NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|8923001|ref|NP_060864|]
View 

palmitoyl-protein thioesterase ABHD10, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 11445445)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
72-295 3.13e-19

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


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 84.68  E-value: 3.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   72 KGKSPGIIFIPG-----YLSYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLgkwrKDVLSIIDDLADGPQ 146
Cdd:COG1506  20 GKKYPVVVYVHGgpgsrDDSFLPLAQALA------SRGYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAARPY 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  147 I------LVGSSLGGWLMLHAAIARPEKVVALIGVATAAD--TLVTKFNQLPvelkkEVEMKGVWSMPSKYSEegvynvq 218
Cdd:COG1506  90 VdpdrigIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDlrSYYGTTREYT-----ERLMGGPWEDPEAYAA------- 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923001  219 YSFIKEAEHhcllhspipVNCPIRLLHGMKDDIVPWHTSMQVADRVLSTDVDVILR--KHSDHRMREKADIQLLVYTID 295
Cdd:COG1506 158 RSPLAYADK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLvyPGEGHGFSGAGAPDYLERILD 227
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
72-295 3.13e-19

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 84.68  E-value: 3.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   72 KGKSPGIIFIPG-----YLSYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLgkwrKDVLSIIDDLADGPQ 146
Cdd:COG1506  20 GKKYPVVVYVHGgpgsrDDSFLPLAQALA------SRGYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAARPY 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  147 I------LVGSSLGGWLMLHAAIARPEKVVALIGVATAAD--TLVTKFNQLPvelkkEVEMKGVWSMPSKYSEegvynvq 218
Cdd:COG1506  90 VdpdrigIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDlrSYYGTTREYT-----ERLMGGPWEDPEAYAA------- 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923001  219 YSFIKEAEHhcllhspipVNCPIRLLHGMKDDIVPWHTSMQVADRVLSTDVDVILR--KHSDHRMREKADIQLLVYTID 295
Cdd:COG1506 158 RSPLAYADK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLvyPGEGHGFSGAGAPDYLERILD 227
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 78-177 4.99e-07

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: 49.81  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001     78 IIFIPGYL----SYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLGKW--RKDVLSIIDDLADGPQILVGS 151
Cdd:pfam00561   3 VLLLHGLPgssdLWRKLAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76

                          90       100
                  ....*....|....*....|....*.
gi 8923001    152 SLGGWLMLHAAIARPEKVVALIGVAT 177
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA 102
PLN02578 PLN02578
hydrolase
 72-178 5.00e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 44.45  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001    72 KGKSPGIIFIPGYlsymnGTKAL----AIEEFCKSlgHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADGPQI 147
Cdd:PLN02578  83 QGEGLPIVLIHGF-----GASAFhwryNIPELAKK--YKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAV 155

                         90       100       110
                 ....*....|....*....|....*....|.
gi 8923001   148 LVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:PLN02578 156 LVGNSLGGFTALSTAVGYPELVAGVALLNSA 186
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 144-175 5.54e-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: 44.16  E-value: 5.54e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 8923001  144 GPQILVGSSLGGWLMLHAAIARPEKVVALIGV 175
Cdd:cd12808 188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
72-295 3.13e-19

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 84.68  E-value: 3.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   72 KGKSPGIIFIPG-----YLSYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLgkwrKDVLSIIDDLADGPQ 146
Cdd:COG1506  20 GKKYPVVVYVHGgpgsrDDSFLPLAQALA------SRGYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAARPY 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  147 I------LVGSSLGGWLMLHAAIARPEKVVALIGVATAAD--TLVTKFNQLPvelkkEVEMKGVWSMPSKYSEegvynvq 218
Cdd:COG1506  90 VdpdrigIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDlrSYYGTTREYT-----ERLMGGPWEDPEAYAA------- 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923001  219 YSFIKEAEHhcllhspipVNCPIRLLHGMKDDIVPWHTSMQVADRVLSTDVDVILR--KHSDHRMREKADIQLLVYTID 295
Cdd:COG1506 158 RSPLAYADK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLvyPGEGHGFSGAGAPDYLERILD 227
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
71-302 1.30e-18

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 83.07  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   71 LKGKSPGIIFIPGYLSYMNGTKALAieEFCKSLGHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADG--PQIL 148
Cdd:COG1647  11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  149 VGSSLGGWLMLHAAIARPEkVVALIGVATAADTLVTKFNQLPV--ELKKEVEMKGvwsmpSKYSEEGVYNVQYS------ 220
Cdd:COG1647  89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLlkYLARSLRGIG-----SDIEDPEVAEYAYDrtplra 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  221 ------FIKEAEHHclLHSpipVNCPIRLLHGMKDDIVPWHTSMQVADRVLSTDVDVILRKHSDHRMREKADIQLLVYTI 294
Cdd:COG1647 163 laelqrLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDKDREEVAEEI 237


                ....*...
gi 8923001  295 DDLIDKLS 302
Cdd:COG1647 238 LDFLERLA 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 65-279 8.65e-17

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: 77.73  E-value: 8.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   65 NLAYKKLKGKSPGIIFIPGYLSYMNGTKALaIEEFCKslGHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADG 144
Cdd:COG0596  13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPL-IPALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  145 PQILVGSSLGGWLMLHAAIARPEKVVALIGVATAADTLVTKFNQlpvelkkevemkgvwsmpSKYSEEGVYNVQYSFIKE 224
Cdd:COG0596  90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR------------------PGLAPEALAALLRALART 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8923001  225 AEHHCLLHspipVNCPIRLLHGMKDDIVPWHTSMQVADRVlsTDVDVILRKHSDH 279
Cdd:COG0596 152 DLRERLAR----ITVPTLVIWGEKDPIVPPALARRLAELL--PNAELVVLPGAGH 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-279 6.50e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.34  E-value: 6.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   78 IIFIPGYLSYMNGTKALAiEEFCKSlGHACIRFDYSGVGSSDG-NSEESTLGKWRKDVLSIIDDLA---DGPQILVGSSL 153
Cdd:COG2267  31 VVLVHGLGEHSGRYAELA-EALAAA-GYAVLAFDLRGHGRSDGpRGHVDSFDDYVDDLRAALDALRarpGLPVVLLGHSM 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  154 GGWLMLHAAIARPEKVVALIGVATAadtlvtkfnqlpvelkkevemkgvwsmpskYSEEGVYNVQYSFIKEAEHHCLLHS 233
Cdd:COG2267 109 GGLIALLYAARYPDRVAGLVLLAPA------------------------------YRADPLLGPSARWLRALRLAEALAR 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 8923001  234 pipVNCPIRLLHGMKDDIVPWHTSMQVADRvLSTDVDVILRKHSDH 279
Cdd:COG2267 159 ---IDVPVLVLHGGADRVVPPEAARRLAAR-LSPDVELVLLPGARH 200
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 69-255 1.92e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 54.15  E-value: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001   69 KKLKGKSPGIIFIPGYlsymNGTK---ALAIEEFCKsLGHACIRFDYSGVGSSDGN-SEESTLgkWRKDVLSIIDDLA-- 142
Cdd:COG1073  31 AGASKKYPAVVVAHGN----GGVKeqrALYAQRLAE-LGFNVLAFDYRGYGESEGEpREEGSP--ERRDARAAVDYLRtl 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  143 ---DGPQILV-GSSLGGWLMLHAAIARPEkVVALIGVATaadtlvtkFNQLPVELK-KEVEMKGVWSMPSKY----SEEG 213
Cdd:COG1073 104 pgvDPERIGLlGISLGGGYALNAAATDPR-VKAVILDSP--------FTSLEDLAAqRAKEARGAYLPGVPYlpnvRLAS 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 8923001  214 VYNVQYSFIKEAEHhcllhspipVNCPIRLLHGMKDDIVPWH 255
Cdd:COG1073 175 LLNDEFDPLAKIEK---------ISRPLLFIHGEKDEAVPFY 207
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
100-279 8.94e-08

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 51.32  E-value: 8.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  100 CKSLGHACIRFDYSGVGSSDGNSEESTlGKwRKDVLSIIDDLAD---GPQILVGSSLGGWLMLHAAIARPEkVVALIGVA 176
Cdd:COG2945  51 LVAAGFAVLRFNFRGVGRSEGEFDEGR-GE-LDDAAAALDWLRAqnpLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001  177 TAAdtlvtkfnqlpvelkkevemkgvwsmpSKYseegvynvQYSFIKeaehhcllhspiPVNCPIRLLHGMKDDIVPWHT 256
Cdd:COG2945 128 PPV---------------------------NRY--------DFSFLA------------PCPAPTLVIHGEQDEVVPPAE 160

                       170       180
                ....*....|....*....|...
gi 8923001  257 SMQVADRvLSTDVDVILRKHSDH 279
Cdd:COG2945 161 VLDWARP-LSPPLPVVVVPGADH 182
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 78-177 4.99e-07

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: 49.81  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001     78 IIFIPGYL----SYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLGKW--RKDVLSIIDDLADGPQILVGS 151
Cdd:pfam00561   3 VLLLHGLPgssdLWRKLAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76

                          90       100
                  ....*....|....*....|....*.
gi 8923001    152 SLGGWLMLHAAIARPEKVVALIGVAT 177
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA 102
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 78-286 2.39e-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: 47.47  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001     78 IIFIPGYLSYMNGTKALAIEefckslGHACIRFDYSGVGSSDGNSEESTLgkwRKDVLSIIDDLADGPQ-ILVGSSLGGW 156
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA------GVAVLAPDLPGHGSSSPPPLDLAD---LADLAALLDELGAARPvVLVGHSLGGA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001    157 LMLHAAIARPEKVVAL------IGVATAADTLVTKFNQLPVELKKEVEMKGVWSMPSKYSEEGVYNVQYSFIKEAEHHCL 230
Cdd:pfam12697  72 VALAAAAAALVVGVLVaplaapPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 8923001    231 LHSPIPVNCPIR--LLHGMKDDIVPWHTSMQVADRvlsTDVDVILRKHSDHRMREKAD 286
Cdd:pfam12697 152 LLPLAAWRDLPVpvLVLAEEDRLVPELAQRLLAAL---AGARLVVLPGAGHLPLDDPE 206
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-279 1.42e-05

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: 45.28  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001     78 IIFIPGYLSYMNgtkalAIEEFCKSL---GHACIRFDYSGVGSSDGN-SEESTLGKWRKDVLSIIDDLADG----PQILV 149
Cdd:pfam12146   7 VVLVHGLGEHSG-----RYAHLADALaaqGFAVYAYDHRGHGRSDGKrGHVPSFDDYVDDLDTFVDKIREEhpglPLFLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001    150 GSSLGGWLMLHAAIARPEKVVALIGVATA---ADTLVTKFNQLPVEL------KKEVEMKGVWSMPSKYSEEgvynvqys 220
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPAlkiKPYLAPPILKLLAKLlgklfpRLRVPNNLLPDSLSRDPEV-------- 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923001    221 fIKEAEHHCLLHSPIPVN--------------------CPIRLLHGMKDDIVPWHTSMQVADRVLSTDVDVILRKHSDH 279
Cdd:pfam12146 154 -VAAYAADPLVHGGISARtlyelldagerllrraaaitVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
PLN02578 PLN02578
hydrolase
 72-178 5.00e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 44.45  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923001    72 KGKSPGIIFIPGYlsymnGTKAL----AIEEFCKSlgHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADGPQI 147
Cdd:PLN02578  83 QGEGLPIVLIHGF-----GASAFhwryNIPELAKK--YKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAV 155

                         90       100       110
                 ....*....|....*....|....*....|.
gi 8923001   148 LVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:PLN02578 156 LVGNSLGGFTALSTAVGYPELVAGVALLNSA 186
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 144-175 5.54e-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: 44.16  E-value: 5.54e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 8923001  144 GPQILVGSSLGGWLMLHAAIARPEKVVALIGV 175
Cdd:cd12808 188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 104-178 1.19e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.93  E-value: 1.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8923001   104 GHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADGPQILVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:PRK14875 157 GRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPA 231
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
127-178 3.58e-03

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


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 37.52  E-value: 3.58e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 8923001  127 LGKWRKDVLSIIDDlADGPQILVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:COG3545  38 LDDWLAALDAAVAA-ADGPVVLVAHSLGCLAVAHWAARLPRKVAGALLVAPP 88
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 135-175 6.04e-03

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: 214008  Cd Length: 280  Bit Score: 37.59  E-value: 6.04e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 8923001  135 LSIIddladGPQILVGSSLGGWLMLHAAIARPEKVVALIGV 175
Cdd:cd12809 167 LDII-----GPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH