML-----VRFYEDVIALKP-AVVIIM 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 311 HGVNDIGQTGTKEEADQVAEEliaayerMIADAHAAGILVYGATILPFgNSFYYTEPGEAARQKV---NEWIRS----GG 383
Cdd:cd04501 67 GGTNDIIVNTSLEMIKDNIRS-------MVELAEANGIKVILASPLPV-DDYPWKPQWLRPANKLkslNRWLKDyareNG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1711019391 384 WFdaVIDFDRLMRDPDDprLLLKEFHTGDFLHPNEAGYRMMGDAVDLKL 432
Cdd:cd04501 139 LL--FLDFYSPLLDERN--VGLKPGLLTDGLHPSREGYRVMAPLAEKAL 183
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
231-428 |
5.53e-16 |
|
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: 75.91 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 231 LVIIGNSITDGRGSGTNRQNRWPDILAERLIKNPPTSntgVLNQGIGGNCVLREclgppAIERFDRDVLGQHGVRWLIIL 310
Cdd:cd00229 1 ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGGPGVE---VINLGVSGATTADA-----LRRLGLRLALLKDKPDLVIIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 311 HGVNDIGqTGTKEEADQVAEELIAAYERMIADAHAAGILVYGATILPFGNSFYYTEPGE--AARQKVNEWIRSGGWFDaV 388
Cdd:cd00229 73 LGTNDLG-RGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRynEAIKAVAAENPAPSGVD-L 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1711019391 389 IDFDRLMRDPDdprlllKEFHTGDFLHPNEAGYRMMGDAV 428
Cdd:cd00229 151 VDLAALLGDED------KSLYSPDGIHPNPAGHKLIAEAL 184
|
|
| SGNH_hydrolase_like_2 |
cd01834 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
231-427 |
3.03e-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: 65.01 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 231 LVIIGNSITDGRGsgtnrqnrWPDILAERLIKNPPTSNTGVLNQGIGGNCVL-ReclgppaIERFDRDVLgQHGVRWLII 309
Cdd:cd01834 4 IVFIGNSITDRGG--------YVGYVETYLAARYPELKLTFRNLGWSGDTVSdL-------AARRDRDVL-PAKPDVVSI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 310 LHGVNDIGQTGtkeEADQVAEELIAAYERMIA----DAHAAGI-LVYGATILPFGNSFYYTEPGEAARQKVNEWIRS--- 381
Cdd:cd01834 68 MFGINDSFRGF---DDPVGLEKFKTNLRRLIDrlknKESAPRIvLVSPIAYEANEDPLPDGAEYNANLAAYADAVRElaa 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1711019391 382 -GGWfdAVIDFDRLMRDpdDPRLLLKEFHTGDFLHPNEAGYRMMGDA 427
Cdd:cd01834 145 eNGV--AFVDLFTPMKE--AFQKAGEAVLTVDGVHPNEAGHRALARL 187
|
|
| SGNH_hydrolase_like_6 |
cd01844 |
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ... |
231-432 |
3.65e-08 |
|
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: 238881 Cd Length: 177 Bit Score: 53.09 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 231 LVIIGNSITDGRGS---GTNrqnrWPDILAERLiknpptsNTGVLNQGIGGNCvlrecLGPPAIERFDRDVLGQhgvrwL 307
Cdd:cd01844 2 WVFYGTSISQGACAsrpGMA----WTAILARRL-------GLEVINLGFSGNA-----RLEPEVAELLRDVPAD-----L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 308 IILhgvnDIGQTGTKEEAdQVAEELIAAYeRMIADAH-AAGILVygatILPFGNSFYYTEPG-EAARQKVNEWIRSGgwf 385
Cdd:cd01844 61 YII----DCGPNIVGAEA-MVRERLGPLV-KGLRETHpDTPILL----VSPRYCPDAELTPGrGKLTLAVRRALREA--- 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1711019391 386 davidFDRLMRDPD------DPRLLLKEFH--TGDFLHPNEAGYRMMGDAVDLKL 432
Cdd:cd01844 128 -----FEKLRADGVpnlyylDGEELLGPDGeaLVDGIHPTDLGHMRYADRFEPVL 177
|
|
| SGNH_hydrolase_like_1 |
cd01832 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
230-428 |
5.55e-08 |
|
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: 52.66 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 230 SLVIIGNSITDGRGSGT--NRQNRWPDILAERLIKNPPTSntGVLNQGIGGNcVLRECLG---PPAIE-RFDrdvlgqhg 303
Cdd:cd01832 1 RYVALGDSITEGVGDPVpdGGYRGWADRLAAALAAADPGI--EYANLAVRGR-RTAQILAeqlPAALAlRPD-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 304 vrwLI-ILHGVNDIGQTGTkeEADQVAEELIAAYERmiADAHAAGILVYG----ATILPFGnsfyytePGEAARQKV-NE 377
Cdd:cd01832 70 ---LVtLLAGGNDILRPGT--DPDTYRADLEEAVRR--LRAAGARVVVFTipdpAVLEPFR-------RRVRARLAAyNA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1711019391 378 WIRS-GGWFDAV-IDFDRlMRDPDDPRLLlkefhTGDFLHPNEAGYRMMGDAV 428
Cdd:cd01832 136 VIRAvAARYGAVhVDLWE-HPEFADPRLW-----ASDRLHPSAAGHARLAALV 182
|
|
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
229-428 |
6.06e-07 |
|
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: 49.43 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 229 GSLVIIGNSITDGrgSGTNRQNRWPDILAERLIKNPPtsNTGVLNQGI------GGncvLReclgppaieRFDRdVLGQH 302
Cdd:cd01822 1 VTILALGDSLTAG--YGLPPEEGWPALLQKRLDARGI--DVTVINAGVsgdttaGG---LA---------RLPA-LLAQH 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 303 GVRWLIILHGVNDI--GQTgtkeeADQVAEELiaayERMIADAHAAGILV----------YGAtilPFGNSFYYTEPGEA 370
Cdd:cd01822 64 KPDLVILELGGNDGlrGIP-----PDQTRANL----RQMIETAQARGAPVllvgmqappnYGP---RYTRRFAAIYPELA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 371 ARQKVnewirsggwfdAVIDF--DRLMRDPDdprlLLKEfhtgDFLHPNEAGYRMMGDAV 428
Cdd:cd01822 132 EEYGV-----------PLVPFflEGVAGDPE----LMQS----DGIHPNAEGQPIIAENV 172
|
|
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
307-427 |
8.33e-07 |
|
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: 48.39 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 307 LIILH-GVNDIGQtgtKEEADQVAEELIAAYERMIADAHAAGILVygATILPFGNSfyytePGEAARQKVNEWIRsgGWF 385
Cdd:cd01833 43 VVLLHlGTNDLVL---NRDPDTAPDRLRALIDQMRAANPDVKIIV--ATLIPTTDA-----SGNARIAEYNAAIP--GVV 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1711019391 386 DAVIDFDRLMRDPDDPRLLLKEFHTGDFLHPNEAGYRMMGDA 427
Cdd:cd01833 111 ADLRTAGSPVVLVDMSTGYTTADDLYDGLHPNDQGYKKMADA 152
|
|
| SGNH_hydrolase_YpmR_like |
cd04506 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
353-428 |
5.32e-05 |
|
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: 44.16 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711019391 353 ATILPFG--NSFYYTEPGEAARQK-VNEWIRS----GGWFDAV--IDFDRLMRDPDDPRLLlkefhTGDFLHPNEAGYRM 423
Cdd:cd04506 122 APIFLVGlyNPFYVYFPNITEINDiVNDWNEAsqklASQYKNAyfVPIFDLFSDGQNKYLL-----TSDHFHPNDKGYQL 196
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....*
gi 1711019391 424 MGDAV 428
Cdd:cd04506 197 IADRV 201
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