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Conserved domains on  [gi|1958796739|ref|XP_038937600|]
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1-acylglycerol-3-phosphate O-acyltransferase ABHD5 isoform X2 [Rattus norvegicus]

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
 28-279 2.94e-43

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: 151.99  E-value: 2.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  28 NFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSH 106
Cdd:PLN02894  124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 107 LILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 175
Cdd:PLN02894  204 LILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 176 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIPVSVIFGARSCIDgNSGTSIQSLRPKSYVKTIA 255
Cdd:PLN02894  282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIR 358

                         250       260
                  ....*....|....*....|....
gi 1958796739 256 ILGAGHYVYADQPEEFNQKVKEIC 279
Cdd:PLN02894  359 VPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 28-279 2.94e-43

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 151.99  E-value: 2.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  28 NFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSH 106
Cdd:PLN02894  124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 107 LILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 175
Cdd:PLN02894  204 LILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 176 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIPVSVIFGARSCIDgNSGTSIQSLRPKSYVKTIA 255
Cdd:PLN02894  282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIR 358

                         250       260
                  ....*....|....*....|....
gi 1958796739 256 ILGAGHYVYADQPEEFNQKVKEIC 279
Cdd:PLN02894  359 VPQGGHFVFLDNPSGFHSAVLYAC 382
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 25-268 3.08e-19

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: 84.48  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  25 WALNFEDLSTDR-PVYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSR 103
Cdd:pfam00561  16 WRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 104 VSHLILVEPWG-FPERPDLADQERPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtv 179
Cdd:pfam00561  94 VKALVLLGALDpPHELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD----- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 180 teyiyhcnVQTPSGETAFKNMTIPYgWAKRPMLQRIGGLhpDIPVSVIFGARSCIDGNSGT-SIQSLRPKSYVKTIAilG 258
Cdd:pfam00561 169 --------YALAKSLVTGALLFIET-WSTELRAKFLGRL--DEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--D 235

                         250
                  ....*....|
gi 1958796739 259 AGHYVYADQP 268
Cdd:pfam00561 236 AGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 25-277 2.96e-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: 81.20  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  25 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRV 104
Cdd:COG0596    39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 105 SHLILVepwgfperpdladqerpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 184
Cdd:COG0596   115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 185 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgglhpDIPVSVIFGARS-CIDGNSGTSIQSLRPKSYVKTIAilGAGHYV 263
Cdd:COG0596   130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202

                         250
                  ....*....|....
gi 1958796739 264 YADQPEEFNQKVKE 277
Cdd:COG0596   203 PLEQPEAFAAALRD 216
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 37-131 5.26e-06

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: 46.85  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  37 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCAL--RLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPW 113
Cdd:cd12808   154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDALldRVGPCIVVAHSQGGGFAFEAARARPDLVRAVVALEPS 222

                          90       100
                  ....*....|....*....|.
gi 1958796739 114 GFPERPDLADqERPIP---VW 131
Cdd:cd12808   223 GAPDPAEAAP-LADVPhllVW 242
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 28-279 2.94e-43

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 151.99  E-value: 2.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  28 NFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSH 106
Cdd:PLN02894  124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 107 LILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 175
Cdd:PLN02894  204 LILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 176 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIPVSVIFGARSCIDgNSGTSIQSLRPKSYVKTIA 255
Cdd:PLN02894  282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIR 358

                         250       260
                  ....*....|....*....|....
gi 1958796739 256 ILGAGHYVYADQPEEFNQKVKEIC 279
Cdd:PLN02894  359 VPQGGHFVFLDNPSGFHSAVLYAC 382
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 25-268 3.08e-19

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: 84.48  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  25 WALNFEDLSTDR-PVYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSR 103
Cdd:pfam00561  16 WRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 104 VSHLILVEPWG-FPERPDLADQERPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtv 179
Cdd:pfam00561  94 VKALVLLGALDpPHELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD----- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 180 teyiyhcnVQTPSGETAFKNMTIPYgWAKRPMLQRIGGLhpDIPVSVIFGARSCIDGNSGT-SIQSLRPKSYVKTIAilG 258
Cdd:pfam00561 169 --------YALAKSLVTGALLFIET-WSTELRAKFLGRL--DEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--D 235

                         250
                  ....*....|
gi 1958796739 259 AGHYVYADQP 268
Cdd:pfam00561 236 AGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 25-277 2.96e-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: 81.20  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  25 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRV 104
Cdd:COG0596    39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 105 SHLILVepwgfperpdladqerpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 184
Cdd:COG0596   115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 185 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgglhpDIPVSVIFGARS-CIDGNSGTSIQSLRPKSYVKTIAilGAGHYV 263
Cdd:COG0596   130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202

                         250
                  ....*....|....
gi 1958796739 264 YADQPEEFNQKVKE 277
Cdd:COG0596   203 PLEQPEAFAAALRD 216
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
38-138 1.37e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.41  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  38 VYAFDLLGFGRSSRPRFDSDAEEvenQFVESIEEWRCALRLD---KMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWg 114
Cdd:COG2267    58 VLAFDLRGHGRSDGPRGHVDSFD---DYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA- 133

                          90       100
                  ....*....|....*....|....*
gi 1958796739 115 fperpDLADQERPIPV-WIRALGAA 138
Cdd:COG2267   134 -----YRADPLLGPSArWLRALRLA 153
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 38-170 2.65e-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: 64.93  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  38 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESI-EEWRCAlrldKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEP 112
Cdd:pfam12146  34 VYAYDHRGHGRSDGKRghVPSFDDYVDdlDTFVDKIrEEHPGL----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958796739 113 WgfperpdLADQERPIPVWIRALGAALTPFNPlaGLRIAGPFGLSLVQRlRPDFKRKY 170
Cdd:pfam12146 110 A-------LKIKPYLAPPILKLLAKLLGKLFP--RLRVPNNLLPDSLSR-DPEVVAAY 157
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-115 8.81e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.72  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  10 TPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEvenqFVESIEEWRCALRLDKMILLGHNLG 89
Cdd:PRK14875  132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDE----LAAAVLAFLDALGIERAHLVGHSMG 207

                          90       100
                  ....*....|....*....|....*.
gi 1958796739  90 GFLAAAYSLKYPSRVSHLILVEPWGF 115
Cdd:PRK14875  208 GAVALRLAARAPQRVASLTLIAPAGL 233
PLN02578 PLN02578
hydrolase
 25-114 2.94e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 50.99  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  25 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEwrcaLRLDKMILLGHNLGGFLAAAYSLKYPSRV 104
Cdd:PLN02578  102 WRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE----VVKEPAVLVGNSLGGFTALSTAVGYPELV 177

                          90
                  ....*....|
gi 1958796739 105 SHLILVEPWG 114
Cdd:PLN02578  178 AGVALLNSAG 187
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 28-116 8.86e-07

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 49.81  E-value: 8.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  28 NFEDLS-TDRPVYAFDLLGFGRSSRPrfdSDAEEVENQFVESIEewRCAL---RLDKMILLGHNLGGFLAAAYSLKYPSR 103
Cdd:PLN03087  224 NFSDAAkSTYRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIE--RSVLeryKVKSFHIVAHSLGCILALALAVKHPGA 298

                          90
                  ....*....|...
gi 1958796739 104 VSHLILVEPWGFP 116
Cdd:PLN03087  299 VKSLTLLAPPYYP 311
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 32-273 4.01e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 46.70  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  32 LSTDRPVYAFDLLGFGRSSRPRFD-SDAEEVENqFVESIEEWRCAlrldkmILLGHNLGGFLAAAYslkYPSRVSHLILV 110
Cdd:pfam12697  18 LAAGVAVLAPDLPGHGSSSPPPLDlADLADLAA-LLDELGAARPV------VLVGHSLGGAVALAA---AAAALVVGVLV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 111 EPWGFPerpdlADQERPIPVWIRALGAALtpfnplaglriaGPFGLSLVQRLRPDFKrkyssmfeDDTVTEYIYHCNVQT 190
Cdd:pfam12697  88 APLAAP-----PGLLAALLALLARLGAAL------------AAPAWLAAESLARGFL--------DDLPADAEWAAALAR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739 191 PSGETAFKNMTIPYGWakrpmlqrigglhPDIPVSVIFGARSciDGNSGTSIQ-SLRPKSYVKTIAILGAGHYVYaDQPE 269
Cdd:pfam12697 143 LAALLAALALLPLAAW-------------RDLPVPVLVLAEE--DRLVPELAQrLLAALAGARLVVLPGAGHLPL-DDPE 206


                  ....
gi 1958796739 270 EFNQ 273
Cdd:pfam12697 207 EVAE 210
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 37-131 5.26e-06

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: 46.85  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  37 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCAL--RLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPW 113
Cdd:cd12808   154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDALldRVGPCIVVAHSQGGGFAFEAARARPDLVRAVVALEPS 222

                          90       100
                  ....*....|....*....|.
gi 1958796739 114 GFPERPDLADqERPIP---VW 131
Cdd:cd12808   223 GAPDPAEAAP-LADVPhllVW 242
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 32-112 7.19e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 43.72  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  32 LSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHnlGGFLAAA--YSLKYPSRVSHLIL 109
Cdd:PLN03084  150 LSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQ--GYFSPPVvkYASAHPDKIKKLIL 227


                  ...
gi 1958796739 110 VEP 112
Cdd:PLN03084  228 LNP 230
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
25-110 3.13e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 41.16  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  25 WALNF-------EDLSTDRPVYAFDLLGFGRSS---RPRFDSDAEEVENQfvesieewrcalRLDKMILLGHNLGGFLAA 94
Cdd:PRK10349   22 WGLNAevwrcidEELSSHFTLHLVDLPGFGRSRgfgALSLADMAEAVLQQ------------APDKAIWLGWSLGGLVAS 89

                          90
                  ....*....|....*.
gi 1958796739  95 AYSLKYPSRVSHLILV 110
Cdd:PRK10349   90 QIALTHPERVQALVTV 105
YpfH COG0400
Predicted esterase [General function prediction only];
41-132 1.24e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.12  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  41 FDLLGF-GRSSRPRFDSDAEEVeNQFVESIEEwRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPwGFPERP 119
Cdd:COG0400    52 FDLSFLeGREDEEGLAAAAEAL-AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSG-YLPGEE 128

                          90
                  ....*....|....*.
gi 1958796739 120 DLADQE---RPIPVWI 132
Cdd:COG0400   129 ALPAPEaalAGTPVFL 144
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 40-128 2.36e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 38.82  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796739  40 AFDLLGFGRSSRP----RFDSDAeevenQFVESieeWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGF 115
Cdd:PRK03592   58 APDLIGMGASDKPdidyTFADHA-----RYLDA---WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVR 129

                          90
                  ....*....|....
gi 1958796739 116 PER-PDLADQERPI 128
Cdd:PRK03592  130 PMTwDDFPPAVREL 143
 
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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