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Conserved domains on  [gi|1335171617|ref|XP_023619430|]
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protein ABHD4 isoform X4 [Myotis lucifugus]

Protein Classification

alpha/beta hydrolase domain-containing protein( domain architecture ID 1005082)

alpha/beta hydrolase (abhydrolase) domain-containing protein

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02894 super family cl30398
hydrolase, alpha/beta fold family protein
68-277 6.81e-42

hydrolase, alpha/beta fold family protein


The actual alignment was detected with superfamily member PLN02894:

Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 148.52  E-value: 6.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617  68 RPQGWLSSWLpAWRPTSMSQLKNVEAKILQCLQNKFLARYVSL----PNQNKIWTVTVSPELR-----------DRTPLV 132
Cdd:PLN02894   31 RTRSLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEPRfintvtfdskeDAPTLV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 133 MVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFP-RDPEGAENEFVMSIETWRETMGIPSMILLGHSLGGFL 211
Cdd:PLN02894  110 MVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYV 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335171617 212 ATSYSIKYPERVKHLILVDPWGFPLRPTDPSE--IRAPPTWVKAVASVLGRSN--PLAVLRIAGPW---VVRR 277
Cdd:PLN02894  190 AAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWgpnLVRR 262
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
68-277 6.81e-42

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 148.52  E-value: 6.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617  68 RPQGWLSSWLpAWRPTSMSQLKNVEAKILQCLQNKFLARYVSL----PNQNKIWTVTVSPELR-----------DRTPLV 132
Cdd:PLN02894   31 RTRSLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEPRfintvtfdskeDAPTLV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 133 MVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFP-RDPEGAENEFVMSIETWRETMGIPSMILLGHSLGGFL 211
Cdd:PLN02894  110 MVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYV 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335171617 212 ATSYSIKYPERVKHLILVDPWGFPLRPTDPSE--IRAPPTWVKAVASVLGRSN--PLAVLRIAGPW---VVRR 277
Cdd:PLN02894  190 AAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWgpnLVRR 262
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
126-272 1.94e-24

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: 97.76  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 126 RDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEgaenEFVMSIETWRETMGIPSMILLGH 205
Cdd:COG0596    21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGH 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335171617 206 SLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAPPTWVKAVASVLGRSNPLAVLRIAGP 272
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVP 163
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
129-262 1.52e-21

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: 90.64  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 129 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPtfPRDPEGAENEFVMSIETWRETMGIPSMILLGHSL 207
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1335171617 208 GGFLATSYSIKYPERVKHLILVDP--WGFPLRPTDPSEIRAPPTWVKAVASVLGRSN 262
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPNP 135
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
201-271 3.71e-04

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 41.46  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 201 ILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAP------------PTWVKAVASVlgrSNPLAVLR 268
Cdd:cd12808   191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267

                  ...
gi 1335171617 269 IAG 271
Cdd:cd12808   268 AAG 270
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
68-277 6.81e-42

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 148.52  E-value: 6.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617  68 RPQGWLSSWLpAWRPTSMSQLKNVEAKILQCLQNKFLARYVSL----PNQNKIWTVTVSPELR-----------DRTPLV 132
Cdd:PLN02894   31 RTRSLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEPRfintvtfdskeDAPTLV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 133 MVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFP-RDPEGAENEFVMSIETWRETMGIPSMILLGHSLGGFL 211
Cdd:PLN02894  110 MVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYV 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335171617 212 ATSYSIKYPERVKHLILVDPWGFPLRPTDPSE--IRAPPTWVKAVASVLGRSN--PLAVLRIAGPW---VVRR 277
Cdd:PLN02894  190 AAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWgpnLVRR 262
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
126-272 1.94e-24

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: 97.76  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 126 RDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEgaenEFVMSIETWRETMGIPSMILLGH 205
Cdd:COG0596    21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGH 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335171617 206 SLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAPPTWVKAVASVLGRSNPLAVLRIAGP 272
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVP 163
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
129-262 1.52e-21

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: 90.64  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 129 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPtfPRDPEGAENEFVMSIETWRETMGIPSMILLGHSL 207
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1335171617 208 GGFLATSYSIKYPERVKHLILVDP--WGFPLRPTDPSEIRAPPTWVKAVASVLGRSN 262
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPNP 135
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
127-234 2.79e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 80.76  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 127 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrptfPRDPEGAENEFVMSIETWRETMGIPSMILLGHS 206
Cdd:PRK14875  130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS----KAVGAGSLDELAAAVLAFLDALGIERAHLVGHS 205
                          90       100
                  ....*....|....*....|....*...
gi 1335171617 207 LGGFLATSYSIKYPERVKHLILVDPWGF 234
Cdd:PRK14875  206 MGGAVALRLAARAPQRVASLTLIAPAGL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
123-232 6.80e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 71.96  E-value: 6.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 123 PELRDRTPLVMVHGFGGGVGLWILNMDSLSARR-TLHTFDLLGFGRSSRPT-FPRDPEGAENEFVMSIETWRETMGIPsM 200
Cdd:COG2267    23 PAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPRgHVDSFDDYVDDLRAALDALRARPGLP-V 101
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1335171617 201 ILLGHSLGGFLATSYSIKYPERVKHLILVDPW 232
Cdd:COG2267   102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
PLN02578 PLN02578
hydrolase
130-244 1.89e-11

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 63.71  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 130 PLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEGAENEFvmsIETWRETMGIPSmILLGHSLGG 209
Cdd:PLN02578   88 PIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQV---ADFVKEVVKEPA-VLVGNSLGG 163
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1335171617 210 FLATSYSIKYPERVKHLILVDP---WGFPLRPTDPSEI 244
Cdd:PLN02578  164 FTALSTAVGYPELVAGVALLNSagqFGSESREKEEAIV 201
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
131-278 7.41e-10

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: 57.99  E-value: 7.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 131 LVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLLGFGRSS--RPTFPRDpegaeNEFVMS----IETWRETMGIPSMILL 203
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDgkRGHVPSF-----DDYVDDldtfVDKIREEHPGLPLFLL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335171617 204 GHSLGGFLATSYSIKYPERVKHLILVDPWgfpLRPTDPSeiraPPTWVKAVASVLGRSNP-LAVL-RIAGPWVVRRP 278
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPA---LKIKPYL----APPILKLLAKLLGKLFPrLRVPnNLLPDSLSRDP 151
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
129-231 8.58e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 58.21  E-value: 8.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 129 TPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPtfprDPEGAENEFVMSIETW--------RETMGIPSM 200
Cdd:PLN02824   30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWgeqlndfcSDVVGDPAF 105
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171617 201 ILLgHSLGGFLATSYSIKYPERVKHLILVDP 231
Cdd:PLN02824  106 VIC-NSVGGVVGLQAAVDAPELVRGVMLINI 135
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
132-255 4.48e-09

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 56.74  E-value: 4.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 132 VMVHGFGGGVGLWILNM-----DSLSARRTLHTFDLLGFGRSSRPTfprDPEGAENEFVMSIE-TWRETMGIPSMILLGH 205
Cdd:PLN03087  205 LFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPKPA---DSLYTLREHLEMIErSVLERYKVKSFHIVAH 281
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335171617 206 SLGGFLATSYSIKYPERVKHLILVDPWGFPLrptdPSEIRAPPTWVKAVA 255
Cdd:PLN03087  282 SLGCILALALAVKHPGAVKSLTLLAPPYYPV----PKGVQATQYVMRKVA 327
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
117-208 1.29e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 55.23  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 117 WTVTVSPELRDRTP-LVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTfprdpegaenEFVMSIETW---- 191
Cdd:PLN02679   76 YLVKGSPEVTSSGPpVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP----------GFSYTMETWaeli 145
                          90       100
                  ....*....|....*....|.
gi 1335171617 192 ----RETMGIPSmILLGHSLG 208
Cdd:PLN02679  146 ldflEEVVQKPT-VLIGNSVG 165
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
127-231 1.76e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 51.37  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 127 DRTPLVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLlgfgrssrPTFPRDPEGAENEFVMSIETWRETMGIPSMILLGH 205
Cdd:COG1075     4 TRYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNY--------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGH 75
                          90       100
                  ....*....|....*....|....*...
gi 1335171617 206 SLGGFLATSY--SIKYPERVKHLILVDP 231
Cdd:COG1075    76 SMGGLVARYYlkRLGGAAKVARVVTLGT 103
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
114-229 4.38e-08

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 53.10  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 114 NKIWTVTVSpelRDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrpTFprdpeGAENEFVMSIETWRE 193
Cdd:PRK10349    2 NNIWWQTKG---QGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR--GF-----GALSLADMAEAVLQQ 71
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1335171617 194 TMGipSMILLGHSLGGFLATSYSIKYPERVKHLILV 229
Cdd:PRK10349   72 APD--KAIWLGWSLGGLVASQIALTHPERVQALVTV 105
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
131-241 1.57e-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: 50.94  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 131 LVMVHGFGGGVGLWIlnmDSLSARRTLHTFDLLGFGRSSRPTFPRDPEGAENEFVMSIETWRETmgipsmILLGHSLGGF 210
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171617 211 LATSYSikyPERVKHLILVDPWGFPLRPTDP 241
Cdd:pfam12697  72 VALAAA---AAALVVGVLVAPLAAPPGLLAA 99
PRK10673 PRK10673
esterase;
127-268 2.83e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.42  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 127 DRTPLVMVHG-FGGGVGLWILNMDsLSARRTLHTFDLLGFGRSsrptfPRDPEGAENEFVMSIETWRETMGIPSMILLGH 205
Cdd:PRK10673   15 NNSPIVLVHGlFGSLDNLGVLARD-LVNDHDIIQVDMRNHGLS-----PRDPVMNYPAMAQDLLDTLDALQIEKATFIGH 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335171617 206 SLGGFLATSYSIKYPERVKHLILVD--PWGFPLRPTDpsEIRAPPTWVKAvASVLGRSNPLAVLR 268
Cdd:PRK10673   89 SMGGKAVMALTALAPDRIDKLVAIDiaPVDYHVRRHD--EIFAAINAVSE-AGATTRQQAAAIMR 150
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
130-240 9.15e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 43.06  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 130 PLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPtfprDPEGAENEFVMSIETWRETMGIPSMILLGHSLGG 209
Cdd:PRK03592   29 PIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP----DIDYTFADHARYLDAWFDALGLDDVVLVGHDWGS 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171617 210 FLATSYSIKYPERVKHLILVDPWgfpLRPTD 240
Cdd:PRK03592  105 ALGFDWAARHPDRVRGIAFMEAI---VRPMT 132
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
201-271 3.71e-04

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 41.46  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 201 ILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAP------------PTWVKAVASVlgrSNPLAVLR 268
Cdd:cd12808   191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267

                  ...
gi 1335171617 269 IAG 271
Cdd:cd12808   268 AAG 270
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
131-232 1.10e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.51  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 131 LVMVHGFGGGVGLWILNMDSLsARRTLHT--FDLLGFGRSS-RPTFPRDPEGAEnefvmsIETW----RETMGIPS--MI 201
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRL-AELGFNVlaFDYRGYGESEgEPREEGSPERRD------ARAAvdylRTLPGVDPerIG 112
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171617 202 LLGHSLGGFLATSYSIKYPeRVKHLILVDPW 232
Cdd:COG1073   113 LLGISLGGGYALNAAATDP-RVKAVILDSPF 142
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
132-247 3.20e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.00  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 132 VMVHGFGGG---VGLWilnmdslsARR------TLHTFDLLGFGRSSRPTFPRDPE----GAENEFVMSIETWRETmgip 198
Cdd:COG1647    19 LLLHGFTGSpaeMRPL--------AEAlakagyTVYAPRLPGHGTSPEDLLKTTWEdwleDVEEAYEILKAGYDKV---- 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1335171617 199 smILLGHSLGGFLATSYSIKYPErVKHLILVDPwgfPLRPTDPSEIRAP 247
Cdd:COG1647    87 --IVIGLSMGGLLALLLAARYPD-VAGLVLLSP---ALKIDDPSAPLLP 129
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
199-247 3.60e-03

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 38.58  E-value: 3.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335171617 199 SMILLGHSLGGflATSY-SIKYPERVKHLILVDPWGFPLRPTDPSEIRAP 247
Cdd:pfam03403 222 KIAVIGHSFGG--ATVIqSLSEDTRFRCGIALDAWMFPVGDDVYSKARQP 269
YpfH COG0400
Predicted esterase [General function prediction only];
131-228 6.02e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.19  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171617 131 LVMVHGFGG----GVGLWilnmDSLSARRTLH-----TFDLLGFGRS----SRPTFPRDPEGAEN---EFVMSIETWRET 194
Cdd:COG0400     8 VVLLHGYGGdeedLLPLA----PELALPGAAVlapraPVPEGPGGRAwfdlSFLEGREDEEGLAAaaeALAAFIDELEAR 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1335171617 195 MGIPS--MILLGHSLGGFLATSYSIKYPERVKHLIL 228
Cdd:COG0400    84 YGIDPerIVLAGFSQGAAMALSLALRRPELLAGVVA 119
 
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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