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Conserved domains on  [gi|31542303|ref|NP_057090|]
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1-acylglycerol-3-phosphate O-acyltransferase ABHD5 isoform a [Homo sapiens]

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
 1-345 1.56e-47

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: 165.47  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303    1 MAAEEEEVDSADTGERSGWlTGWLP---TWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTP 77
Cdd:PLN02894  14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSKVRWFRSASNEPR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   78 LVLLHGFGGGLGLWAL---------------NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCA 141
Cdd:PLN02894  93 FINTVTFDSKEDAPTLvmvhgygasqgfffrNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  142 LGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLR 215
Cdd:PLN02894 173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIR 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  216 IAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGkmHPDIPV 290
Cdd:PLN02894 251 GLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPT 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31542303  291 SVIFGARSCIDGNSGtsiQSLRPHSYV--KTIAILGAGHYVYADQPEEFNQKVKEIC 345
Cdd:PLN02894 329 TFIYGRHDWMNYEGA---VEARKRMKVpcEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 1-345 1.56e-47

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 165.47  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303    1 MAAEEEEVDSADTGERSGWlTGWLP---TWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTP 77
Cdd:PLN02894  14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSKVRWFRSASNEPR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   78 LVLLHGFGGGLGLWAL---------------NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCA 141
Cdd:PLN02894  93 FINTVTFDSKEDAPTLvmvhgygasqgfffrNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  142 LGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLR 215
Cdd:PLN02894 173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIR 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  216 IAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGkmHPDIPV 290
Cdd:PLN02894 251 GLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPT 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31542303  291 SVIFGARSCIDGNSGtsiQSLRPHSYV--KTIAILGAGHYVYADQPEEFNQKVKEIC 345
Cdd:PLN02894 329 TFIYGRHDWMNYEGA---VEARKRMKVpcEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 104-334 6.30e-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: 90.26  E-value: 6.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   104 VYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWG-FP 182
Cdd:pfam00561  30 VIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDpPH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   183 ERPDLADQDRPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtvteyiyhcnVQTPSG 259
Cdd:pfam00561 108 ELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD-------------YALAKS 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31542303   260 ETAFKNMTIPYgWAKRPMLQRIGKmhPDIPVSVIFGARSCIDGNSGT-SIQSLRPHSYVKTIAilGAGHYVYADQP 334
Cdd:pfam00561 175 LVTGALLFIET-WSTELRAKFLGR--LDEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--DAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 91-343 1.18e-18

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: 83.51  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  91 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRV 170
Cdd:COG0596  39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 171 NHLILVepwgfperpdladqdrpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 250
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 251 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgkmhpDIPVSVIFGARS-CIDGNSGTSIQSLRPHSYVKTIAilGAGHYV 329
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202

                       250
                ....*....|....
gi 31542303 330 YADQPEEFNQKVKE 343
Cdd:COG0596 203 PLEQPEAFAAALRD 216
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 103-197 2.33e-05

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: 45.70  E-value: 2.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 103 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCALgLDKM---ILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 178
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDAL-LDRVgpcIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221

                        90       100
                ....*....|....*....|..
gi 31542303 179 WGFPERPDLADqDRPIP---VW 197
Cdd:cd12808 222 SGAPDPAEAAP-LADVPhllVW 242
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 1-345 1.56e-47

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 165.47  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303    1 MAAEEEEVDSADTGERSGWlTGWLP---TWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTP 77
Cdd:PLN02894  14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSKVRWFRSASNEPR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   78 LVLLHGFGGGLGLWAL---------------NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCA 141
Cdd:PLN02894  93 FINTVTFDSKEDAPTLvmvhgygasqgfffrNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  142 LGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLR 215
Cdd:PLN02894 173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIR 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  216 IAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGkmHPDIPV 290
Cdd:PLN02894 251 GLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPT 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31542303  291 SVIFGARSCIDGNSGtsiQSLRPHSYV--KTIAILGAGHYVYADQPEEFNQKVKEIC 345
Cdd:PLN02894 329 TFIYGRHDWMNYEGA---VEARKRMKVpcEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 104-334 6.30e-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: 90.26  E-value: 6.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   104 VYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWG-FP 182
Cdd:pfam00561  30 VIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDpPH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   183 ERPDLADQDRPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtvteyiyhcnVQTPSG 259
Cdd:pfam00561 108 ELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD-------------YALAKS 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31542303   260 ETAFKNMTIPYgWAKRPMLQRIGKmhPDIPVSVIFGARSCIDGNSGT-SIQSLRPHSYVKTIAilGAGHYVYADQP 334
Cdd:pfam00561 175 LVTGALLFIET-WSTELRAKFLGR--LDEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--DAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 91-343 1.18e-18

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: 83.51  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  91 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRV 170
Cdd:COG0596  39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 171 NHLILVepwgfperpdladqdrpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 250
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 251 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgkmhpDIPVSVIFGARS-CIDGNSGTSIQSLRPHSYVKTIAilGAGHYV 329
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202

                       250
                ....*....|....
gi 31542303 330 YADQPEEFNQKVKE 343
Cdd:COG0596 203 PLEQPEAFAAALRD 216
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 104-236 1.15e-12

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: 66.85  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   104 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESI-EEWRCAlgldKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 178
Cdd:pfam12146  34 VYAYDHRGHGRSDGKRghVPSFDDYVDdlDTFVDKIrEEHPGL----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 31542303   179 WgfperpdLADQDRPIPVWIRALGAALTPFNPlaGLRIAGPFGLSLVQRlRPDFKRKY 236
Cdd:pfam12146 110 A-------LKIKPYLAPPILKLLAKLLGKLFP--RLRVPNNLLPDSLSR-DPEVVAAY 157
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
104-204 2.52e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.41  E-value: 2.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 104 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESIEewrcALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPW 179
Cdd:COG2267  58 VLAFDLRGHGRSDGPRghVDSFDDYVDdlRAALDALR----ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133

                        90       100
                ....*....|....*....|....*.
gi 31542303 180 gfperpDLADQDRPIPV-WIRALGAA 204
Cdd:COG2267 134 ------YRADPLLGPSArWLRALRLA 153
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 76-181 1.40e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 52.64  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   76 TPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEvenqFVESIEEWRCALGLDKMILLGHNLG 155
Cdd:PRK14875 132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDE----LAAAVLAFLDALGIERAHLVGHSMG 207

                         90       100
                 ....*....|....*....|....*.
gi 31542303  156 GFLAAAYSLKYPSRVNHLILVEPWGF 181
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL 233
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 104-339 5.96e-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: 49.78  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   104 VYAFDLLGFGRSSRPRFD-SDAEEVENqFVESIEEWRCAlgldkmILLGHNLGGFLAAAYSlkyPSRVNHLILVEPWGFP 182
Cdd:pfam12697  24 VLAPDLPGHGSSSPPPLDlADLADLAA-LLDELGAARPV------VLVGHSLGGAVALAAA---AAALVVGVLVAPLAAP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   183 erpdlADQDRPIPVWIRALGAALtpfnplaglriaGPFGLSLVQRLRPDFKrkyssmfeDDTVTEYIYHCNVQTPSGETA 262
Cdd:pfam12697  94 -----PGLLAALLALLARLGAAL------------AAPAWLAAESLARGFL--------DDLPADAEWAAALARLAALLA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31542303   263 FKNMTIPYGWakrpmlqrigkmhPDIPVSVIFGARSciDGNSGTSIQ-SLRPHSYVKTIAILGAGHYVYaDQPEEFNQ 339
Cdd:pfam12697 149 ALALLPLAAW-------------RDLPVPVLVLAEE--DRLVPELAQrLLAALAGARLVVLPGAGHLPL-DDPEEVAE 210
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 100-182 1.44e-06

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 49.81  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  100 TNRPVYAFDLLGFGRSSRPrfdSDAEEVENQFVESIEewRCAL---GLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILV 176
Cdd:PLN03087 231 STYRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIE--RSVLeryKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305


                 ....*.
gi 31542303  177 EPWGFP 182
Cdd:PLN03087 306 APPYYP 311
PLN02578 PLN02578
hydrolase
 91-180 2.67e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 48.68  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   91 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEwrcaLGLDKMILLGHNLGGFLAAAYSLKYPSRV 170
Cdd:PLN02578 102 WRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE----VVKEPAVLVGNSLGGFTALSTAVGYPELV 177

                         90
                 ....*....|
gi 31542303  171 NHLILVEPWG 180
Cdd:PLN02578 178 AGVALLNSAG 187
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 103-197 2.33e-05

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: 45.70  E-value: 2.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 103 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCALgLDKM---ILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 178
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDAL-LDRVgpcIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221

                        90       100
                ....*....|....*....|..
gi 31542303 179 WGFPERPDLADqDRPIP---VW 197
Cdd:cd12808 222 SGAPDPAEAAP-LADVPhllVW 242
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 106-194 1.04e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 43.44  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303  106 AFDLLGFGRSSRP----RFDSDAeevenQFVESieeWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGF 181
Cdd:PRK03592  58 APDLIGMGASDKPdidyTFADHA-----RYLDA---WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVR 129

                         90
                 ....*....|....
gi 31542303  182 PER-PDLADQDRPI 194
Cdd:PRK03592 130 PMTwDDFPPAVREL 143
YpfH COG0400
Predicted esterase [General function prediction only];
107-206 1.43e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303 107 FDLLGF-GRSSRPRFDSDAEEVeNQFVESIEEwRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILV------EPW 179
Cdd:COG0400  52 FDLSFLeGREDEEGLAAAAEAL-AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALsgylpgEEA 129

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 31542303 180 GFPERPDLA---------DQDRPIPV--------WIRALGAALT 206
Cdd:COG0400 130 LPAPEAALAgtpvflahgTQDPVIPVerareaaeALEAAGADVT 173
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 103-176 2.06e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.20  E-value: 2.06e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31542303 103 PVYAFDLLGFGRSSRPRfdsdAEEVENQfvesIEEWRCALGLDKMILLGHNLGGFLAAAY--SLKYPSRVNHLILV 176
Cdd:COG1075  34 PVYALNYPSTNGSIEDS----AEQLAAF----VDAVLAATGAEKVDLVGHSMGGLVARYYlkRLGGAAKVARVVTL 101
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 98-178 2.12e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 42.95  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   98 LCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHnlGGFLAAA--YSLKYPSRVNHLIL 175
Cdd:PLN03084 150 LSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQ--GYFSPPVvkYASAHPDKIKKLIL 227


                 ...
gi 31542303  176 VEP 178
Cdd:PLN03084 228 LNP 230
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
91-176 7.03e-03

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 37.69  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542303   91 WALNFG-------DLCTNRPVYAFDLLGFGRSS---RPRFDSDAEEVENQfvesieewrcalGLDKMILLGHNLGGFLAA 160
Cdd:PRK10349  22 WGLNAEvwrcideELSSHFTLHLVDLPGFGRSRgfgALSLADMAEAVLQQ------------APDKAIWLGWSLGGLVAS 89

                         90
                 ....*....|....*.
gi 31542303  161 AYSLKYPSRVNHLILV 176
Cdd:PRK10349  90 QIALTHPERVQALVTV 105
 
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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