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Conserved domains on  [gi|1335171613|ref|XP_023619429|]
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protein ABHD4 isoform X3 [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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN02894 super family cl30398
hydrolase, alpha/beta fold family protein
 32-314 1.07e-64

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: 209.00  E-value: 1.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  32 IWTVTVsPELRDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFP-RDPEGAENEFVMSIETWRET 110
Cdd:PLN02894   94 INTVTF-DSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 111 MGIPSMILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSE--IRAPPTWVKAVASVLGRSN--PLAVLRIA 186
Cdd:PLN02894  173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 187 GPWGPGLVQRFRpdfKRKFADFFEDDTISE--------YIYHCNAQNPSGETAFKAMMESFGWARRPMIERIHLIRkdVP 258
Cdd:PLN02894  253 GPWGPNLVRRYT---TARFGAHSTGDILSEeesklltdYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VP 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1335171613 259 ITMIYGSNTWIDTSTGKKV--KLQRPDSYVRdmeIEGASHHVYADQPHIFNAVVEEIC 314
Cdd:PLN02894  328 TTFIYGRHDWMNYEGAVEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 32-314 1.07e-64

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 209.00  E-value: 1.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  32 IWTVTVsPELRDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFP-RDPEGAENEFVMSIETWRET 110
Cdd:PLN02894   94 INTVTF-DSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 111 MGIPSMILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSE--IRAPPTWVKAVASVLGRSN--PLAVLRIA 186
Cdd:PLN02894  173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 187 GPWGPGLVQRFRpdfKRKFADFFEDDTISE--------YIYHCNAQNPSGETAFKAMMESFGWARRPMIERIHLIRkdVP 258
Cdd:PLN02894  253 GPWGPNLVRRYT---TARFGAHSTGDILSEeesklltdYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VP 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1335171613 259 ITMIYGSNTWIDTSTGKKV--KLQRPDSYVRdmeIEGASHHVYADQPHIFNAVVEEIC 314
Cdd:PLN02894  328 TTFIYGRHDWMNYEGAVEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 42-317 5.53e-27

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: 105.47  E-value: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  42 RDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEgaenEFVMSIETWRETMGIPSMILLGH 121
Cdd:COG0596    21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 122 SLGGFLATSYSIKYPERVKHLILVDpwgfplrptdpseirapptwvkavasvlgrsnplavlriagpwgpglvqrfrpDF 201
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------EV 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 202 KRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMIERIhlirkDVPITMIYGSN-TWIDTSTGKKVKL 279
Cdd:COG0596   124 LAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKdPIVPPALARRLAE 185

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1335171613 280 QRPDSYVRdmEIEGASHHVYADQPHIFNAVVEEICDSV 317
Cdd:COG0596   186 LLPNAELV--VLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 45-303 1.81e-22

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: 93.72  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  45 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPtfPRDPEGAENEFVMSIETWRETMGIPSMILLGHSL 123
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 124 GGFLATSYSIKYPERVKHLILVDP--WGFPLRPTDPSEIRAPPTWVKAVASVLGRsNPLAVLrIAGPWGPGLV-QRFRPD 200
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAP-NPLGRL-VAKLLALLLLrLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 201 FKRKFADFFEDDtiseyiyhcnAQNPSGETAFKAMMESfGWARRPMIERIHliRKDVPITMIYGSNTWIDTSTGkKVKLQ 280
Cdd:pfam00561 157 LPLLNKRFPSGD----------YALAKSLVTGALLFIE-TWSTELRAKFLG--RLDEPTLIIWGDQDPLVPPQA-LEKLA 222

                         250       260
                  ....*....|....*....|...
gi 1335171613 281 RPDSYVRDMEIEGASHHVYADQP 303
Cdd:pfam00561 223 QLFPNARLVVIPDAGHFAFLEGP 245
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 117-187 3.23e-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: 41.85  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 117 ILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAP------------PTWVKAVASVlgrSNPLAVLR 184
Cdd:cd12808   191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                  ...
gi 1335171613 185 IAG 187
Cdd:cd12808   268 AAG 270
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 32-314 1.07e-64

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 209.00  E-value: 1.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  32 IWTVTVsPELRDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFP-RDPEGAENEFVMSIETWRET 110
Cdd:PLN02894   94 INTVTF-DSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 111 MGIPSMILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSE--IRAPPTWVKAVASVLGRSN--PLAVLRIA 186
Cdd:PLN02894  173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 187 GPWGPGLVQRFRpdfKRKFADFFEDDTISE--------YIYHCNAQNPSGETAFKAMMESFGWARRPMIERIHLIRkdVP 258
Cdd:PLN02894  253 GPWGPNLVRRYT---TARFGAHSTGDILSEeesklltdYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VP 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1335171613 259 ITMIYGSNTWIDTSTGKKV--KLQRPDSYVRdmeIEGASHHVYADQPHIFNAVVEEIC 314
Cdd:PLN02894  328 TTFIYGRHDWMNYEGAVEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 42-317 5.53e-27

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: 105.47  E-value: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  42 RDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEgaenEFVMSIETWRETMGIPSMILLGH 121
Cdd:COG0596    21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 122 SLGGFLATSYSIKYPERVKHLILVDpwgfplrptdpseirapptwvkavasvlgrsnplavlriagpwgpglvqrfrpDF 201
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------EV 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 202 KRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMIERIhlirkDVPITMIYGSN-TWIDTSTGKKVKL 279
Cdd:COG0596   124 LAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKdPIVPPALARRLAE 185

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1335171613 280 QRPDSYVRdmEIEGASHHVYADQPHIFNAVVEEICDSV 317
Cdd:COG0596   186 LLPNAELV--VLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 45-303 1.81e-22

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: 93.72  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  45 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPtfPRDPEGAENEFVMSIETWRETMGIPSMILLGHSL 123
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 124 GGFLATSYSIKYPERVKHLILVDP--WGFPLRPTDPSEIRAPPTWVKAVASVLGRsNPLAVLrIAGPWGPGLV-QRFRPD 200
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAP-NPLGRL-VAKLLALLLLrLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 201 FKRKFADFFEDDtiseyiyhcnAQNPSGETAFKAMMESfGWARRPMIERIHliRKDVPITMIYGSNTWIDTSTGkKVKLQ 280
Cdd:pfam00561 157 LPLLNKRFPSGD----------YALAKSLVTGALLFIE-TWSTELRAKFLG--RLDEPTLIIWGDQDPLVPPQA-LEKLA 222

                         250       260
                  ....*....|....*....|...
gi 1335171613 281 RPDSYVRDMEIEGASHHVYADQP 303
Cdd:pfam00561 223 QLFPNARLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-150 3.46e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 81.14  E-value: 3.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  43 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrptfPRDPEGAENEFVMSIETWRETMGIPSMILLGHS 122
Cdd:PRK14875  130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS----KAVGAGSLDELAAAVLAFLDALGIERAHLVGHS 205

                          90       100
                  ....*....|....*....|....*...
gi 1335171613 123 LGGFLATSYSIKYPERVKHLILVDPWGF 150
Cdd:PRK14875  206 MGGAVALRLAARAPQRVASLTLIAPAGL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
39-148 1.04e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 71.96  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  39 PELRDRTPLVMVHGFGGGVGLWILNMDSLSARR-TLHTFDLLGFGRSSRPT-FPRDPEGAENEFVMSIETWRETMGIPsM 116
Cdd:COG2267    23 PAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPRgHVDSFDDYVDDLRAALDALRARPGLP-V 101

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1335171613 117 ILLGHSLGGFLATSYSIKYPERVKHLILVDPW 148
Cdd:COG2267   102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
PLN02578 PLN02578
hydrolase
 46-160 6.89e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 65.25  E-value: 6.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  46 PLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEGAENEFvmsIETWRETMGIPSmILLGHSLGG 125
Cdd:PLN02578   88 PIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQV---ADFVKEVVKEPA-VLVGNSLGG 163

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1335171613 126 FLATSYSIKYPERVKHLILVDP---WGFPLRPTDPSEI 160
Cdd:PLN02578  164 FTALSTAVGYPELVAGVALLNSagqFGSESREKEEAIV 201
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 45-147 5.59e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 59.37  E-value: 5.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  45 TPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPtfprDPEGAENEFVMSIETW--------RETMGIPSM 116
Cdd:PLN02824   30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWgeqlndfcSDVVGDPAF 105

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171613 117 ILLgHSLGGFLATSYSIKYPERVKHLILVDP 147
Cdd:PLN02824  106 VIC-NSVGGVVGLQAAVDAPELVRGVMLINI 135
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 33-146 1.53e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 58.31  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  33 WTVTVSPELRDRTP-LVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTfprdpegaenEFVMSIETW---- 107
Cdd:PLN02679   76 YLVKGSPEVTSSGPpVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP----------GFSYTMETWaeli 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1335171613 108 ----RETMGIPSmILLGHSLGGF---LATSYSikYPERVKHLILVD 146
Cdd:PLN02679  146 ldflEEVVQKPT-VLIGNSVGSLacvIAASES--TRDLVRGLVLLN 188
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 47-309 1.62e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 57.10  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  47 LVMVHGFGGGVGLWIlnmDSLSARRTLHTFDLLGFGRSSRPTFPRDPEGAENEFVmsietwRETMGIPSMILLGHSLGGF 126
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALL------DELGAARPVVLVGHSLGGA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 127 LATSYsikYPERVKHLILVDPWGFPLRPTDPseirapptwvkavasvlgrsnplAVLRIAGPWGPGLVQRFRPDFKRkfA 206
Cdd:pfam12697  72 VALAA---AAAALVVGVLVAPLAAPPGLLAA-----------------------LLALLARLGAALAAPAWLAAESL--A 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 207 DFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPmierihlirkdVPITMIYGSNTWIDTSTGKKVKLQRPDSYV 286
Cdd:pfam12697 124 RGFLDDLPADAEWAAALARLAALLAALALLPLAAWRDLP-----------VPVLVLAEEDRLVPELAQRLLAALAGARLV 192

                         250       260
                  ....*....|....*....|...
gi 1335171613 287 rdmEIEGASHHVYaDQPHIFNAV 309
Cdd:pfam12697 193 ---VLPGAGHLPL-DDPEEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 47-206 1.69e-09

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: 57.22  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  47 LVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLLGFGRSS--RPTFPRDpegaeNEFVMS----IETWRETMGIPSMILL 119
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDgkRGHVPSF-----DDYVDDldtfVDKIREEHPGLPLFLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 120 GHSLGGFLATSYSIKYPERVKHLILVDPWgfpLRPTDPSeiraPPTWVKAVASVLGRSNPLavLRIAGPWGPGLVQRfRP 199
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPA---LKIKPYL----APPILKLLAKLLGKLFPR--LRVPNNLLPDSLSR-DP 151


                  ....*..
gi 1335171613 200 DFKRKFA 206
Cdd:pfam12146 152 EVVAAYA 158
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 48-171 3.93e-09

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 57.51  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  48 VMVHGFGGGVGLWILNM-----DSLSARRTLHTFDLLGFGRSSRPTfprDPEGAENEFVMSIE-TWRETMGIPSMILLGH 121
Cdd:PLN03087  205 LFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPKPA---DSLYTLREHLEMIErSVLERYKVKSFHIVAH 281

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335171613 122 SLGGFLATSYSIKYPERVKHLILVDPWGFPLrptdPSEIRAPPTWVKAVA 171
Cdd:PLN03087  282 SLGCILALALAVKHPGAVKSLTLLAPPYYPV----PKGVQATQYVMRKVA 327
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
30-145 9.14e-09

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 55.41  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  30 NKIWTVTVSpelRDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrpTFprdpeGAenefvMSIETWRE 109
Cdd:PRK10349    2 NNIWWQTKG---QGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR--GF-----GA-----LSLADMAE 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1335171613 110 TM---GIPSMILLGHSLGGFLATSYSIKYPERVKHLILV 145
Cdd:PRK10349   67 AVlqqAPDKAIWLGWSLGGLVASQIALTHPERVQALVTV 105
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 43-147 1.00e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 52.14  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  43 DRTPLVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLlgfgrssrPTFPRDPEGAENEFVMSIETWRETMGIPSMILLGH 121
Cdd:COG1075     4 TRYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNY--------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGH 75

                          90       100
                  ....*....|....*....|....*...
gi 1335171613 122 SLGGFLATSY--SIKYPERVKHLILVDP 147
Cdd:COG1075    76 SMGGLVARYYlkRLGGAAKVARVVTLGT 103
PRK10673 PRK10673
esterase;
43-184 4.28e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.42  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  43 DRTPLVMVHG-FGGGVGLWILNMDsLSARRTLHTFDLLGFGRSsrptfPRDPEGAENEFVMSIETWRETMGIPSMILLGH 121
Cdd:PRK10673   15 NNSPIVLVHGlFGSLDNLGVLARD-LVNDHDIIQVDMRNHGLS-----PRDPVMNYPAMAQDLLDTLDALQIEKATFIGH 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335171613 122 SLGGFLATSYSIKYPERVKHLILVD--PWGFPLRPTDpsEIRAPPTWVKAvASVLGRSNPLAVLR 184
Cdd:PRK10673   89 SMGGKAVMALTALAPDRIDKLVAIDiaPVDYHVRRHD--EIFAAINAVSE-AGATTRQQAAAIMR 150
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
48-311 4.32e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 44.16  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  48 VMVHGFGGG---VGLWilnmdslsARR------TLHTFDLLGFGRSSRPTFPRDPE----GAENEFVMSIETWRETmgip 114
Cdd:COG1647    19 LLLHGFTGSpaeMRPL--------AEAlakagyTVYAPRLPGHGTSPEDLLKTTWEdwleDVEEAYEILKAGYDKV---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 115 smILLGHSLGGFLATSYSIKYPErVKHLILVDPwgfPLRPTDPSEIRAPptwvkavasvlgrsnplavlriagpwgpgLV 194
Cdd:COG1647    87 --IVIGLSMGGLLALLLAARYPD-VAGLVLLSP---ALKIDDPSAPLLP-----------------------------LL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 195 QRFRPdFKRKFADFFEDDTISEYIYHCNAQNpsgetAFKAMMESFGWARRpmieriHLIRKDVPITMIYGSN-TWIDTST 273
Cdd:COG1647   132 KYLAR-SLRGIGSDIEDPEVAEYAYDRTPLR-----ALAELQRLIREVRR------DLPKITAPTLIIQSRKdEVVPPES 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1335171613 274 GKKVKLQRPDSYVRDMEIEGASH--HVYADQPHIFNAVVE 311
Cdd:COG1647   200 ARYIYERLGSPDKELVWLEDSGHviTLDKDREEVAEEILD 239
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 46-156 9.49e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 43.44  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  46 PLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPtfprDPEGAENEFVMSIETWRETMGIPSMILLGHSLGG 125
Cdd:PRK03592   29 PIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP----DIDYTFADHARYLDAWFDALGLDDVVLVGHDWGS 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171613 126 FLATSYSIKYPERVKHLILVDPWgfpLRPTD 156
Cdd:PRK03592  105 ALGFDWAARHPDRVRGIAFMEAI---VRPMT 132
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 117-187 3.23e-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: 41.85  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613 117 ILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAP------------PTWVKAVASVlgrSNPLAVLR 184
Cdd:cd12808   191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                  ...
gi 1335171613 185 IAG 187
Cdd:cd12808   268 AAG 270
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 47-148 1.85e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.13  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  47 LVMVHGFGGGVGLWILNMDSLsARRTLHT--FDLLGFGRSS-RPTFPRDPEGaenefvMSIETW----RETMGIPS--MI 117
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRL-AELGFNVlaFDYRGYGESEgEPREEGSPER------RDARAAvdylRTLPGVDPerIG 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335171613 118 LLGHSLGGFLATSYSIKYPeRVKHLILVDPW 148
Cdd:COG1073   113 LLGISLGGGYALNAAATDP-RVKAVILDSPF 142
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 115-163 4.48e-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: 4.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335171613 115 SMILLGHSLGGflATSY-SIKYPERVKHLILVDPWGFPLRPTDPSEIRAP 163
Cdd:pfam03403 222 KIAVIGHSFGG--ATVIqSLSEDTRFRCGIALDAWMFPVGDDVYSKARQP 269
YpfH COG0400
Predicted esterase [General function prediction only];
47-144 4.79e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335171613  47 LVMVHGFGG----GVGLWilnmDSLSARRTLH-----TFDLLGFGRS----SRPTFPRDPEGAEN---EFVMSIETWRET 110
Cdd:COG0400     8 VVLLHGYGGdeedLLPLA----PELALPGAAVlapraPVPEGPGGRAwfdlSFLEGREDEEGLAAaaeALAAFIDELEAR 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1335171613 111 MGIPS--MILLGHSLGGFLATSYSIKYPERVKHLIL 144
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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