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Conserved domains on  [gi|440918693|ref|NP_001258999|]
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palmitoyl-protein thioesterase ABHD10, mitochondrial isoform 2 precursor [Mus musculus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10787854)

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

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];
62-264 3.57e-22

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


:

Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 92.70  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647   11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADGLVTQYHALPVETQ--KEIEMKGEWTLPSRYNKEGYFRIP-------Y 210
Cdd:COG1647   89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYlaRSLRGIGSDIEDPEVAEYAYDRTPlralaelQ 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 440918693 211 SFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 264
Cdd:COG1647  168 RLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
 
Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
62-264 3.57e-22

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 92.70  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647   11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADGLVTQYHALPVETQ--KEIEMKGEWTLPSRYNKEGYFRIP-------Y 210
Cdd:COG1647   89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYlaRSLRGIGSDIEDPEVAEYAYDRTPlralaelQ 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 440918693 211 SFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 264
Cdd:COG1647  168 RLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
PLN02578 PLN02578
hydrolase
102-164 7.75e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.84  E-value: 7.75e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440918693 102 DYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALI 164
Cdd:PLN02578 119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVA 181
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
88-268 8.08e-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: 46.05  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693   88 EEFCKSL---GHAFIRFDYSGIGSSDGNLAECT-VGKWRKDVLSILDDVAEG----PQILVGSSLGGWLMLHAAIARPEK 159
Cdd:pfam12146  21 AHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  160 VIALIGIATAADglVTQYHALPVeTQKEIEMKG----EWTLPSRYNKEGYFRIPySFIKEAEHHCLLHSPIPV------- 228
Cdd:pfam12146 101 VDGLILSAPALK--IKPYLAPPI-LKLLAKLLGklfpRLRVPNNLLPDSLSRDP-EVVAAYAADPLVHGGISArtlyell 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 440918693  229 -------------TCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQG 268
Cdd:pfam12146 177 dagerllrraaaiTVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGL 229
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
135-166 1.10e-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: 1.10e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 440918693 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 3.36e-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: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693   69 IIFIPGYLSNMNGIKAVAV---EEFCKsLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSI---LDDVAEGPQILVGS 142
Cdd:TIGR03101  28 VIYLPPFAEEMNKSRRMVAlqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106
                          90       100
                  ....*....|....*....|..
gi 440918693  143 SLGGWLMLHAAIARPEKVIALI 164
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
 
Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
62-264 3.57e-22

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 92.70  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647   11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADGLVTQYHALPVETQ--KEIEMKGEWTLPSRYNKEGYFRIP-------Y 210
Cdd:COG1647   89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYlaRSLRGIGSDIEDPEVAEYAYDRTPlralaelQ 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 440918693 211 SFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 264
Cdd:COG1647  168 RLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
63-262 3.45e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 78.52  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  63 KGKTPGIIFIPGYLSNMNGIKAVAVEEFCkSLGHAFIRFDYSGIGSSDGNLAectvGKWRKDVLSILDDVAEGPQI---- 138
Cdd:COG1506   20 GKKYPVVVYVHGGPGSRDDSFLPLAQALA-SRGYAVLAPDYRGYGESAGDWG----GDEVDDVLAAIDYLAARPYVdpdr 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 139 --LVGSSLGGWLMLHAAIARPEKVIALIGIATAADgLVTQYHALPVETqkEIEMKGEWTLPSRYNKegyfripYSFIKEA 216
Cdd:COG1506   95 igIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD-LRSYYGTTREYT--ERLMGGPWEDPEAYAA-------RSPLAYA 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 440918693 217 EHhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDV 262
Cdd:COG1506  165 DK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPV 201
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
56-264 5.04e-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: 78.12  E-value: 5.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  56 NLAYKRLKGKTPGIIFIPGYLSNMNGIKAVAvEEFCKslGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG 135
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLI-PALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 136 PQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHAlpvetqkeiemkgewtlpSRYNKEGYFRIPYSFIKE 215
Cdd:COG0596   90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR------------------PGLAPEALAALLRALART 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 440918693 216 AEHHCLLHspipVTCPVRLLHGMKDEIVPWQRSLQVADRIvsPDVDVIL 264
Cdd:COG0596  152 DLRERLAR----ITVPTLVIWGEKDPIVPPALARRLAELL--PNAELVV 194
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
69-264 5.24e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.34  E-value: 5.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  69 IIFIPGYLSNMNGIKAVAvEEFCKSlGHAFIRFDYSGIGSSDGNLAEC-TVGKWRKDVLSILDDVAE---GPQILVGSSL 144
Cdd:COG2267   31 VVLVHGLGEHSGRYAELA-EALAAA-GYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDALRArpgLPVVLLGHSM 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 145 GGWLMLHAAIARPEKVIALIGIATaadglvtqyhalpvetqkeiemkgewtlpsRYNKEGYFRIPYSFIKEAEHHCLLHS 224
Cdd:COG2267  109 GGLIALLYAARYPDRVAGLVLLAP------------------------------AYRADPLLGPSARWLRALRLAEALAR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 440918693 225 pipVTCPVRLLHGMKDEIVPWQRSLQVADRIvSPDVDVIL 264
Cdd:COG2267  159 ---IDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVL 194
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
94-258 3.93e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 52.99  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  94 LGHAFIRFDYSGIGSSDGNLAEctVGK-WRKDV------LSILDDVAEGPQILVGSSLGGWLMLHAAIARPEkVIALIGI 166
Cdd:COG1073   63 LGFNVLAFDYRGYGESEGEPRE--EGSpERRDAraavdyLRTLPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 167 ATAADglvtqyhALPVETQKEIEMKGEWTLPSRYNK----EGYFRIPYSFIKEAEHhcllhspipVTCPVRLLHGMKDEI 242
Cdd:COG1073  140 SPFTS-------LEDLAAQRAKEARGAYLPGVPYLPnvrlASLLNDEFDPLAKIEK---------ISRPLLFIHGEKDEA 203
                        170
                 ....*....|....*.
gi 440918693 243 VPWQRSLQVADRIVSP 258
Cdd:COG1073  204 VPFYMSEDLYEAAAEP 219
PLN02578 PLN02578
hydrolase
102-164 7.75e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.84  E-value: 7.75e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440918693 102 DYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALI 164
Cdd:PLN02578 119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVA 181
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
91-263 1.86e-06

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 47.46  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  91 CKSLGHAFIRFDYSGIGSSDGNLAEcTVGKwRKDVLSILDDVAE---GPQILVGSSLGGWLMLHAAIARPEkVIALIGIA 167
Cdd:COG2945   51 LVAAGFAVLRFNFRGVGRSEGEFDE-GRGE-LDDAAAALDWLRAqnpLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693 168 TAAdglvtqyhalpvetqkeiemkgewtlpSRYnkegyfriPYSFIKeaehhcllhspiPVTCPVRLLHGMKDEIVPWQR 247
Cdd:COG2945  128 PPV---------------------------NRY--------DFSFLA------------PCPAPTLVIHGEQDEVVPPAE 160
                        170
                 ....*....|....*.
gi 440918693 248 SLQVADRiVSPDVDVI 263
Cdd:COG2945  161 VLDWARP-LSPPLPVV 175
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
88-268 8.08e-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: 46.05  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693   88 EEFCKSL---GHAFIRFDYSGIGSSDGNLAECT-VGKWRKDVLSILDDVAEG----PQILVGSSLGGWLMLHAAIARPEK 159
Cdd:pfam12146  21 AHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  160 VIALIGIATAADglVTQYHALPVeTQKEIEMKG----EWTLPSRYNKEGYFRIPySFIKEAEHHCLLHSPIPV------- 228
Cdd:pfam12146 101 VDGLILSAPALK--IKPYLAPPI-LKLLAKLLGklfpRLRVPNNLLPDSLSRDP-EVVAAYAADPLVHGGISArtlyell 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 440918693  229 -------------TCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQG 268
Cdd:pfam12146 177 dagerllrraaaiTVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGL 229
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
135-166 1.10e-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: 1.10e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 440918693 135 GPQILVGSSLGGWLMLHAAIARPEKVIALIGI 166
Cdd:cd12808  188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
141-265 1.48e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 42.22  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693  141 GSSLGGWLMLHAAIARPEKVIALIGIATAADglVTQYHA---LPVETQKEiemkgEWTLPsRYNKEGYFRI-PYSFIKEa 216
Cdd:pfam00326  70 GGSYGGYLTGAALNQRPDLFKAAVAHVPVVD--WLAYMSdtsLPFTERYM-----EWGNP-WDNEEGYDYLsPYSPADN- 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 440918693  217 ehhcllhspIPVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILR 265
Cdd:pfam00326 141 ---------VKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLL 180
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
69-175 3.35e-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: 41.34  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693   69 IIFIPGYLSNMNG----IKAVAveefckSLGHAFIRFDYSGIGSSDGNLAECTVGKW--RKDVLSILDDVAEGPQILVGS 142
Cdd:pfam00561   3 VLLLHGLPGSSDLwrklAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 440918693  143 SLGGWLMLHAAIARPEKVIALIGIATAADGLVT 175
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDPPHEL 109
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
69-173 8.82e-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: 39.76  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693   69 IIFIPGYlsnmnGIKAVAVEEFCKSlGHAFIRFDYSGIGSSDGNLAECTVgkwRKDVLSILDDVAEGPQ-ILVGSSLGGW 147
Cdd:pfam12697   1 VVLVHGA-----GLSAAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD---LADLAALLDELGAARPvVLVGHSLGGA 71
                          90       100
                  ....*....|....*....|....*.
gi 440918693  148 LMLHAAIARPEKVIALIGIATAADGL 173
Cdd:pfam12697  72 VALAAAAAALVVGVLVAPLAAPPGLL 97
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
93-161 9.85e-04

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 39.87  E-value: 9.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440918693  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 1.08e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.93  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440918693  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 3.36e-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: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918693   69 IIFIPGYLSNMNGIKAVAV---EEFCKsLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSI---LDDVAEGPQILVGS 142
Cdd:TIGR03101  28 VIYLPPFAEEMNKSRRMVAlqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106
                          90       100
                  ....*....|....*....|..
gi 440918693  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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