|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
23-255 |
1.05e-20 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 86.98 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 23 TAKPTVVLVHGAFADSSSWNGVTQILQkDGYNVVA----------AANPLRSVSTDAAYVSSVVNNIK-GPVVLVGHSYG 91
Cdd:COG0596 21 PDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIApdlrghgrsdKPAGGYTLDDLADDLAALLDALGlERVVLVGHSMG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 92 GQVITNAALD-TNNVKSLVYVAAFApdageaaadlagkfpggtlgqalaapvkladgsvdlsidqAKFHQQFAHDVSAKE 170
Cdd:COG0596 100 GMVALELAARhPERVAGLVLVDEVL----------------------------------------AALAEPLRRPGLAPE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 171 AALMAAgqrpiteAALTEKSGAPAWKKL--PSYFIYGDGDKNIPAQGLRFMAERAGSKHTVVIKGASHVVMVSHPQDVAT 248
Cdd:COG0596 140 ALAALL-------RALARTDLRERLARItvPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212
|
....*..
gi 1541711573 249 LIEEAAK 255
Cdd:COG0596 213 ALRDFLA 219
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
26-243 |
1.53e-14 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 71.00 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 26 PTVVLVHGAFADSSSWNGVTQILQKDGYNVVA----------AANPLRSVSTDAayVSSVVNNIK-----GPVVLVGHSY 90
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIAldlrgfgkssRPKAQDDYRTDD--LAEDLEYILealglEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 91 GGQVITNAALD-TNNVKSLVYVAAFAPDAGEAAADL--AGKFPGG-----------TLGQALAAPVKLADGSVDLSIDQA 156
Cdd:pfam00561 79 GGLIALAYAAKyPDRVKALVLLGALDPPHELDEADRfiLALFPGFfdgfvadfapnPLGRLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 157 KFHQQFAHDVSAKEAALMAAGQRPITEAALTEKSGAPAWKKLPSYFIYGDGDKNIPAQGLRFMAERAGSKHTVVIKGASH 236
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238
|
....*..
gi 1541711573 237 VVMVSHP 243
Cdd:pfam00561 239 FAFLEGP 245
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
23-94 |
1.44e-03 |
|
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238363 [Multi-domain] Cd Length: 275 Bit Score: 39.15 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 23 TAKPTVVLVHGaFADS--SSWN-GVTQILQKDG-YNVVA-------------AANPLRSVstdAAYVSSVVNNIK----- 80
Cdd:cd00707 34 PSRPTRFIIHG-WTSSgeESWIsDLRKAYLSRGdYNVIVvdwgrganpnypqAVNNTRVV---GAELAKFLDFLVdntgl 109
|
90
....*....|....*.
gi 1541711573 81 --GPVVLVGHSYGGQV 94
Cdd:cd00707 110 slENVHLIGHSLGAHV 125
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
23-255 |
1.05e-20 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 86.98 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 23 TAKPTVVLVHGAFADSSSWNGVTQILQkDGYNVVA----------AANPLRSVSTDAAYVSSVVNNIK-GPVVLVGHSYG 91
Cdd:COG0596 21 PDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIApdlrghgrsdKPAGGYTLDDLADDLAALLDALGlERVVLVGHSMG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 92 GQVITNAALD-TNNVKSLVYVAAFApdageaaadlagkfpggtlgqalaapvkladgsvdlsidqAKFHQQFAHDVSAKE 170
Cdd:COG0596 100 GMVALELAARhPERVAGLVLVDEVL----------------------------------------AALAEPLRRPGLAPE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 171 AALMAAgqrpiteAALTEKSGAPAWKKL--PSYFIYGDGDKNIPAQGLRFMAERAGSKHTVVIKGASHVVMVSHPQDVAT 248
Cdd:COG0596 140 ALAALL-------RALARTDLRERLARItvPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212
|
....*..
gi 1541711573 249 LIEEAAK 255
Cdd:COG0596 213 ALRDFLA 219
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
26-243 |
1.53e-14 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 71.00 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 26 PTVVLVHGAFADSSSWNGVTQILQKDGYNVVA----------AANPLRSVSTDAayVSSVVNNIK-----GPVVLVGHSY 90
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIAldlrgfgkssRPKAQDDYRTDD--LAEDLEYILealglEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 91 GGQVITNAALD-TNNVKSLVYVAAFAPDAGEAAADL--AGKFPGG-----------TLGQALAAPVKLADGSVDLSIDQA 156
Cdd:pfam00561 79 GGLIALAYAAKyPDRVKALVLLGALDPPHELDEADRfiLALFPGFfdgfvadfapnPLGRLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 157 KFHQQFAHDVSAKEAALMAAGQRPITEAALTEKSGAPAWKKLPSYFIYGDGDKNIPAQGLRFMAERAGSKHTVVIKGASH 236
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238
|
....*..
gi 1541711573 237 VVMVSHP 243
Cdd:pfam00561 239 FAFLEGP 245
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
28-247 |
5.06e-13 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 65.96 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 28 VVLVHGAFADSSSWNGvtqiLQKDGYNVVAAANP-----------LRSVSTDAAYVSSVVNniKGPVVLVGHSYGGQVIT 96
Cdd:pfam12697 1 VVLVHGAGLSAAPLAA----LLAAGVAVLAPDLPghgssspppldLADLADLAALLDELGA--ARPVVLVGHSLGGAVAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 97 NAALDTNNVKslVYVAAFAPDAGEAAAdlagkfpggtlgqALAAPVKLADGSVDLSIDQAKFHQQFAHDVSAKEAALMAA 176
Cdd:pfam12697 75 AAAAAALVVG--VLVAPLAAPPGLLAA-------------LLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541711573 177 GQRPITEAALTEKSGAPAWKKLPS-YFIYGDGDKNIPAQGLRFMAERAGsKHTVVIKGASHVVMvSHPQDVA 247
Cdd:pfam12697 140 LARLAALLAALALLPLAAWRDLPVpVLVLAEEDRLVPELAQRLLAALAG-ARLVVLPGAGHLPL-DDPEEVA 209
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
21-245 |
2.05e-11 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 61.56 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 21 AETAKPTVVLVHGAFADSSSWNGVTQILQKDGYNVVA--------AANPLRSVSTDAAYVS---SVVNNIK----GPVVL 85
Cdd:COG2267 24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAfdlrghgrSDGPRGHVDSFDDYVDdlrAALDALRarpgLPVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 86 VGHSYGGQVITNAALDTNN-VKSLVyvaafapdageaaadlagkfpggtlgqaLAAPVKLADgsvdlsidqakfhqqfah 164
Cdd:COG2267 104 LGHSMGGLIALLYAARYPDrVAGLV----------------------------LLAPAYRAD------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 165 dvsakeaALMAAGQRPITEAALTEksGAPAWkKLPSYFIYGDGDKNIPAQGLRFMAERAGS-KHTVVIKGASHVVMVSHP 243
Cdd:COG2267 138 -------PLLGPSARWLRALRLAE--ALARI-DVPVLVLHGGADRVVPPEAARRLAARLSPdVELVLLPGARHELLNEPA 207
|
..
gi 1541711573 244 QD 245
Cdd:COG2267 208 RE 209
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
21-113 |
2.97e-11 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 58.69 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 21 AETAKPTVVLVHGAFADSSSWNGVTQILQKDGYNVVAAANPLRSVSTD--AAYVSSVVNNIK-----GPVVLVGHSYGGQ 93
Cdd:COG1075 1 YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEdsAEQLAAFVDAVLaatgaEKVDLVGHSMGGL 80
|
90 100
....*....|....*....|...
gi 1541711573 94 VITNAALD---TNNVKSLVYVAA 113
Cdd:COG1075 81 VARYYLKRlggAAKVARVVTLGT 103
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
24-236 |
1.70e-08 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 53.76 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 24 AKPTVVLVHGaFADSSSW-NGVTQILQKDGYNVVA-------AANPLRS-VSTDAAYV---SSVVNNIK-----GPVVLV 86
Cdd:pfam12146 3 PRAVVVLVHG-LGEHSGRyAHLADALAAQGFAVYAydhrghgRSDGKRGhVPSFDDYVddlDTFVDKIReehpgLPLFLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 87 GHSYGGQVITNAALDT-NNVKSLVYVA-AFAPDAGEA--AADLAGKFPGGTLGQALAAPVKLADgsvDLSIDQAkFHQQF 162
Cdd:pfam12146 82 GHSMGGLIAALYALRYpDKVDGLILSApALKIKPYLAppILKLLAKLLGKLFPRLRVPNNLLPD---SLSRDPE-VVAAY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541711573 163 AHD--VSAKEAALMAAGqrpITEAALTEKSGAPAWKkLPSYFIYGDGDKNIPAQGLRFMAERAGS--KHTVVIKGASH 236
Cdd:pfam12146 158 AADplVHGGISARTLYE---LLDAGERLLRRAAAIT-VPLLLLHGGADRVVDPAGSREFYERAGStdKTLKLYPGLYH 231
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
12-255 |
1.42e-05 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 44.93 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 12 TVLLSASAIAETAKPTVVLVHGAFADSSSWNGVTQILQKDGYNVVAAANP-----------------LRSVstDAAYvsS 74
Cdd:COG1647 2 KILGAEPFFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPghgtspedllkttwedwLEDV--EEAY--E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 75 VVNNIKGPVVLVGHSYGGQVITNAALDTNNVKSLVYVAA--FAPDAGEAAADLAGKFpggtlgqalaAPVKLADGSVDLS 152
Cdd:COG1647 78 ILKAGYDKVIVIGLSMGGLLALLLAARYPDVAGLVLLSPalKIDDPSAPLLPLLKYL----------ARSLRGIGSDIED 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 153 IDQAKFHQQFAHDVSAKE-AALMAAGQRPIteaalteksgaPAWKKlPSYFIYGDGDKNIPAQGLRFMAERAGS--KHTV 229
Cdd:COG1647 148 PEVAEYAYDRTPLRALAElQRLIREVRRDL-----------PKITA-PTLIIQSRKDEVVPPESARYIYERLGSpdKELV 215
|
250 260
....*....|....*....|....*.
gi 1541711573 230 VIKGASHVVMVSHpqDVATLIEEAAK 255
Cdd:COG1647 216 WLEDSGHVITLDK--DREEVAEEILD 239
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
19-247 |
1.96e-05 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 44.52 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 19 AIAETAKPTVVLVHGAFADSSSWNGVTQILQKDGYNVVA---------------AANPLRS-VSTDAAYVSSVVNNIKGP 82
Cdd:COG1073 31 AGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAfdyrgygesegepreEGSPERRdARAAVDYLRTLPGVDPER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 83 VVLVGHSYGGQVITNAALDTNNVKSLVYVAAFApDAGEAAADLAGKFPGGTLGQALAAPVkladgsvdlsidqakfhqqf 162
Cdd:COG1073 111 IGLLGISLGGGYALNAAATDPRVKAVILDSPFT-SLEDLAAQRAKEARGAYLPGVPYLPN-------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 163 ahdvsAKEAALMAAGQRPITEAALTeksgapawkKLPSYFIYGDGDKNIPAQGLRFMAERAGS-KHTVVIKGASHVVMVS 241
Cdd:COG1073 170 -----VRLASLLNDEFDPLAKIEKI---------SRPLLFIHGEKDEAVPFYMSEDLYEAAAEpKELLIVPGAGHVDLYD 235
|
....*.
gi 1541711573 242 HPQDVA 247
Cdd:COG1073 236 RPEEEY 241
|
|
| Abhydrolase_5 |
pfam12695 |
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ... |
28-120 |
2.27e-04 |
|
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase enzymes.
Pssm-ID: 315383 [Multi-domain] Cd Length: 164 Bit Score: 40.51 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 28 VVLVHGAFADSSSWNGVTQILQKDGYNVVAAANPLRSVSTDAAYVSSVV---NNIKGPVVlVGHSYGGQVITNAALDTNN 104
Cdd:pfam12695 2 LIFYPGAKVEPLSYAPLANKLAKSGYLVVLVKMPLNLAVLGPNRALSIIkahPKIQKWVV-GGHSLGGVMASRFAADNEL 80
|
90
....*....|....*.
gi 1541711573 105 VKSLVYVAAFaPDAGE 120
Cdd:pfam12695 81 IKGVVFLASY-PDKDS 95
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
25-252 |
2.89e-04 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 41.16 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 25 KPTVVLVHGAFADSS-SWNGVTQILQKDGYNVVAAANPLRSVST------DAAYVSSVVNNIK-------GPVVLVGHSY 90
Cdd:COG1506 23 YPVVVYVHGGPGSRDdSFLPLAQALASRGYAVLAPDYRGYGESAgdwggdEVDDVLAAIDYLAarpyvdpDRIGIYGHSY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 91 GGQVITNAALDTNNVkslvyVAAFAPDAG----EAAADLAGKFPGGTLGQALAAPVKLADGSVDLSIDQAKfhqqfahdv 166
Cdd:COG1506 103 GGYMALLAAARHPDR-----FKAAVALAGvsdlRSYYGTTREYTERLMGGPWEDPEAYAARSPLAYADKLK--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 167 sakeaalmaagqRPIteaalteksgapawkklpsYFIYGDGDKNIP-AQGLRF---MAERAGSKHTVVIKGASHVVMVSH 242
Cdd:COG1506 169 ------------TPL-------------------LLIHGEADDRVPpEQAERLyeaLKKAGKPVELLVYPGEGHGFSGAG 217
|
250
....*....|
gi 1541711573 243 PQDVATLIEE 252
Cdd:COG1506 218 APDYLERILD 227
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
23-94 |
1.44e-03 |
|
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238363 [Multi-domain] Cd Length: 275 Bit Score: 39.15 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 23 TAKPTVVLVHGaFADS--SSWN-GVTQILQKDG-YNVVA-------------AANPLRSVstdAAYVSSVVNNIK----- 80
Cdd:cd00707 34 PSRPTRFIIHG-WTSSgeESWIsDLRKAYLSRGdYNVIVvdwgrganpnypqAVNNTRVV---GAELAKFLDFLVdntgl 109
|
90
....*....|....*.
gi 1541711573 81 --GPVVLVGHSYGGQV 94
Cdd:cd00707 110 slENVHLIGHSLGAHV 125
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
13-116 |
7.09e-03 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 37.05 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541711573 13 VLLSASAIAETAKPTVVLVHGAFADSSSW--NGVTQILQKDGYNVVAA--------ANPLRSV--STDAAYVSSVVNNIK 80
Cdd:COG0429 49 VDLDWSDPPAPSKPLVVLLHGLEGSSDSHyaRGLARALYARGWDVVRLnfrgcggePNLLPRLyhSGDTEDLVWVLAHLR 128
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1541711573 81 -----GPVVLVGHSYGGQVITNAALDT-NNVKSLVYVAAFAP 116
Cdd:COG0429 129 arypyAPLYAVGFSLGGNLLLKYLGEQgDDAPPLKAAVAVSP 170
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
82-135 |
8.05e-03 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 36.79 E-value: 8.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541711573 82 PVVLVGHSYGGQVITnAALDTNNVKSLVYVAA-------FAPD-----------AGEAAADLAGKFPGGTLG 135
Cdd:COG4757 108 PLLLVGHSLGGQLLG-LAPNAERVDRLVTVASgsgywrdYPPRrrlkvllfwhlLGPLLTRLLGYFPGRRLG 178
|
|
| |
