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Conserved domains on  [gi|16131232|ref|NP_417812|]
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putative hydrolase YheT [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

YheT family hydrolase( domain architecture ID 10013695)

YheT family hydrolase belongs to the alpa/beta-hydrolase superfamily

Graphical summary

 Zoom to residue level

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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