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Conserved domains on  [gi|1780267313|ref|WP_155624667|]
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MULTISPECIES: alpha/beta hydrolase [Burkholderia]

Protein Classification

alpha/beta hydrolase( domain architecture ID 12114401)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
66-304 1.10e-90

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: 270.24  E-value: 1.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  66 APPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAAR--GNTPLFL 143
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREehPGLPLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 144 MGHSMGGAIAALYAIERlpasGHTLAGLVLSSPALAPG-RDVPRWMLAMSRFISRVWPSFP-AIRIDAALLSRDPAIVAA 221
Cdd:pfam12146  81 LGHSMGGLIAALYALRY----PDKVDGLILSAPALKIKpYLAPPILKLLAKLLGKLFPRLRvPNNLLPDSLSRDPEVVAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 222 NRADPLVhHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGGFHETMN 301
Cdd:pfam12146 157 YAADPLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLN 235

                  ...
gi 1780267313 302 DLE 304
Cdd:pfam12146 236 EPD 238
 
Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
66-304 1.10e-90

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: 270.24  E-value: 1.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  66 APPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAAR--GNTPLFL 143
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREehPGLPLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 144 MGHSMGGAIAALYAIERlpasGHTLAGLVLSSPALAPG-RDVPRWMLAMSRFISRVWPSFP-AIRIDAALLSRDPAIVAA 221
Cdd:pfam12146  81 LGHSMGGLIAALYALRY----PDKVDGLILSAPALKIKpYLAPPILKLLAKLLGKLFPRLRvPNNLLPDSLSRDPEVVAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 222 NRADPLVhHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGGFHETMN 301
Cdd:pfam12146 157 YAADPLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLN 235

                  ...
gi 1780267313 302 DLE 304
Cdd:pfam12146 236 EPD 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
40-318 6.40e-57

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 183.66  E-value: 6.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  40 PARMGRLRTADGLELASYRWPAADgsaPPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVER 119
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRPAG---SPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 120 FDDYLNDADALVAEA-ARGNTPLFLMGHSMGGAIAALYAIERlpasGHTLAGLVLSSPALapgrdvprwmlamsrfisrv 198
Cdd:COG2267    79 FDDYVDDLRAALDALrARPGLPVVLLGHSMGGLIALLYAARY----PDRVAGLVLLAPAY-------------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 199 wpsfpairidaallsrdpaivaanRADPLVHhdaVPARTGAELldamaRIERGRGSLRVPVLIYHGTSDKLTEPDGSRAF 278
Cdd:COG2267   135 ------------------------RADPLLG---PSARWLRAL-----RLAEALARIDVPVLVLHGGADRVVPPEAARRL 182
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1780267313 279 GAHVgSPDRTLTLYEGGFHETMNDLERERVIDALIAWIHA 318
Cdd:COG2267   183 AARL-SPDVELVLLPGARHELLNEPAREEVLAAILAWLER 221
PHA02857 PHA02857
monoglyceride lipase; Provisional
68-316 3.18e-40

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 141.95  E-value: 3.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  68 PRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAARG--NTPLFLMG 145
Cdd:PHA02857   24 PKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTypGVPVFLLG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 146 HSMGGAIAALYAIErlpaSGHTLAGLVLSSPaLAPGRDVPRWMLAMSRFISRVWPSFPAIRIDAALLSRDPAIVAANRAD 225
Cdd:PHA02857  104 HSMGATISILAAYK----NPNLFTAMILMSP-LVNAEAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 226 PLVHHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSpDRTLTLYEGGFHETMNDLE- 304
Cdd:PHA02857  179 PLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDe 257
                         250
                  ....*....|...
gi 1780267313 305 -RERVIDALIAWI 316
Cdd:PHA02857  258 vKKSVMKEIETWI 270
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
47-316 1.67e-11

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 64.03  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  47 RTADGLELASYRWPAADGSAppraTVALVHGLAEHAG-RYERLAA-------------------------RLNAAGISVL 100
Cdd:TIGR01607   3 RNKDGLLLKTYSWIVKNAIG----IIVLIHGLKSHLRlQFLKINAkivnndravlidtdnyyiykdswieNFNKNGYSVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 101 AIDLRGHGRSPGK---RAWVERFDDYLNDA--------DALVAEAARGNT--------------PLFLMGHSMGGAIaAL 155
Cdd:TIGR01607  79 GLDLQGHGESDGLqnlRGHINCFDDLVYDViqymnrinDSIILENETKSDdesydivntkenrlPMYIIGLSMGGNI-AL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 156 YAIERLPASGH-----------TLAGLVLSSPALAPGRDVPRWM-LAMSRFISRVWPSFpaiRIDAAL-LSRDPAIVAAN 222
Cdd:TIGR01607 158 RLLELLGKSNEnndklnikgciSLSGMISIKSVGSDDSFKFKYFyLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDII 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 223 RADPLVHHDAVPARTGAELLDA-------MARIERGrgslrVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGG 295
Cdd:TIGR01607 235 KFDKFRYDGGITFNLASELIKAtdtldcdIDYIPKD-----IPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
                         330       340
                  ....*....|....*....|.
gi 1780267313 296 FHETMNDLERERVIDALIAWI 316
Cdd:TIGR01607 310 DHVITIEPGNEEVLKKIIEWI 330
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
126-213 6.21e-03

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 37.20  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  126 DADALVAEAAR------GNTPLFLMGHSMGGAIAALYAiERLPASGHTLAGLVLSSPALAPGRDVPRWMLAMSRFISRVW 199
Cdd:smart00824  45 SADALVEAQAEavlraaGGRPFVLVGHSSGGLLAHAVA-ARLEARGIPPAAVVLLDTYPPGDPAPEGWLPELLRGVFERE 123
                           90
                   ....*....|....
gi 1780267313  200 PSFpaIRIDAALLS 213
Cdd:smart00824 124 DSF--VPMDDARLT 135
 
Name Accession Description Interval E-value
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
66-304 1.10e-90

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: 270.24  E-value: 1.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  66 APPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAAR--GNTPLFL 143
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREehPGLPLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 144 MGHSMGGAIAALYAIERlpasGHTLAGLVLSSPALAPG-RDVPRWMLAMSRFISRVWPSFP-AIRIDAALLSRDPAIVAA 221
Cdd:pfam12146  81 LGHSMGGLIAALYALRY----PDKVDGLILSAPALKIKpYLAPPILKLLAKLLGKLFPRLRvPNNLLPDSLSRDPEVVAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 222 NRADPLVhHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGGFHETMN 301
Cdd:pfam12146 157 YAADPLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLN 235

                  ...
gi 1780267313 302 DLE 304
Cdd:pfam12146 236 EPD 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
40-318 6.40e-57

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 183.66  E-value: 6.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  40 PARMGRLRTADGLELASYRWPAADgsaPPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVER 119
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRPAG---SPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 120 FDDYLNDADALVAEA-ARGNTPLFLMGHSMGGAIAALYAIERlpasGHTLAGLVLSSPALapgrdvprwmlamsrfisrv 198
Cdd:COG2267    79 FDDYVDDLRAALDALrARPGLPVVLLGHSMGGLIALLYAARY----PDRVAGLVLLAPAY-------------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 199 wpsfpairidaallsrdpaivaanRADPLVHhdaVPARTGAELldamaRIERGRGSLRVPVLIYHGTSDKLTEPDGSRAF 278
Cdd:COG2267   135 ------------------------RADPLLG---PSARWLRAL-----RLAEALARIDVPVLVLHGGADRVVPPEAARRL 182
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1780267313 279 GAHVgSPDRTLTLYEGGFHETMNDLERERVIDALIAWIHA 318
Cdd:COG2267   183 AARL-SPDVELVLLPGARHELLNEPAREEVLAAILAWLER 221
PHA02857 PHA02857
monoglyceride lipase; Provisional
68-316 3.18e-40

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 141.95  E-value: 3.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  68 PRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAARG--NTPLFLMG 145
Cdd:PHA02857   24 PKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTypGVPVFLLG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 146 HSMGGAIAALYAIErlpaSGHTLAGLVLSSPaLAPGRDVPRWMLAMSRFISRVWPSFPAIRIDAALLSRDPAIVAANRAD 225
Cdd:PHA02857  104 HSMGATISILAAYK----NPNLFTAMILMSP-LVNAEAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 226 PLVHHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSpDRTLTLYEGGFHETMNDLE- 304
Cdd:PHA02857  179 PLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDe 257
                         250
                  ....*....|...
gi 1780267313 305 -RERVIDALIAWI 316
Cdd:PHA02857  258 vKKSVMKEIETWI 270
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
72-321 1.69e-38

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 136.61  E-value: 1.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  72 VALVHGLAehAGRYE--RLAARLNAAGISVLAIDLRGHGRSPG--KRAwveRFDDYLNDADALVAEAARGNTPLFLMGHS 147
Cdd:COG1647    18 VLLLHGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPEdlLKT---TWEDWLEDVEEAYEILKAGYDKVIVIGLS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 148 MGGAIAALYAiERLPAsghtLAGLVLSSPALapgrDVPRWMLAMSRFISRVWPSFPAIRIDaallsrdpaivAANRADPL 227
Cdd:COG1647    93 MGGLLALLLA-ARYPD----VAGLVLLSPAL----KIDDPSAPLLPLLKYLARSLRGIGSD-----------IEDPEVAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 228 VHHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGGFHETMNDLERER 307
Cdd:COG1647   153 YAYDRTPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDKDREE 232
                         250
                  ....*....|....
gi 1780267313 308 VIDALIAWIHAHAP 321
Cdd:COG1647   233 VAEEILDFLERLAA 246
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
69-316 6.10e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 130.78  E-value: 6.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  69 RATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAARGN--TPLFLMGH 146
Cdd:PLN02652  136 RGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENpgVPCFLFGH 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 147 SMGGAI---AALYaierlPASGHTLAGLVLSSPAL-------APGRDVPRWMLAMSRFisrvwpSFPAIRIDAALLSRDP 216
Cdd:PLN02652  216 STGGAVvlkAASY-----PSIEDKLEGIVLTSPALrvkpahpIVGAVAPIFSLVAPRF------QFKGANKRGIPVSRDP 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 217 AIVAANRADPLVHHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGGF 296
Cdd:PLN02652  285 AALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFL 364
                         250       260
                  ....*....|....*....|
gi 1780267313 297 HETMNDLERERVIDALIAWI 316
Cdd:PLN02652  365 HDLLFEPEREEVGRDIIDWM 384
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
51-318 4.11e-29

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 113.72  E-value: 4.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  51 GLELASYRWpAADGSAPPRATVALVHGLAEHAG-RYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDA-- 127
Cdd:PLN02298   42 GLSLFTRSW-LPSSSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCls 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 128 --DALVAEAARGNTPLFLMGHSMGGAIAALYAIERlPASghtLAGLVLSSPALAPGRDV-PRWMLA-MSRFISRVWPSFP 203
Cdd:PLN02298  121 ffNSVKQREEFQGLPRFLYGESMGGAICLLIHLAN-PEG---FDGAVLVAPMCKISDKIrPPWPIPqILTFVARFLPTLA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 204 aIRIDAALLSR---DPA--IVAANraDPLVHHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTEPDGSRAF 278
Cdd:PLN02298  197 -IVPTADLLEKsvkVPAkkIIAKR--NPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRAL 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1780267313 279 GAHVGSPDRTLTLYEGGFHETM---NDLERERVIDALIAWIHA 318
Cdd:PLN02298  274 YEEAKSEDKTIKIYDGMMHSLLfgePDENIEIVRRDILSWLNE 316
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
47-319 1.08e-27

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 110.23  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  47 RTADGLELASYRW-PaadGSAPPRATVALVHGLAEHAGRY-ERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYL 124
Cdd:PLN02385   67 VNSRGVEIFSKSWlP---ENSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 125 NDadalVAE---AARGNT-----PLFLMGHSMGGAIAaLYAIERLPasgHTLAGLVLSSPALAPGRDV-PRW-MLAMSRF 194
Cdd:PLN02385  144 DD----VIEhysKIKGNPefrglPSFLFGQSMGGAVA-LKVHLKQP---NAWDGAILVAPMCKIADDVvPPPlVLQILIL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 195 ISRVWPS---FPAIRIdAALLSRDPAIVAANRADPLVHHDAVPARTGAELLDAMARIERGRGSLRVPVLIYHGTSDKLTE 271
Cdd:PLN02385  216 LANLLPKaklVPQKDL-AELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTD 294
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1780267313 272 PDGSRAFGAHVGSPDRTLTLYEGGFHETmndLERE------RVIDALIAWIHAH 319
Cdd:PLN02385  295 PSVSKFLYEKASSSDKKLKLYEDAYHSI---LEGEpdemifQVLDDIISWLDSH 345
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
46-319 2.63e-25

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 101.92  E-value: 2.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  46 LRTADGLELASYRWPAADGSaPPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGK---RAWVERFdD 122
Cdd:COG1073    15 FKSRDGIKLAGDLYLPAGAS-KKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpreEGSPERR-D 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 123 YLNDADALVAEAARGNTPLFLMGHSMGGAIAALYAIERlpasgHTLAGLVLSSPALApgrdvpRWMLA---MSRFISRVW 199
Cdd:COG1073    93 ARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATD-----PRVKAVILDSPFTS------LEDLAaqrAKEARGAYL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 200 PSFPairidaallsrdpaivaanradplVHHDAVPARTGAELLDAMARIERgrgsLRVPVLIYHGTSDKLTEPDGSRAFG 279
Cdd:COG1073   162 PGVP------------------------YLPNVRLASLLNDEFDPLAKIEK----ISRPLLFIHGEKDEAVPFYMSEDLY 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1780267313 280 AHVGSPdRTLTLYEGGFHETMNDLERERVIDALIAWIHAH 319
Cdd:COG1073   214 EAAAEP-KELLIVPGAGHVDLYDRPEEEYFDKLAEFFKKN 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
48-319 8.56e-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: 86.21  E-value: 8.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  48 TADGLELAsYRWPAADGsapprATVALVHGLAEHAGRYERLAARLnAAGISVLAIDLRGHGRSPgKRAWVERFDDYLNDA 127
Cdd:COG0596     8 TVDGVRLH-YREAGPDG-----PPVVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGHGRSD-KPAGGYTLDDLADDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 128 DALVAeaARGNTPLFLMGHSMGGAIAALYAIERlpasGHTLAGLVLSSpalapgrDVPRWMLAMsrfisrvwpsfpairi 207
Cdd:COG0596    80 AALLD--ALGLERVVLVGHSMGGMVALELAARH----PERVAGLVLVD-------EVLAALAEP---------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 208 daallsrdpaiVAANRADPLVHHDAVPARTGAELLDAMARIergrgslRVPVLIYHGTSDKLTEPDGSRAFGAHVgsPDR 287
Cdd:COG0596   131 -----------LRRPGLAPEALAALLRALARTDLRERLARI-------TVPTLVIWGEKDPIVPPALARRLAELL--PNA 190
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1780267313 288 TLTLYEGGFHETMNDlERERVIDALIAWIHAH 319
Cdd:COG0596   191 ELVVLPGAGHFPPLE-QPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
74-297 7.76e-17

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: 78.32  E-value: 7.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  74 LVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVE-RFDDYLNDADALVaeAARGNTPLFLMGHSMGGAI 152
Cdd:pfam00561   5 LLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYIL--EALGLEKVNLVGHSMGGLI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 153 AALYAiERLPASGHTLAGLVLSSPALAPGRDVPRWMLAMSRFISR-----------VWPSFPA------IRIDAALLSRD 215
Cdd:pfam00561  83 ALAYA-AKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGfvadfapnplgRLVAKLLallllrLRLLKALPLLN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 216 PAIVAANRADP-LVHHDAVPARTGAELLDAMARIergrGSLRVPVLIYHGTSDKLTEPDGSRAFGAHVgsPDRTLTLYEG 294
Cdd:pfam00561 162 KRFPSGDYALAkSLVTGALLFIETWSTELRAKFL----GRLDEPTLIIWGDQDPLVPPQALEKLAQLF--PNARLVVIPD 235

                  ...
gi 1780267313 295 GFH 297
Cdd:pfam00561 236 AGH 238
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
45-319 5.31e-16

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 75.82  E-value: 5.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  45 RLRTADGLELASYRWPAADGSAPPraTVALVHGLAEHA-GRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVErFDDY 123
Cdd:COG1506     1 TFKSADGTTLPGWLYLPADGKKYP--VVVYVHGGPGSRdDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-VDDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 124 LNDADALVAEAARGNTPLFLMGHSMGGAiAALYAIERLPasgHTLAGLVLSSPalapgrdvprwmlaMSRFISRVWPSFP 203
Cdd:COG1506    78 LAAIDYLAARPYVDPDRIGIYGHSYGGY-MALLAAARHP---DRFKAAVALAG--------------VSDLRSYYGTTRE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 204 AIRIDAALLSRDPAIVAANradplvhhdavpartgaellDAMARIERgrgsLRVPVLIYHGTSDKLTEPDGSRAF--GAH 281
Cdd:COG1506   140 YTERLMGGPWEDPEAYAAR--------------------SPLAYADK----LKTPLLLIHGEADDRVPPEQAERLyeALK 195
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1780267313 282 VGSPDRTLTLYEGGFHEtMNDLERERVIDALIAWIHAH 319
Cdd:COG1506   196 KAGKPVELLVYPGEGHG-FSGAGAPDYLERILDFLDRH 232
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
45-292 1.34e-15

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 75.69  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  45 RLRTADGLELASYRWPAAdgsAPPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRS-PGKRAWVE-RFDD 122
Cdd:COG4757    11 TITAADGYPLAARLFPPA---GPPRAVVLINPATGVPQRFYRPFARYLAERGFAVLTYDYRGIGLSrPGSLRGFDaGYRD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 123 YLN-DADALVAEAAR--GNTPLFLMGHSMGGAIAALYaierlpASGHTLAGLVL--SSPALAPGRDVPR--WMLAMSRFI 195
Cdd:COG4757    88 WGElDLPAVLDALRArfPGLPLLLVGHSLGGQLLGLA------PNAERVDRLVTvaSGSGYWRDYPPRRrlKVLLFWHLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 196 ----SRVWPSFPAIRIdaALLSRDPAIVAANRADPLVHHDAVPARTGAELLDAMARIergrgslRVPVLIYHGTSDKLTE 271
Cdd:COG4757   162 gpllTRLLGYFPGRRL--GFGEDLPAGVARQWRRWCRRPRYFFDDDGEDLEAALAAV-------TAPVLAISFTDDELAP 232
                         250       260
                  ....*....|....*....|.
gi 1780267313 272 PDGSRAFGAHVGSPDRTLTLY 292
Cdd:COG4757   233 PAAVDRLLAYYPNAPVTRRRL 253
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
47-316 1.67e-11

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 64.03  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  47 RTADGLELASYRWPAADGSAppraTVALVHGLAEHAG-RYERLAA-------------------------RLNAAGISVL 100
Cdd:TIGR01607   3 RNKDGLLLKTYSWIVKNAIG----IIVLIHGLKSHLRlQFLKINAkivnndravlidtdnyyiykdswieNFNKNGYSVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 101 AIDLRGHGRSPGK---RAWVERFDDYLNDA--------DALVAEAARGNT--------------PLFLMGHSMGGAIaAL 155
Cdd:TIGR01607  79 GLDLQGHGESDGLqnlRGHINCFDDLVYDViqymnrinDSIILENETKSDdesydivntkenrlPMYIIGLSMGGNI-AL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 156 YAIERLPASGH-----------TLAGLVLSSPALAPGRDVPRWM-LAMSRFISRVWPSFpaiRIDAAL-LSRDPAIVAAN 222
Cdd:TIGR01607 158 RLLELLGKSNEnndklnikgciSLSGMISIKSVGSDDSFKFKYFyLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDII 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 223 RADPLVHHDAVPARTGAELLDA-------MARIERGrgslrVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRTLTLYEGG 295
Cdd:TIGR01607 235 KFDKFRYDGGITFNLASELIKAtdtldcdIDYIPKD-----IPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
                         330       340
                  ....*....|....*....|.
gi 1780267313 296 FHETMNDLERERVIDALIAWI 316
Cdd:TIGR01607 310 DHVITIEPGNEEVLKKIIEWI 330
PRK10749 PRK10749
lysophospholipase L2; Provisional
71-211 7.39e-11

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 62.32  E-value: 7.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  71 TVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRS-----PGKRAWVERFDDYLNDADALVAE--AARGNTPLFL 143
Cdd:PRK10749   56 VVVICPGRIESYVKYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQeiQPGPYRKRYA 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780267313 144 MGHSMGGAIAALYaIERLPasgHTLAGLVLSSPALAPGRDVPRWmlaMSRFISRVWPSFPAIRIDAAL 211
Cdd:PRK10749  136 LAHSMGGAILTLF-LQRHP---GVFDAIALCAPMFGIVLPLPSW---MARRILNWAEGHPRIRDGYAI 196
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
41-172 4.51e-10

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.82  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  41 ARMGRLRTADGLELASYRW-PAADGsapPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGK----RA 115
Cdd:COG0412     3 TETVTIPTPDGVTLPGYLArPAGGG---PRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdeaRA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1780267313 116 WVERFDD--YLNDADALVAEAAR----GNTPLFLMGHSMGGAIAALYAierlpASGHTLAGLV 172
Cdd:COG0412    80 LMGALDPelLAADLRAALDWLKAqpevDAGRVGVVGFCFGGGLALLAA-----ARGPDLAAAV 137
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
85-320 8.47e-10

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 57.94  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  85 YERLAARLnAAGISVLAIDLRGHGRSPGKRAwVERFDDYlndADALVAE-AARGNTPLFLMGHSMGGAIAalYAI-ERLP 162
Cdd:COG3208    22 YRPWAAAL-PPDIEVLAVQLPGRGDRLGEPP-LTSLEEL---ADDLAEElAPLLDRPFALFGHSMGALLA--FELaRRLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 163 ASGHTL-AGLVLSSpALAPGR-DVPRWMLAMS-----RFISRVWPSFPAIRIDAALLSrdpAIVAANRADplvhhdavpa 235
Cdd:COG3208    95 RRGRPLpAHLFVSG-RRAPHLpRRRRPLHDLSdaellAELRRLGGTPEEVLADPELLE---LFLPILRAD---------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 236 rtgAELLDAMARIERGRgsLRVPVLIYHGTSDKLTEPDGSRAFGAHVGSPDRtLTLYEGG--FHETmndlERERVIDALI 313
Cdd:COG3208   161 ---FRLLETYRYTPGPP--LDCPITALGGDDDPLVSPEELAAWREHTTGPFR-LRVFPGGhfFLRD----HPAELLALIR 230

                  ....*..
gi 1780267313 314 AWIHAHA 320
Cdd:COG3208   231 AALAALA 237
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
65-176 1.54e-09

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.45  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  65 SAPPRATVALVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAwvERFDDYLNDADAlvaeaARGNTPLFLM 144
Cdd:COG1075     1 YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSA--EQLAAFVDAVLA-----ATGAEKVDLV 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1780267313 145 GHSMGGaIAALYAIERLPASGHtLAGLV-LSSP 176
Cdd:COG1075    74 GHSMGG-LVARYYLKRLGGAAK-VARVVtLGTP 104
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
62-182 9.03e-09

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 54.50  E-value: 9.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  62 ADGSAPPRATVALVHGLAehAGR----YERLAARLNAAGISVLAIDL--RGHGRSPGKRAwverfdDYLNDADALVAEAA 135
Cdd:COG3571     2 TEGPEDPRATLLLAHGAG--AGMdspfMVALAEALAAAGIAVARFEFpyMVAGRRPPDRA------PVLDAAWRAVIAAL 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780267313 136 RG---NTPLFLMGHSMGGAIAALYAIERLPASGHtlagLVLSSPALAPGR 182
Cdd:COG3571    74 RArlaGLPLVIGGKSMGGRVASMLAAEGGGAAGL----VCLGYPFHPPGK 119
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
46-178 5.29e-08

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 53.28  E-value: 5.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  46 LRTADGLELASYRWPAADGsapPRATVALVHGLAEHAGRYERLAA----RLNAAGISVLAIDLRGHGRSPGKRAwVERFD 121
Cdd:TIGR03101   5 LDAPHGFRFCLYHPPVAVG---PRGVVIYLPPFAEEMNKSRRMVAlqarAFAAGGFGVLQIDLYGCGDSAGDFA-AARWD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1780267313 122 DYLNDADALVA-EAARGNTPLFLMGHSMGGAIAALYAIeRLPASghtLAGLVLSSPAL 178
Cdd:TIGR03101  81 VWKEDVAAAYRwLIEQGHPPVTLWGLRLGALLALDAAN-PLAAK---CNRLVLWQPVV 134
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
74-237 1.55e-07

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 51.32  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  74 LVHGLAEHAGRYerlaARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAargntPLFLMGHSMGGAIA 153
Cdd:pfam12697   3 LVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAAR-----PVVLVGHSLGGAVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 154 ALYaierlpASGHTLAGLVLSSPALAPGRDVPRWMLAMSRFISRVWPSFPAIRIDAALLSRDPAIVAANRADPLVHHDAV 233
Cdd:pfam12697  74 LAA------AAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALL 147

                  ....
gi 1780267313 234 PART 237
Cdd:pfam12697 148 AALA 151
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
68-181 1.24e-06

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 48.35  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  68 PRATVALVHGlaehAGR------YERLAARLNAAGISVLAID-------LRGHGRSPGKRAwvERFDDYLNDAdalVAEA 134
Cdd:pfam20408   1 PKARLLLAHG----AGAgmdspfMQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRA--PKLLEAFRAV---IAAL 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1780267313 135 ARGNTPLFLMGHSMGGAIAALYAierlpASGHTLAGLVLSSPALAPG 181
Cdd:pfam20408  72 RGPDLPLFIGGKSMGGRVASLLA-----DDSGVKGVIALGYPFHPPG 113
YpfH COG0400
Predicted esterase [General function prediction only];
65-193 1.78e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 44.90  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  65 SAPPRATVALVHGLAEHAGRYERLAARLNAAGISVLAidLRG-HGRSPGKRAW--------------VERFDDYLNDA-D 128
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLA--PRApVPEGPGGRAWfdlsflegredeegLAAAAEALAAFiD 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780267313 129 ALVAEAARGNTPLFLMGHSMGGAIAALYAIERlpasGHTLAGLVLSSPALAPGRDVPRWMLAMSR 193
Cdd:COG0400    79 ELEARYGIDPERIVLAGFSQGAAMALSLALRR----PELLAGVVALSGYLPGEEALPAPEAALAG 139
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
70-314 1.95e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 45.71  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  70 ATVALVHGLAEHAGRYERLAARLnAAGISVLAIDLRGHGRSpGKRAWVERFDDYlndADALVAE-AARGNTPLFLMGHSM 148
Cdd:PRK14875  132 TPVVLIHGFGGDLNNWLFNHAAL-AAGRPVIALDLPGHGAS-SKAVGAGSLDEL---AAAVLAFlDALGIERAHLVGHSM 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 149 GGAIAALYAIERlPASghtLAGLVLSSPAlAPGRDVPRWMLamSRFISRvwPSFPAIRIDAALLSRDPAIVAANRADPLV 228
Cdd:PRK14875  207 GGAVALRLAARA-PQR---VASLTLIAPA-GLGPEINGDYI--DGFVAA--ESRRELKPVLELLFADPALVTRQMVEDLL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 229 HH---DAVPARTGAeLLDAMARIERGRGSLR-------VPVLIYHGTSDKLTEPDGSRAFGAHVgspdrTLTLYEGGFHe 298
Cdd:PRK14875  278 KYkrlDGVDDALRA-LADALFAGGRQRVDLRdrlaslaIPVLVIWGEQDRIIPAAHAQGLPDGV-----AVHVLPGAGH- 350
                         250
                  ....*....|....*.
gi 1780267313 299 tMNDLERERVIDALIA 314
Cdd:PRK14875  351 -MPQMEAAADVNRLLA 365
PRK05855 PRK05855
SDR family oxidoreductase;
48-149 2.56e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 45.74  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  48 TADGLELASYRWpaadgSAPPRATVALVHGLAEHAGRYERLAARLnAAGISVLAIDLRGHGRS---PGKRAWveRFDDYL 124
Cdd:PRK05855    9 SSDGVRLAVYEW-----GDPDRPTVVLVHGYPDNHEVWDGVAPLL-ADRFRVVAYDVRGAGRSsapKRTAAY--TLARLA 80
                          90       100
                  ....*....|....*....|....*
gi 1780267313 125 NDADAlVAEAARGNTPLFLMGHSMG 149
Cdd:PRK05855   81 DDFAA-VIDAVSPDRPVHLLAHDWG 104
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
98-173 2.68e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 44.83  E-value: 2.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780267313  98 SVLAIDLRGHGRSPGKRawVERFDDylndADALVAE--AARGNTPLFLMGHSMGGAIAALYAIERLPAsghTLAGLVL 173
Cdd:PRK11126   29 PRLYIDLPGHGGSAAIS--VDGFAD----VSRLLSQtlQSYNILPYWLVGYSLGGRIAMYYACQGLAG---GLCGLIV 97
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
88-295 9.10e-05

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 43.79  E-value: 9.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  88 LAARLNAAGISVLAIDLRghgrSPGKR-AWVeRFDDYLNDA--DAL-VAEAARGNTPLFLMGHSMGGAIAALYAiERLPA 163
Cdd:COG3243   227 LVRYLVDQGFTVFLISWG----NPDAEdRDL-GLDDYVEDGilAAVdAVREITGEDKVNLLGYCLGGTLLAIYA-ALLAA 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 164 SGHT-LAGLVL-----------------SSPALAPGRD-------VPRWMLA----MSRFISRVWPSFpairIDAALLSR 214
Cdd:COG3243   301 RGPDrVASLTLlatpldfsepgelgvfiDESQLADLEAlmaakgyLPGRLMAgafsLLRPNDLIWSYY----VNNYLLGE 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 215 DPAIVAANR--ADPLvhhdAVPARTGAELL------DAMA--RIE-RGR----GSLRVPVLIYHGTSDKLTEPDGSRAFG 279
Cdd:COG3243   377 NPPPFDLLYwnADST----RLPGRMHSQYLrdlyleNRLAkgELElGGRpvdlSDITVPVLVVAGEEDHIAPWRSVYALA 452
                         250
                  ....*....|....*.
gi 1780267313 280 AHVGSPDRTLTLYEGG 295
Cdd:COG3243   453 QLVGGKDVTFVLAPGG 468
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
59-303 3.91e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 41.63  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  59 WPAADGS-APPRATVALV---HGLAEHAGRYERLAARLNAAGISVLAID------------LRGHGRSPGKRAWVERFDD 122
Cdd:COG4188    48 YPATAPAdAPAGGPFPLVvlsHGLGGSREGYAYLAEHLASHGYVVAAPDhpgsnaadlsaaLDGLADALDPEELWERPLD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 123 YLNDADALvaEAARGNTPLF----------LMGHSMGGAIAALyaierlpasghtLAGLVLSSPALAPGRDVPRWMLAMS 192
Cdd:COG4188   128 LSFVLDQL--LALNKSDPPLagrldldrigVIGHSLGGYTALA------------LAGARLDFAALRQYCGKNPDLQCRA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313 193 RFISRVWPSFpairidaallsRDPAIVAANRADPLVHHDAVPartgaellDAMARIergrgslRVPVLIYHGTSDKLT-E 271
Cdd:COG4188   194 LDLPRLAYDL-----------RDPRIKAVVALAPGGSGLFGE--------EGLAAI-------TIPVLLVAGSADDVTpA 247
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1780267313 272 PDGSRAFGAHVGSPDRTLTLYEGGFHETMNDL 303
Cdd:COG4188   248 PDEQIRPFDLLPGADKYLLTLEGATHFSFLDP 279
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
70-180 1.06e-03

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 40.04  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  70 ATVALVHGLA-------------EHAGRYERLAA-RLNAAGISVLAIDLRG-----HGRSpgkrawVERFDDYLNDADA- 129
Cdd:pfam07819   5 IPVLFIPGNAgsykqvrsiasvaANLYQVLRKLLqNDNGFHLDFFSVDFNEelsafHGRT------LLDQAEYLNDAIRy 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1780267313 130 ---LVAEAARGNTPLFLMGHSMGG--AIAALYAIERLPASGHTLagLVLSSPALAP 180
Cdd:pfam07819  79 ilsLYASGRPGPTSVILIGHSMGGivARAALTLPNYIPQSVNTI--ITLSSPHAKP 132
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
85-185 1.24e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 39.68  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  85 YERLAARLNAaGISVLAIDLRGHGRSPGKRAWVERFDDYLndADALVAEAARGntPLFLMGHSMGGAIAalYAI-ERLPA 163
Cdd:pfam00975  16 FRSLARRLPP-PAEVLAVQYPGRGRGEPPLNSIEALADEY--AEALRQIQPEG--PYALFGHSMGGMLA--FEVaRRLER 88
                          90       100
                  ....*....|....*....|..
gi 1780267313 164 SGHTLAGLVLSSpALAPGRDVP 185
Cdd:pfam00975  89 QGEAVRSLFLSD-ASAPHTVRY 109
PLN02965 PLN02965
Probable pheophorbidase
74-151 5.62e-03

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 37.98  E-value: 5.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780267313  74 LVHGLAEHAGRYERLAARLNAAGISVLAIDLRGHGRSPGKRAWVERFDDYLNDADALVAEAArGNTPLFLMGHSMGGA 151
Cdd:PLN02965    8 FVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLP-PDHKVILVGHSIGGG 84
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
126-213 6.21e-03

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 37.20  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  126 DADALVAEAAR------GNTPLFLMGHSMGGAIAALYAiERLPASGHTLAGLVLSSPALAPGRDVPRWMLAMSRFISRVW 199
Cdd:smart00824  45 SADALVEAQAEavlraaGGRPFVLVGHSSGGLLAHAVA-ARLEARGIPPAAVVLLDTYPPGDPAPEGWLPELLRGVFERE 123
                           90
                   ....*....|....
gi 1780267313  200 PSFpaIRIDAALLS 213
Cdd:smart00824 124 DSF--VPMDDARLT 135
PRK10673 PRK10673
esterase;
57-163 9.27e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.02  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780267313  57 YRWPAADG--SAPPratVALVHGLAehaGRYERLA--ARLNAAGISVLAIDLRGHGRSPgkraWVERFD------DYLND 126
Cdd:PRK10673    5 IRAQTAQNphNNSP---IVLVHGLF---GSLDNLGvlARDLVNDHDIIQVDMRNHGLSP----RDPVMNypamaqDLLDT 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1780267313 127 ADALVAEAArgntplFLMGHSMGGAIA-ALYA-----IERLPA 163
Cdd:PRK10673   75 LDALQIEKA------TFIGHSMGGKAVmALTAlapdrIDKLVA 111
 
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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