|
Name |
Accession |
Description |
Interval |
E-value |
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1-307 |
1.90e-34 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 125.11 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 1 MALQEIEFTSHNGRdAIQAWAYEPVGTPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADA 80
Cdd:COG2267 1 MTRRLVTLPTRDGL-RLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 81 GDnaaevVISDELTLQQQLAGQfDDLPWVVFGHSWGSMIARAMATRPGTRLDGLALCGivaqPRgfettldhktlakaMA 160
Cdd:COG2267 80 DD-----YVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA----PA--------------YR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 161 TAPTDPAPEALVAQMfdgfadrlseddgptgwvarskevvadhgkdkfnnfgapmstRFLQGLADIyamangdsfyatmp 240
Cdd:COG2267 136 ADPLLGPSARWLRAL------------------------------------------RLAEALARI-------------- 159
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6KHM_Z 241 NIPIVLFAGSEDPAGDfgtgVKAVAERLRRDGHNVELHLYDGLRHEVHNEPEsRADVESSLVTFVDR 307
Cdd:COG2267 160 DVPVLVLHGGADRVVP----PEAARRLAARLSPDVELVLLPGARHELLNEPA-REEVLAAILAWLER 221
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
28-292 |
4.02e-33 |
|
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: 121.94 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 28 PTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADAGDnaaevVISDELTLQQQLAGQFDDLP 107
Cdd:pfam12146 3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDD-----YVDDLDTFVDKIREEHPGLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 108 WVVFGHSWGSMIARAMATRPGTRLDGLALCGIVAQPRgfettldhktlakamatAPTDPAPEALVAQMFDGFADRLS-ED 186
Cdd:pfam12146 78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIK-----------------PYLAPPILKLLAKLLGKLFPRLRvPN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 187 DGPTGWVARSKEVVADHGKDKFNNFGapMSTRFLQGLADI--YAMANGDSFyatmpNIPIVLFAGSEDPAGDFGtGVKAV 264
Cdd:pfam12146 141 NLLPDSLSRDPEVVAAYAADPLVHGG--ISARTLYELLDAgeRLLRRAAAI-----TVPLLLLHGGADRVVDPA-GSREF 212
|
250 260
....*....|....*....|....*...
6KHM_Z 265 AERLRRDghNVELHLYDGLRHEVHNEPE 292
Cdd:pfam12146 213 YERAGST--DKTLKLYPGLYHELLNEPD 238
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
20-305 |
1.06e-09 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 58.36 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 20 WAYEPVgtPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADAGdnaaeVVISDELTLQQQL 99
Cdd:PHA02857 18 WKPITY--PKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFG-----VYVRDVVQHVVTI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 100 AGQFDDLPWVVFGHSWGSMIARAMATRPGTRLDGLalcgIVAQPrgfettldhktlakaMATAPTDPAPEALVAQMFDGF 179
Cdd:PHA02857 91 KSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAM----ILMSP---------------LVNAEAVPRLNLLAAKLMGIF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 180 ADRLSEDDGPTGWVARSKEVVADHGKDKFNNfGAPMSTRFLQgladiYAMANGDSFYATMPN--IPIVLFAGSEDPAGDf 257
Cdd:PHA02857 152 YPNKIVGKLCPESVSRDMDEVYKYQYDPLVN-HEKIKAGFAS-----QVLKATNKVRKIIPKikTPILILQGTNNEISD- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
6KHM_Z 258 gtgVKAVAERLRRDGHNVELHLYDGLRHEVHNEPES-RADVESSLVTFV 305
Cdd:PHA02857 225 ---VSGAYYFMQHANCNREIKIYEGAKHHLHKETDEvKKSVMKEIETWI 270
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
229-305 |
2.79e-04 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 41.38 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 229 MANGDSFYATMPNIPIVLFAGsedpagdfGTG---VKAVAERLRRDGHNVELHLYDGLRHE----VHNEPESRADvESSL 301
Cdd:cd06189 86 GPLGDFFLREDSDRPLILIAG--------GTGfapIKSILEHLLAQGSKRPIHLYWGARTEedlyLDELLEAWAE-AHPN 156
|
....
6KHM_Z 302 VTFV 305
Cdd:cd06189 157 FTYV 160
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1-307 |
1.90e-34 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 125.11 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 1 MALQEIEFTSHNGRdAIQAWAYEPVGTPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADA 80
Cdd:COG2267 1 MTRRLVTLPTRDGL-RLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 81 GDnaaevVISDELTLQQQLAGQfDDLPWVVFGHSWGSMIARAMATRPGTRLDGLALCGivaqPRgfettldhktlakaMA 160
Cdd:COG2267 80 DD-----YVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA----PA--------------YR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 161 TAPTDPAPEALVAQMfdgfadrlseddgptgwvarskevvadhgkdkfnnfgapmstRFLQGLADIyamangdsfyatmp 240
Cdd:COG2267 136 ADPLLGPSARWLRAL------------------------------------------RLAEALARI-------------- 159
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6KHM_Z 241 NIPIVLFAGSEDPAGDfgtgVKAVAERLRRDGHNVELHLYDGLRHEVHNEPEsRADVESSLVTFVDR 307
Cdd:COG2267 160 DVPVLVLHGGADRVVP----PEAARRLAARLSPDVELVLLPGARHELLNEPA-REEVLAAILAWLER 221
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
28-292 |
4.02e-33 |
|
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: 121.94 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 28 PTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADAGDnaaevVISDELTLQQQLAGQFDDLP 107
Cdd:pfam12146 3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDD-----YVDDLDTFVDKIREEHPGLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 108 WVVFGHSWGSMIARAMATRPGTRLDGLALCGIVAQPRgfettldhktlakamatAPTDPAPEALVAQMFDGFADRLS-ED 186
Cdd:pfam12146 78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIK-----------------PYLAPPILKLLAKLLGKLFPRLRvPN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 187 DGPTGWVARSKEVVADHGKDKFNNFGapMSTRFLQGLADI--YAMANGDSFyatmpNIPIVLFAGSEDPAGDFGtGVKAV 264
Cdd:pfam12146 141 NLLPDSLSRDPEVVAAYAADPLVHGG--ISARTLYELLDAgeRLLRRAAAI-----TVPLLLLHGGADRVVDPA-GSREF 212
|
250 260
....*....|....*....|....*...
6KHM_Z 265 AERLRRDghNVELHLYDGLRHEVHNEPE 292
Cdd:pfam12146 213 YERAGST--DKTLKLYPGLYHELLNEPD 238
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
34-288 |
2.58e-13 |
|
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: 68.30 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 34 IIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGrtamQSGVWADAGDNAAEVVISDELTLQQQLAGQfddlPWVVFGH 113
Cdd:pfam00561 5 LLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFG----KSSRPKAQDDYRTDDLAEDLEYILEALGLE----KVNLVGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 114 SWGSMIARAMATRPGTRLDGLALCGIVAQPRGFETTLDHktLAKAMATAPTDPAPEALVAQMFDGFADRLSEDDGPTGWV 193
Cdd:pfam00561 77 SMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRF--ILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 194 ARSKEVVADHGKDKFNNFGAPMSTR--FLQGLADIYAMangdsFYATMPNIPIVLFAGSEDPAGDfgtgvKAVAERLRRD 271
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGAllFIETWSTELRA-----KFLGRLDEPTLIIWGDQDPLVP-----PQALEKLAQL 224
|
250
....*....|....*..
6KHM_Z 272 GHNVELHLYDGLRHEVH 288
Cdd:pfam00561 225 FPNARLVVIPDAGHFAF 241
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
21-194 |
2.33e-10 |
|
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: 59.63 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 21 AYEPVGTPTAVVQIIHGLGEHSRRYLHMIsALLDAGFVVIADDHAGHGRTAMQSGVWaDAGDNAAEVVisdeltlqqQLA 100
Cdd:COG0596 15 HYREAGPDGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGY-TLDDLADDLA---------ALL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 101 GQFDDLPWVVFGHSWGSMIARAMATRPGTRLDGLALCGIVAQprgfettldhkTLAKAMATAPTDPAP--EALVAQMFDG 178
Cdd:COG0596 84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRRPGLAPEAlaALLRALARTD 152
|
170
....*....|....*.
6KHM_Z 179 FADRLSEDDGPTGWVA 194
Cdd:COG0596 153 LRERLARITVPTLVIW 168
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
20-305 |
1.06e-09 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 58.36 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 20 WAYEPVgtPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADAGdnaaeVVISDELTLQQQL 99
Cdd:PHA02857 18 WKPITY--PKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFG-----VYVRDVVQHVVTI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 100 AGQFDDLPWVVFGHSWGSMIARAMATRPGTRLDGLalcgIVAQPrgfettldhktlakaMATAPTDPAPEALVAQMFDGF 179
Cdd:PHA02857 91 KSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAM----ILMSP---------------LVNAEAVPRLNLLAAKLMGIF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 180 ADRLSEDDGPTGWVARSKEVVADHGKDKFNNfGAPMSTRFLQgladiYAMANGDSFYATMPN--IPIVLFAGSEDPAGDf 257
Cdd:PHA02857 152 YPNKIVGKLCPESVSRDMDEVYKYQYDPLVN-HEKIKAGFAS-----QVLKATNKVRKIIPKikTPILILQGTNNEISD- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
6KHM_Z 258 gtgVKAVAERLRRDGHNVELHLYDGLRHEVHNEPES-RADVESSLVTFV 305
Cdd:PHA02857 225 ---VSGAYYFMQHANCNREIKIYEGAKHHLHKETDEvKKSVMKEIETWI 270
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
7-183 |
5.49e-09 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 55.79 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 7 EFTSHNGRDaIQAWAYEPVGT-PTAVVQIIHGlGEHSR--RYLHMISALLDAGFVVIADDHAGHGRTAMQSGV--WADAG 81
Cdd:COG1506 1 TFKSADGTT-LPGWLYLPADGkKYPVVVYVHG-GPGSRddSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGdeVDDVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 82 DnAAEVVISDeltlqqqlaGQFDDLPWVVFGHSWGSMIARAMATRPGTRLDGLALCGIVAQPRGFETTLDHktLAKAMAT 161
Cdd:COG1506 79 A-AIDYLAAR---------PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTRE--YTERLMG 146
|
170 180
....*....|....*....|..
6KHM_Z 162 APTDPaPEALVAQMFDGFADRL 183
Cdd:COG1506 147 GPWED-PEAYAARSPLAYADKL 167
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
4-136 |
2.63e-08 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 54.12 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 4 QEIEFTSHNGRdAIQAWAYEPVGTPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGV-----WA 78
Cdd:COG4757 8 ESVTITAADGY-PLAARLFPPAGPPRAVVLINPATGVPQRFYRPFARYLAERGFAVLTYDYRGIGLSRPGSLRgfdagYR 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
6KHM_Z 79 DAGDNAAEVVIsdeltlqQQLAGQFDDLPWVVFGHSWGSMIArAMATRPGtRLDGLAL 136
Cdd:COG4757 87 DWGELDLPAVL-------DALRARFPGLPLLLVGHSLGGQLL-GLAPNAE-RVDRLVT 135
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
14-136 |
1.39e-06 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 49.51 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 14 RDAIQAWAYEPV-GTPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWAdagdnAAEVVISDE 92
Cdd:PLN02652 120 RNALFCRSWAPAaGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVP-----SLDYVVEDT 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
6KHM_Z 93 LTLQQQLAGQFDDLPWVVFGHSWGSMIARAMATRPGTR--LDGLAL 136
Cdd:PLN02652 195 EAFLEKIRSENPGVPCFLFGHSTGGAVVLKAASYPSIEdkLEGIVL 240
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
1-136 |
4.45e-06 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 47.22 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 1 MALQEIEFTSHNGRDaIQAWAYEPVGT--PTAVVQIIHGLG---EHSRRYLHMisaLLDAGFVVIADDHAGHGRTamqSG 75
Cdd:COG1073 8 VNKEDVTFKSRDGIK-LAGDLYLPAGAskKYPAVVVAHGNGgvkEQRALYAQR---LAELGFNVLAFDYRGYGES---EG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
6KHM_Z 76 VWADAGD---NAAEVVISdelTLQQQLAGQFDDLpwVVFGHS-WGSMIARAMATRPgtRLDGLAL 136
Cdd:COG1073 81 EPREEGSperRDARAAVD---YLRTLPGVDPERI--GLLGISlGGGYALNAAATDP--RVKAVIL 138
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
24-124 |
2.17e-04 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 42.40 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 24 PVGTPTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADDHAGHGRTAMQSGVWADAGDNAAEVVIS---------DELT 94
Cdd:COG4188 57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAADLSAALDGLADALDPEELWErpldlsfvlDQLL 136
|
90 100 110
....*....|....*....|....*....|....
6KHM_Z 95 LQQQLAGQFD---DLPWV-VFGHSWGSMIARAMA 124
Cdd:COG4188 137 ALNKSDPPLAgrlDLDRIgVIGHSLGGYTALALA 170
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
229-305 |
2.79e-04 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 41.38 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 229 MANGDSFYATMPNIPIVLFAGsedpagdfGTG---VKAVAERLRRDGHNVELHLYDGLRHE----VHNEPESRADvESSL 301
Cdd:cd06189 86 GPLGDFFLREDSDRPLILIAG--------GTGfapIKSILEHLLAQGSKRPIHLYWGARTEedlyLDELLEAWAE-AHPN 156
|
....
6KHM_Z 302 VTFV 305
Cdd:cd06189 157 FTYV 160
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
1-135 |
8.61e-04 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 39.95 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 1 MALQEIEFTSHNGrDAIQAWAYEPVGT-PTAVVQIIHGLGEHSRRYLHMISALLDAGFVVIADD-HAGHGRTAMQSGVWA 78
Cdd:COG0412 1 MTTETVTIPTPDG-VTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDlYGRGGPGDDPDEARA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
6KHM_Z 79 DAGDNAAEVVISDELTLQQQLAGQ--FDDLPWVVFGHSWGSMIARAMATRpGTRLDGLA 135
Cdd:COG0412 80 LMGALDPELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAAR-GPDLAAAV 137
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
34-292 |
1.27e-03 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 39.38 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 34 IIHGLGEHSRRylhmISALLDAGFVVIADDHAGHGRTAMQSGVWADAGDnaaevvisdeltLQQQLAGQFDDLPWVVFGH 113
Cdd:pfam12697 3 LVHGAGLSAAP----LAALLAAGVAVLAPDLPGHGSSSPPPLDLADLAD------------LAALLDELGAARPVVLVGH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 114 SWGSMIARAMAtrPGTRLDGLALCGIVAQPRGFETTLDHKTLAKAMATAPTDPAPEALVAQMFDGFADRLSEDdgptgwv 193
Cdd:pfam12697 67 SLGGAVALAAA--AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 194 arskevvadhgkdkfnnfgapmstRFLQGLADIYAMANGDSFYATMPNIPIVLFAGSEDPAgdfgtgVKAVAERLRRDGH 273
Cdd:pfam12697 138 ------------------------AALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRL------VPELAQRLLAALA 187
|
250
....*....|....*....
6KHM_Z 274 NVELHLYDGLRHEVHNEPE 292
Cdd:pfam12697 188 GARLVVLPGAGHLPLDDPE 206
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
105-253 |
2.44e-03 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 38.68 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6KHM_Z 105 DLPWVVFGHSWGSMIA----RAMATRPGTRLDGLALCGivaqprgfettldhktlakamATAPTDPAPEALVAQMFD-GF 179
Cdd:COG3208 71 DRPFALFGHSMGALLAfelaRRLERRGRPLPAHLFVSG---------------------RRAPHLPRRRRPLHDLSDaEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6KHM_Z 180 ADRLSEDDGPTGWVARSKEVVAdhgkdkfnnfgapmstRFLQGL-ADiYAMANGdsfYATMP----NIPIVLFAGSEDP 253
Cdd:COG3208 130 LAELRRLGGTPEEVLADPELLE----------------LFLPILrAD-FRLLET---YRYTPgpplDCPITALGGDDDP 188
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
243-285 |
9.39e-03 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 36.77 E-value: 9.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
6KHM_Z 243 PIVLFAGSEDPAGDFGtgvKAVAERLRRDGHNVELHLYDGLRH 285
Cdd:COG0657 141 PTLIVTGEADPLVDES---EALAAALRAAGVPVELHVYPGGGH 180
|
|
| |
