|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10985 |
PRK10985 |
putative hydrolase; Provisional |
15-338 |
0e+00 |
|
putative hydrolase; Provisional
Pssm-ID: 182883 Cd Length: 324 Bit Score: 712.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 15 SAEFIPMRGFSNCHLQTMLPRLFRRQVKFTPYWQRLELPDGDFVDLAWSENPAQAQHKPRLVVFHGLEGSLNSPYAHGLV 94
Cdd:PRK10985 1 SAEFTPMRGASNPHLQTLLPRLIRRKVLFTPYWQRLELPDGDFVDLAWSEDPAQARHKPRLVLFHGLEGSFNSPYAHGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 95 EAAQKRGWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQREFGHAPTAAVGYSLGGNMLACLLAKEGNDLPVDA 174
Cdd:PRK10985 81 EAAQKRGWLGVVMHFRGCSGEPNRLHRIYHSGETEDARFFLRWLQREFGHVPTAAVGYSLGGNMLACLLAKEGDDLPLDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 175 AVIVSAPFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGTLPINLAQLKSVRRIREFDDLITARIHGYADAID 254
Cdd:PRK10985 161 AVIVSAPLMLEACSYRMEQGFSRVYQRYLLNLLKANAARKLAAYPGTLPINLAQLKSVRRLREFDDLITARIHGFADAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 255 YYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTEHGGHVGFIGGTLLHPQMWLESRIPDWLTTY 334
Cdd:PRK10985 241 YYRQCSALPLLNQIRKPTLIIHAKDDPFMTHEVIPKPESLPPNVEYQLTEHGGHVGFVGGTLLKPQMWLEQRIPDWLTTY 320
|
....
gi 16131232 335 LEAK 338
Cdd:PRK10985 321 LEAK 324
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
14-335 |
4.33e-177 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 493.51 E-value: 4.33e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 14 SSAEFIPMRGFSNCHLQTMLPRLFRRQVKFTPYWQRLELPDGDFVDLAWSENPAQaqHKPRLVVFHGLEGSLNSPYAHGL 93
Cdd:COG0429 5 STSPFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWSDPPAP--SKPLVVLLHGLEGSSDSHYARGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 94 VEAAQKRGWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQREFGHAPTAAVGYSLGGNMLACLLAKEGNDLP-V 172
Cdd:COG0429 83 ARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDAPpL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 173 DAAVIVSAPFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGtlPINLAQLKSVRRIREFDDLITARIHGYADA 252
Cdd:COG0429 163 KAAVAVSPPLDLAASADRLERGFNRLYQRYFLRSLKRKLRRKLALFPG--LIDLEALKRIRTLREFDDAYTAPLHGFKDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 253 IDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTEHGGHVGFIGGTLLHPQMWLESRIPDWLT 332
Cdd:COG0429 241 EDYYQRASALPFLPQIRVPTLILNAADDPFLPPECLPEAAELNPNVTLELTKHGGHVGFISGKSPGRRYWLERRILEFLD 320
|
...
gi 16131232 333 TYL 335
Cdd:COG0429 321 AHL 323
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
73-315 |
1.31e-37 |
|
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: 134.94 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 73 PRLVVFHGLEGSLNSPYahGLVEAAQKRGWLGVVMHFRGCSGEPNRMHRiyHSGETEDASWFLRWLQREFGHAPTAAVGY 152
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFGKSSRPKAQ--DDYRTDDLAEDLEYILEALGLEKVNLVGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 153 SLGGNMLACLLAKegNDLPVDAAVIVSA---PFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGTL-----PI 224
Cdd:pfam00561 77 SMGGLIALAYAAK--YPDRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLllrlrLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 225 NLAQLKSVRRIREFDDLITARIHGYADAIDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTE 304
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
|
250
....*....|.
gi 16131232 305 HGGHVGFIGGT 315
Cdd:pfam00561 235 DAGHFAFLEGP 245
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10985 |
PRK10985 |
putative hydrolase; Provisional |
15-338 |
0e+00 |
|
putative hydrolase; Provisional
Pssm-ID: 182883 Cd Length: 324 Bit Score: 712.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 15 SAEFIPMRGFSNCHLQTMLPRLFRRQVKFTPYWQRLELPDGDFVDLAWSENPAQAQHKPRLVVFHGLEGSLNSPYAHGLV 94
Cdd:PRK10985 1 SAEFTPMRGASNPHLQTLLPRLIRRKVLFTPYWQRLELPDGDFVDLAWSEDPAQARHKPRLVLFHGLEGSFNSPYAHGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 95 EAAQKRGWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQREFGHAPTAAVGYSLGGNMLACLLAKEGNDLPVDA 174
Cdd:PRK10985 81 EAAQKRGWLGVVMHFRGCSGEPNRLHRIYHSGETEDARFFLRWLQREFGHVPTAAVGYSLGGNMLACLLAKEGDDLPLDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 175 AVIVSAPFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGTLPINLAQLKSVRRIREFDDLITARIHGYADAID 254
Cdd:PRK10985 161 AVIVSAPLMLEACSYRMEQGFSRVYQRYLLNLLKANAARKLAAYPGTLPINLAQLKSVRRLREFDDLITARIHGFADAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 255 YYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTEHGGHVGFIGGTLLHPQMWLESRIPDWLTTY 334
Cdd:PRK10985 241 YYRQCSALPLLNQIRKPTLIIHAKDDPFMTHEVIPKPESLPPNVEYQLTEHGGHVGFVGGTLLKPQMWLEQRIPDWLTTY 320
|
....
gi 16131232 335 LEAK 338
Cdd:PRK10985 321 LEAK 324
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
14-335 |
4.33e-177 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 493.51 E-value: 4.33e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 14 SSAEFIPMRGFSNCHLQTMLPRLFRRQVKFTPYWQRLELPDGDFVDLAWSENPAQaqHKPRLVVFHGLEGSLNSPYAHGL 93
Cdd:COG0429 5 STSPFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWSDPPAP--SKPLVVLLHGLEGSSDSHYARGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 94 VEAAQKRGWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQREFGHAPTAAVGYSLGGNMLACLLAKEGNDLP-V 172
Cdd:COG0429 83 ARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDAPpL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 173 DAAVIVSAPFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGtlPINLAQLKSVRRIREFDDLITARIHGYADA 252
Cdd:COG0429 163 KAAVAVSPPLDLAASADRLERGFNRLYQRYFLRSLKRKLRRKLALFPG--LIDLEALKRIRTLREFDDAYTAPLHGFKDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 253 IDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTEHGGHVGFIGGTLLHPQMWLESRIPDWLT 332
Cdd:COG0429 241 EDYYQRASALPFLPQIRVPTLILNAADDPFLPPECLPEAAELNPNVTLELTKHGGHVGFISGKSPGRRYWLERRILEFLD 320
|
...
gi 16131232 333 TYL 335
Cdd:COG0429 321 AHL 323
|
|
| PLN02511 |
PLN02511 |
hydrolase |
25-314 |
4.26e-41 |
|
hydrolase
Pssm-ID: 215282 [Multi-domain] Cd Length: 388 Bit Score: 147.62 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 25 SNCHLQTMLPRLFRRQVKFTpyWQR--LELPDGDFVDLAW--SENPAQAQHKPRLVVFHGLEGSLNSPYAHGLVEAAQKR 100
Cdd:PLN02511 51 GNRHVETIFASFFRSLPAVR--YRRecLRTPDGGAVALDWvsGDDRALPADAPVLILLPGLTGGSDDSYVRHMLLRARSK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 101 GWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQREFGHAPTAAVGYSLGGNMLACLLAKEGNDLPVDAAVIVSA 180
Cdd:PLN02511 129 GWRVVVFNSRGCADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANILVNYLGEEGENCPLSGAVSLCN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 181 PFMLEACSYHMEKGFSRVYQRYLlnllkANAARKLAA--------YPGTLPINLAqlKSVRRIREFDDLITARIHGYADA 252
Cdd:PLN02511 209 PFDLVIADEDFHKGFNNVYDKAL-----AKALRKIFAkhallfegLGGEYNIPLV--ANAKTVRDFDDGLTRVSFGFKSV 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131232 253 IDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPE-SLPPQVEYQLTEHGGHVGFIGG 314
Cdd:PLN02511 282 DAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPARGIPREDiKANPNCLLIVTPSGGHLGWVAG 344
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
73-315 |
1.31e-37 |
|
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: 134.94 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 73 PRLVVFHGLEGSLNSPYahGLVEAAQKRGWLGVVMHFRGCSGEPNRMHRiyHSGETEDASWFLRWLQREFGHAPTAAVGY 152
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFGKSSRPKAQ--DDYRTDDLAEDLEYILEALGLEKVNLVGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 153 SLGGNMLACLLAKegNDLPVDAAVIVSA---PFMLEACSYHMEKGFSRVYQRYLLNLLKANAARKLAAYPGTL-----PI 224
Cdd:pfam00561 77 SMGGLIALAYAAK--YPDRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLllrlrLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 225 NLAQLKSVRRIREFDDLITARIHGYADAIDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTE 304
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
|
250
....*....|.
gi 16131232 305 HGGHVGFIGGT 315
Cdd:pfam00561 235 DAGHFAFLEGP 245
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
76-309 |
3.41e-08 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 53.79 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 76 VVFHGLEGSLNSpyAHGLVEAAQKRGWLGVVMHFRGCSGEPNRMHRIYHSGETEDASWFLRWLQRefGHAPTAAVGYSLG 155
Cdd:COG1647 19 LLLHGFTGSPAE--MRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKA--GYDKVIVIGLSMG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 156 GnMLACLLAKEGNDlpVDAAVIVSAPFMLEACSYHMeKGFSRVYQRYLLNLLK--ANAARKLAAYPGTlpinlaqlkSVR 233
Cdd:COG1647 95 G-LLALLLAARYPD--VAGLVLLSPALKIDDPSAPL-LPLLKYLARSLRGIGSdiEDPEVAEYAYDRT---------PLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 234 RIREFDDLItarihgyadaidyyrqCSAMPMLNRIAKPTLIIHAKDDpfmdhQVIPkPESLP--------PQVEYQLTEH 305
Cdd:COG1647 162 ALAELQRLI----------------REVRRDLPKITAPTLIIQSRKD-----EVVP-PESARyiyerlgsPDKELVWLED 219
|
....
gi 16131232 306 GGHV 309
Cdd:COG1647 220 SGHV 223
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
49-335 |
7.15e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 52.33 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 49 RLELPDGDFVDlAWSENPAQAQHKPRLVVFHGLEGSLNSPYAHGLVEAAQkRGWLGVVMHFRGCSGEPNRMHRiyhsGET 128
Cdd:COG1506 1 TFKSADGTTLP-GWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALAS-RGYAVLAPDYRGYGESAGDWGG----DEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 129 EDASWFLRWLQREFGHAPT--AAVGYSLGGNMLACLLAKEGNdlPVDAAVIVSAPFmleacsyhmekgfsrvyqryllnl 206
Cdd:COG1506 75 DDVLAAIDYLAARPYVDPDriGIYGHSYGGYMALLAAARHPD--RFKAAVALAGVS------------------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 207 lkanaarklaaypgtlpiNLAQLksvrrIREFDDLITARIHGYADAIDYYRQCSAMPMLNRIAKPTLIIHAKDDPfmdhq 286
Cdd:COG1506 129 ------------------DLRSY-----YGTTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADD----- 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131232 287 VIPKPES---------LPPQVEYQLTEHGGHvGFIGGTLLHpqmWLEsRIPDWLTTYL 335
Cdd:COG1506 181 RVPPEQAerlyealkkAGKPVELLVYPGEGH-GFSGAGAPD---YLE-RILDFLDRHL 233
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
48-311 |
1.88e-07 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 51.16 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 48 QRLELPDGDFVDLAWSENPAQAQHKPRLVVFHGLeGSLNSPYAHgLVEAAQKRGWlGVVMH-FRGCSGEPNRMHRIYHSG 126
Cdd:COG2267 4 RLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGL-GEHSGRYAE-LAEALAAAGY-AVLAFdLRGHGRSDGPRGHVDSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 127 E-TEDASWFLRWLQREfGHAPTAAVGYSLGGNMLACLLAKEGNDLpvdAAVIVSAPFMLEacsyhmekgfsrvyqrylln 205
Cdd:COG2267 81 DyVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRV---AGLVLLAPAYRA-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 206 llkanaarklaaypgtlpinlaqlksvrrirefDDLITARIHGYADAidyyrqcSAMPMLNRIAKPTLIIHAKDDPFMDH 285
Cdd:COG2267 137 ---------------------------------DPLLGPSARWLRAL-------RLAEALARIDVPVLVLHGGADRVVPP 176
|
250 260
....*....|....*....|....*..
gi 16131232 286 QVIPKP-ESLPPQVEYQLTEHGGHVGF 311
Cdd:COG2267 177 EAARRLaARLSPDVELVLLPGARHELL 203
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
69-286 |
2.16e-07 |
|
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: 51.06 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 69 AQHKPRLVVFHGL-EGSLNspYAHgLVEAAQKRGWlGVVMH-FRGcSG--EPNRMHriYHSGET--EDASWFLRWLQREF 142
Cdd:pfam12146 1 GEPRAVVVLVHGLgEHSGR--YAH-LADALAAQGF-AVYAYdHRG-HGrsDGKRGH--VPSFDDyvDDLDTFVDKIREEH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 143 GHAPTAAVGYSLGGNMLACLLAKEGNDLpvdAAVIVSAPfmleACSYHMEKGfsRVYQRYLLNLLkANAARKLAAYPGTL 222
Cdd:pfam12146 74 PGLPLFLLGHSMGGLIAALYALRYPDKV---DGLILSAP----ALKIKPYLA--PPILKLLAKLL-GKLFPRLRVPNNLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131232 223 PINLAQLKSVRRIREFDDLITARI-----HGYADAIDYyrqcsAMPMLNRIAKPTLIIHAKDDPFMDHQ 286
Cdd:pfam12146 144 PDSLSRDPEVVAAYAADPLVHGGIsartlYELLDAGER-----LLRRAAAITVPLLLLHGGADRVVDPA 207
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
66-309 |
4.26e-07 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 50.30 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 66 PAQAQHK-PRLVVFHGLEGSLN--SPYAHGLVEaaqkRGWLGVVMHFRGC---SGEPnRMHRIYhsgETEDASWFLRWLQ 139
Cdd:COG1073 30 PAGASKKyPAVVVAHGNGGVKEqrALYAQRLAE----LGFNVLAFDYRGYgesEGEP-REEGSP---ERRDARAAVDYLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 140 REFGHAPT--AAVGYSLGGNMlACLLAKEgndLPVDAAVIVSAPFmleacsyhmekgfsrvyqrylLNLLKANAARKLAA 217
Cdd:COG1073 102 TLPGVDPEriGLLGISLGGGY-ALNAAAT---DPRVKAVILDSPF---------------------TSLEDLAAQRAKEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 218 YPGTLPinlaqLKSVRRIREFDDLITARihgyADAIDYyrqcsampmLNRIAKPTLIIHAKDDpfmdhQVIPKPESL--- 294
Cdd:COG1073 157 RGAYLP-----GVPYLPNVRLASLLNDE----FDPLAK---------IEKISRPLLFIHGEKD-----EAVPFYMSEdly 213
|
250
....*....|....*...
gi 16131232 295 ---PPQVEYQLTEHGGHV 309
Cdd:COG1073 214 eaaAEPKELLIVPGAGHV 231
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
232-312 |
2.51e-03 |
|
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: 38.83 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 232 VRRIREFDDLITARIHGYADAIDYYRQCSAMPMLNRIAKPTLIIHAKDDPFMDHQVIPKPESLPPQVEYQLTEHGGHVGF 311
Cdd:COG0596 124 LAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPP 203
|
.
gi 16131232 312 I 312
Cdd:COG0596 204 L 204
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
49-176 |
2.77e-03 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 38.79 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131232 49 RLELPDGDFVD--LAWsenPAQAQHKPRLVVFHGLEGSlnSPYAHGLVEAAQKRGWLGVVM---HFRGCSGEPNRMHRIY 123
Cdd:COG0412 7 TIPTPDGVTLPgyLAR---PAGGGPRPGVVVLHEIFGL--NPHIRDVARRLAAAGYVVLAPdlyGRGGPGDDPDEARALM 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131232 124 HSGETE----DASWFLRWLQR--EFGHAPTAAVGYSLGGnMLACLLAKEGNDLpvDAAV 176
Cdd:COG0412 82 GALDPEllaaDLRAALDWLKAqpEVDAGRVGVVGFCFGG-GLALLAAARGPDL--AAAV 137
|
|
|