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Conserved domains on  [gi|1851859573|ref|NP_001371152|]
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palmitoyl-protein thioesterase ABHD10, mitochondrial isoform 4 [Mus musculus]

Protein Classification

carboxylesterase( domain architecture ID 10787854)

carboxylesterase catalyzes the hydrolysis of carboxylic esters to yield the corresponding alcohol and a carboxylate, such as Geobacillus stearothermophilus Est30, a member of alpha/beta hydrolase family that hydrolyzes short chain aliphatic and aromatic esters

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
62-278 2.86e-22

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


:

Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 93.08  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647    11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETETQKEIEMKgewtlpsrynKEGY 219
Cdd:COG1647    89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALK--IDDPSAPLLPLLKYLARSLRGIGSDIEDPEVA----------EYAY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851859573 220 FRIP-------YSFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 278
Cdd:COG1647   156 DRTPlralaelQRLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
 
Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
62-278 2.86e-22

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 93.08  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647    11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETETQKEIEMKgewtlpsrynKEGY 219
Cdd:COG1647    89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALK--IDDPSAPLLPLLKYLARSLRGIGSDIEDPEVA----------EYAY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851859573 220 FRIP-------YSFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 278
Cdd:COG1647   156 DRTPlralaelQRLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
PLN02578 PLN02578
hydrolase
 102-164 9.81e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.45  E-value: 9.81e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 102 DYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALI 164
Cdd:PLN02578  119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVA 181
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 88-282 6.32e-06

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: 46.44  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  88 EEFCKSL---GHAFIRFDYSGIGSSDGNLAECT-VGKWRKDVLSILDDVAEG----PQILVGSSLGGWLMLHAAIARPEK 159
Cdd:pfam12146  21 AHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 160 VIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETetqKEIEMKGEWTLPSRYNKEgyfripysfIKEAEHHCLLHSP 239
Cdd:pfam12146 101 VDGLILSAPALK--IKPYLAPPILKLLAKLLGKLFPR---LRVPNNLLPDSLSRDPEV---------VAAYAADPLVHGG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 240 IPV--------------------TCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQG 282
Cdd:pfam12146 167 ISArtlyelldagerllrraaaiTVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGL 229
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 135-166 1.20e-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: 43.00  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1851859573 135 GPQILVGSSLGGWLMLHAAIARPEKVIALIGI 166
Cdd:cd12808   188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
 69-164 3.73e-03

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 38.26  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  69 IIFIPGYLSNMNGIKAVAV---EEFCKsLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSI---LDDVAEGPQILVGS 142
Cdd:TIGR03101  28 VIYLPPFAEEMNKSRRMVAlqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106

                          90       100
                  ....*....|....*....|..
gi 1851859573 143 SLGGWLMLHAAIARPEKVIALI 164
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
 
Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
62-278 2.86e-22

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 93.08  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647    11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETETQKEIEMKgewtlpsrynKEGY 219
Cdd:COG1647    89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALK--IDDPSAPLLPLLKYLARSLRGIGSDIEDPEVA----------EYAY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851859573 220 FRIP-------YSFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 278
Cdd:COG1647   156 DRTPlralaelQRLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 56-278 4.68e-16

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: 75.42  E-value: 4.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  56 NLAYKRLKGKTPGIIFIPGYLSNMNGIKAVAvEEFCKslGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG 135
Cdd:COG0596    13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLI-PALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 136 PQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHALPVEVLAYSfnpstwetetqKEIEMKGEWTLPSRYN 215
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALA-----------ALLRALARTDLRERLA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 216 KegyfripysfikeaehhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIvsPDVDVIL 278
Cdd:COG0596   159 R-------------------------ITVPTLVIWGEKDPIVPPALARRLAELL--PNAELVV 194
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
63-276 1.43e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 74.28  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  63 KGKTPGIIFIPGYLSNMNGIKAVAVEEFCkSLGHAFIRFDYSGIGSSDGNLAectvGKWRKDVLSILDDVAEGPQI---- 138
Cdd:COG1506    20 GKKYPVVVYVHGGPGSRDDSFLPLAQALA-SRGYAVLAPDYRGYGESAGDWG----GDEVDDVLAAIDYLAARPYVdpdr 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 139 --LVGSSLGGWLMLHAAIARPEKVIALIGIATAADgLVTQYHalpvevlaysfnpstwETETQKEIEMKGEWTLPSRYNK 216
Cdd:COG1506    95 igIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD-LRSYYG----------------TTREYTERLMGGPWEDPEAYAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 217 egyfripYSFIKEAEHhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDV 276
Cdd:COG1506   158 -------RSPLAYADK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPV 201
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
69-278 3.20e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 67.72  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  69 IIFIPGYLSNMNGIKAVAvEEFCKSlGHAFIRFDYSGIGSSDGNLAEC-TVGKWRKDVLSILDDVAE---GPQILVGSSL 144
Cdd:COG2267    31 VVLVHGLGEHSGRYAELA-EALAAA-GYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDALRArpgLPVVLLGHSM 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 145 GGWLMLHAAIARPEKVIALIGIATaadglvtqyhalpvevlaysfnpstwetetqkeiemkgewtlpsRYNKEGYFRIPY 224
Cdd:COG2267   109 GGLIALLYAARYPDRVAGLVLLAP--------------------------------------------AYRADPLLGPSA 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1851859573 225 SFIKEAEHHCLLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIvSPDVDVIL 278
Cdd:COG2267   145 RWLRALRLAEALAR---IDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVL 194
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 63-272 2.15e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 51.07  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  63 KGKTPGIIFIPGYLSNMNGIkAVAVEEFCKsLGHAFIRFDYSGIGSSDGNLAEctVGK-WRKDV------LSILDDVAEG 135
Cdd:COG1073    34 SKKYPAVVVAHGNGGVKEQR-ALYAQRLAE-LGFNVLAFDYRGYGESEGEPRE--EGSpERRDAraavdyLRTLPGVDPE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 136 PQILVGSSLGGWLMLHAAIARPEkVIALIGIATAAdglvtqyhalpvevlaysfnpSTWETETQKEIEMKGEWTLPSRYN 215
Cdd:COG1073   110 RIGLLGISLGGGYALNAAATDPR-VKAVILDSPFT---------------------SLEDLAAQRAKEARGAYLPGVPYL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1851859573 216 K----EGYFRIPYSFIKEAEHhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSP 272
Cdd:COG1073   168 PnvrlASLLNDEFDPLAKIEK---------ISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP 219
PLN02578 PLN02578
hydrolase
 102-164 9.81e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.45  E-value: 9.81e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 102 DYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALI 164
Cdd:PLN02578  119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVA 181
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 88-282 6.32e-06

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: 46.44  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  88 EEFCKSL---GHAFIRFDYSGIGSSDGNLAECT-VGKWRKDVLSILDDVAEG----PQILVGSSLGGWLMLHAAIARPEK 159
Cdd:pfam12146  21 AHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 160 VIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETetqKEIEMKGEWTLPSRYNKEgyfripysfIKEAEHHCLLHSP 239
Cdd:pfam12146 101 VDGLILSAPALK--IKPYLAPPILKLLAKLLGKLFPR---LRVPNNLLPDSLSRDPEV---------VAAYAADPLVHGG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 240 IPV--------------------TCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQG 282
Cdd:pfam12146 167 ISArtlyelldagerllrraaaiTVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGL 229
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
141-279 8.91e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 42.99  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 141 GSSLGGWLMLHAAIARPEKVIALIGIATAADglVTQYHALPVEVLA--YSFNPSTWetetqkeiemkgewtlpsrYNKEG 218
Cdd:pfam00326  70 GGSYGGYLTGAALNQRPDLFKAAVAHVPVVD--WLAYMSDTSLPFTerYMEWGNPW-------------------DNEEG 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1851859573 219 YFRI-PYSFIKEaehhcllhspIPVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILR 279
Cdd:pfam00326 129 YDYLsPYSPADN----------VKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLL 180
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
91-277 1.01e-04

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 42.46  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  91 CKSLGHAFIRFDYSGIGSSDGNLAEcTVGKwRKDVLSILDDVAE---GPQILVGSSLGGWLMLHAAIARPEkVIALIGIA 167
Cdd:COG2945    51 LVAAGFAVLRFNFRGVGRSEGEFDE-GRGE-LDDAAAALDWLRAqnpLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 168 TAAdglvtqyhalpvevlaysfnpstwetetqkeiemkgewtlpSRYnkegyfriPYSFIKeaehhcllhspiPVTCPVR 247
Cdd:COG2945   128 PPV-----------------------------------------NRY--------DFSFLA------------PCPAPTL 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 1851859573 248 LLHGMKDEIVPWQRSLQVADRiVSPDVDVI 277
Cdd:COG2945   147 VIHGEQDEVVPPAEVLDWARP-LSPPLPVV 175
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 135-166 1.20e-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: 43.00  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1851859573 135 GPQILVGSSLGGWLMLHAAIARPEKVIALIGI 166
Cdd:cd12808   188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-194 2.02e-04

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: 42.11  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  69 IIFIPGYLSNMNG----IKAVAveefckSLGHAFIRFDYSGIGSSDGNLAECTVGKW--RKDVLSILDDVAEGPQILVGS 142
Cdd:pfam00561   3 VLLLHGLPGSSDLwrklAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1851859573 143 SLGGWLMLHAAIARPEKVIALIGIATAADGlvtqyHALPVEVLAYSFNPSTW 194
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDPP-----HELDEADRFILALFPGF 123
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 69-173 7.20e-04

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 40.15  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  69 IIFIPGYlsnmnGIKAVAVEEFCKSlGHAFIRFDYSGIGSSDGNLAECTVgkwRKDVLSILDDVAEGPQ-ILVGSSLGGW 147
Cdd:pfam12697   1 VVLVHGA-----GLSAAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD---LADLAALLDELGAARPvVLVGHSLGGA 71

                          90       100
                  ....*....|....*....|....*.
gi 1851859573 148 LMLHAAIARPEKVIALIGIATAADGL 173
Cdd:pfam12697  72 VALAAAAAALVVGVLVAPLAAPPGLL 97
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
93-161 9.69e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 40.25  E-value: 9.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851859573  93 SLGHAFIRFDYSGIGSS-DGNLAECTVGK--W-RKDVLSILDDVAE----GPQILVGSSLGGWLM-LHAAIARPEKVI 161
Cdd:COG4757    57 ERGFAVLTYDYRGIGLSrPGSLRGFDAGYrdWgELDLPAVLDALRArfpgLPLLLVGHSLGGQLLgLAPNAERVDRLV 134
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 95-172 1.00e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.31  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851859573  95 GHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADG 172
Cdd:PRK14875  157 GRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLG 234
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
 69-164 3.73e-03

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 38.26  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573  69 IIFIPGYLSNMNGIKAVAV---EEFCKsLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSI---LDDVAEGPQILVGS 142
Cdd:TIGR03101  28 VIYLPPFAEEMNKSRRMVAlqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106

                          90       100
                  ....*....|....*....|..
gi 1851859573 143 SLGGWLMLHAAIARPEKVIALI 164
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
 
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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