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Conserved domains on  [gi|56090461|ref|NP_001007665|]
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putative protein-lysine deacylase ABHD14B [Rattus norvegicus]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-209 2.47e-26

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: 100.85  E-value: 2.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   7 SEGTIQVRGQSLFFREARPgNGQAVrfsvLLLHGIRFSSETWQNLgtLHRLAEaGYRAVAIDLPGLGRSKEAAAPAPIGE 86
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGP-DGPPV----VLLHGLPGSSYEWRPL--IPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  87 LApgSFLAAVVDALELGSLVVISPSLSGMYALPF------------------------LVAPESQLRGYVPVAPICTDKI 142
Cdd:COG0596  75 LA--DDLAALLDALGLERVVLVGHSMGGMVALELaarhpervaglvlvdevlaalaepLRRPGLAPEALAALLRALARTD 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56090461 143 NAADYARVKTPTLIVYGDQDPMGSSSFQH--LKQLPNHRVLVMEGAGHPCYLDKPDEWHTGLLDFLQEL 209
Cdd:COG0596 153 LRERLARITVPTLVIWGEKDPIVPPALARrlAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-209 2.47e-26

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: 100.85  E-value: 2.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   7 SEGTIQVRGQSLFFREARPgNGQAVrfsvLLLHGIRFSSETWQNLgtLHRLAEaGYRAVAIDLPGLGRSKEAAAPAPIGE 86
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGP-DGPPV----VLLHGLPGSSYEWRPL--IPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  87 LApgSFLAAVVDALELGSLVVISPSLSGMYALPF------------------------LVAPESQLRGYVPVAPICTDKI 142
Cdd:COG0596  75 LA--DDLAALLDALGLERVVLVGHSMGGMVALELaarhpervaglvlvdevlaalaepLRRPGLAPEALAALLRALARTD 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56090461 143 NAADYARVKTPTLIVYGDQDPMGSSSFQH--LKQLPNHRVLVMEGAGHPCYLDKPDEWHTGLLDFLQEL 209
Cdd:COG0596 153 LRERLARITVPTLVIWGEKDPIVPPALARrlAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 14-142 4.21e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 49.39  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   14 RGQSLFFREARPGNGQAVRFSVLLLHGI-RFSSETWQNLGTLhrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGELAPG-- 90
Cdd:PLN02298  41 RGLSLFTRSWLPSSSSPPRALIFMVHGYgNDISWTFQSTAIF--LAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEdc 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 56090461   91 -SFLAAVVDALELGSL--VVISPSLSGMYALPFLVAPESQLRGYVPVAPIC--TDKI 142
Cdd:PLN02298 119 lSFFNSVKQREEFQGLprFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkiSDKI 175
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 35-100 7.42e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 42.20  E-value: 7.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56090461    35 VLLLHGIRFSSETWQNlgtLHRLAEAGYRAVAIDLPGLGRSKEaaapapIGELAPGSFLAAVVDAL 100
Cdd:TIGR03695   5 LVFLHGFLGSGADWQA---LIEALGPHFRCLAIDLPGHGSSQS------PSDIERYDFEEAAQLLL 61
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 35-118 1.24e-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: 41.72  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461    35 VLLLHGIRFSSETWQNLGTLhrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGELAPGSFLAAVVDALELGSLVVISPSLSG 114
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80


                  ....
gi 56090461   115 MYAL 118
Cdd:pfam00561  81 LIAL 84
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-209 2.47e-26

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: 100.85  E-value: 2.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   7 SEGTIQVRGQSLFFREARPgNGQAVrfsvLLLHGIRFSSETWQNLgtLHRLAEaGYRAVAIDLPGLGRSKEAAAPAPIGE 86
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGP-DGPPV----VLLHGLPGSSYEWRPL--IPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  87 LApgSFLAAVVDALELGSLVVISPSLSGMYALPF------------------------LVAPESQLRGYVPVAPICTDKI 142
Cdd:COG0596  75 LA--DDLAALLDALGLERVVLVGHSMGGMVALELaarhpervaglvlvdevlaalaepLRRPGLAPEALAALLRALARTD 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56090461 143 NAADYARVKTPTLIVYGDQDPMGSSSFQH--LKQLPNHRVLVMEGAGHPCYLDKPDEWHTGLLDFLQEL 209
Cdd:COG0596 153 LRERLARITVPTLVIWGEKDPIVPPALARrlAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-208 1.49e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 75.04  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  15 GQSLFFREARPGngQAVRFSVLLLHGIRFSSETWQNLGtlHRLAEAGYRAVAIDLPGLGRSkeaaaPAPIGELApgSF-- 92
Cdd:COG2267  13 GLRLRGRRWRPA--GSPRGTVVLVHGLGEHSGRYAELA--EALAAAGYAVLAFDLRGHGRS-----DGPRGHVD--SFdd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  93 ----LAAVVDALEL---GSLVVISPSLSGMYALPFLVAPESQLRGYVPVAP-ICTDKIN------------AADYARVKT 152
Cdd:COG2267  82 yvddLRAALDALRArpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPaYRADPLLgpsarwlralrlAEALARIDV 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56090461 153 PTLIVYGDQDPMGSSS-----FQHLkqLPNHRVLVMEGAGHPCYLDKP-DEWHTGLLDFLQE 208
Cdd:COG2267 162 PVLVLHGGADRVVPPEaarrlAARL--SPDVELVLLPGARHELLNEPArEEVLAAILAWLER 221
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
35-188 1.39e-12

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 64.22  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  35 VLLLHGIRFSSEtwQNLGTLHRLAEAGYRAVAIDL--PGLGRSKEAAAPAPIGELAPGSFLAAVVDALEL---------G 103
Cdd:COG0412  32 VVVLHEIFGLNP--HIRDVARRLAAAGYVVLAPDLygRGGPGDDPDEARALMGALDPELLAADLRAALDWlkaqpevdaG 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461 104 SLVVISPSLSGMYALpFLVAPESQLRGYVPVAPICTDKINAADYARVKTPTLIVYGDQDPMGSSS-----FQHLKQL-PN 177
Cdd:COG0412 110 RVGVVGFCFGGGLAL-LAAARGPDLAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDPLVPPEqvaalEAALAAAgVD 188

                       170
                ....*....|.
gi 56090461 178 HRVLVMEGAGH 188
Cdd:COG0412 189 VELHVYPGAGH 199
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
32-210 4.47e-11

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 60.34  E-value: 4.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  32 RFSVLLLHGIRFSSETWQNLGtlHRLAEAGYRAVAIDLPGLGRSKEAAApapigELAPGSFLAAVVDALELGS------- 104
Cdd:COG1647  15 RKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLL-----KTTWEDWLEDVEEAYEILKagydkvi 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461 105 -----------------------LVVISPSLS----GMYALPFL--------------VAPESQLRGY--VPVAPICT-- 139
Cdd:COG1647  88 viglsmggllalllaarypdvagLVLLSPALKiddpSAPLLPLLkylarslrgigsdiEDPEVAEYAYdrTPLRALAElq 167

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56090461 140 --DKINAADYARVKTPTLIVYGDQDPMGSSS-----FQHLKQlPNHRVLVMEGAGHPCYLDK-PDEWHTGLLDFLQELA 210
Cdd:COG1647 168 rlIREVRRDLPKITAPTLIIQSRKDEVVPPEsaryiYERLGS-PDKELVWLEDSGHVITLDKdREEVAEEILDFLERLA 245
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 25-208 6.03e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 51.45  E-value: 6.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  25 PGNGQAVRFSVLLLHGIRFSSETWQNLGtlHRLAEAGYRAVAIDLPGLGRSkeAAAPAPIGELAPGSFLAAV-------- 96
Cdd:COG1073  30 PAGASKKYPAVVVAHGNGGVKEQRALYA--QRLAELGFNVLAFDYRGYGES--EGEPREEGSPERRDARAAVdylrtlpg 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  97 VDALELGslvVISPSLSGMYAL----------------PFL-VAPESQLR------GYVPVAPIC---------TDKINA 144
Cdd:COG1073 106 VDPERIG---LLGISLGGGYALnaaatdprvkavildsPFTsLEDLAAQRakeargAYLPGVPYLpnvrlasllNDEFDP 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56090461 145 ADYA-RVKTPTLIVYGDQDPMGssSFQHLKQL-----PNHRVLVMEGAGH-PCYLDKPDEWHTGLLDFLQE 208
Cdd:COG1073 183 LAKIeKISRPLLFIHGEKDEAV--PFYMSEDLyeaaaEPKELLIVPGAGHvDLYDRPEEEYFDKLAEFFKK 251
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 14-142 4.21e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 49.39  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   14 RGQSLFFREARPGNGQAVRFSVLLLHGI-RFSSETWQNLGTLhrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGELAPG-- 90
Cdd:PLN02298  41 RGLSLFTRSWLPSSSSPPRALIFMVHGYgNDISWTFQSTAIF--LAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEdc 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 56090461   91 -SFLAAVVDALELGSL--VVISPSLSGMYALPFLVAPESQLRGYVPVAPIC--TDKI 142
Cdd:PLN02298 119 lSFFNSVKQREEFQGLprFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkiSDKI 175
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-118 9.07e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 48.40  E-value: 9.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   10 TIQVRGQSLFFREARPGNGQAVrfsvLLLHGirFSSE--TWqnLGTLHRLAeAGYRAVAIDLPGLGRSKEAAAPAPIGEL 87
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDGTPV----VLIHG--FGGDlnNW--LFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDEL 183

                         90       100       110
                 ....*....|....*....|....*....|.
gi 56090461   88 ApgSFLAAVVDALELGSLVVISPSLSGMYAL 118
Cdd:PRK14875 184 A--AAVLAFLDALGIERAHLVGHSMGGAVAL 212
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
35-208 1.17e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.70  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  35 VLLLHGIRFSSEtWQNLGTLHRLAEAGYRAVAIDLPGLGRSKEAAAPAPIGElapgsfLAAVVDALE------LGSLVVI 108
Cdd:COG1506  26 VVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDD------VLAAIDYLAarpyvdPDRIGIY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461 109 SPSLSGMYALpFLVAPESQL-RGYVPVAPICT--------------------------DKINAADYA-RVKTPTLIVYGD 160
Cdd:COG1506  99 GHSYGGYMAL-LAAARHPDRfKAAVALAGVSDlrsyygttreyterlmggpwedpeayAARSPLAYAdKLKTPLLLIHGE 177

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 56090461 161 QD---PMGSSS--FQHLKQL-PNHRVLVMEGAGHPCYLDKPDEWHTGLLDFLQE 208
Cdd:COG1506 178 ADdrvPPEQAErlYEALKKAgKPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 149-210 3.14e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 43.68  E-value: 3.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56090461  149 RVKTPTLIVYGDQD-------PMGSSSFQHLKQLPNHRVLVMEGAGHPCYLDKPDEWHTGLLDFLQELA 210
Cdd:PLN02679 290 RISLPILVLWGDQDpftpldgPVGKYFSSLPSQLPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQLP 358
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 35-100 7.42e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 42.20  E-value: 7.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56090461    35 VLLLHGIRFSSETWQNlgtLHRLAEAGYRAVAIDLPGLGRSKEaaapapIGELAPGSFLAAVVDAL 100
Cdd:TIGR03695   5 LVFLHGFLGSGADWQA---LIEALGPHFRCLAIDLPGHGSSQS------PSDIERYDFEEAAQLLL 61
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 35-118 1.24e-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: 41.72  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461    35 VLLLHGIRFSSETWQNLGTLhrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGELAPGSFLAAVVDALELGSLVVISPSLSG 114
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80


                  ....
gi 56090461   115 MYAL 118
Cdd:pfam00561  81 LIAL 84
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 35-75 1.67e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 41.49  E-value: 1.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 56090461   35 VLLLHGirfsSETWqnlGTLHR-----LAEAGYRAVAIDLPGLGRS 75
Cdd:PRK00870  49 VLLLHG----EPSW---SYLYRkmipiLAAAGHRVIAPDLIGFGRS 87
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 35-100 2.39e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 39.04  E-value: 2.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56090461  35 VLLLHGIRFSSETWQNLGtlHRLAEAGYRAVAIDLPGLGRSKEAAAPApigelapgsfLAAVVDAL 100
Cdd:COG1075   8 VVLVHGLGGSAASWAPLA--PRLRAAGYPVYALNYPSTNGSIEDSAEQ----------LAAFVDAV 61
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 35-197 3.22e-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: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461    35 VLLLHGirfsseTWQNLGTLHRLAEAGYRAVAIDLPGLGRSKE--------AAAPAPIGELAP-----------GSFLAA 95
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPppldladlADLAALLDELGAarpvvlvghslGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461    96 VVDALELGSLVVISPSLSGM----------------YALPFLVAPESQLRGYVPVAPI----------------CTDKIN 143
Cdd:pfam12697  75 AAAAAALVVGVLVAPLAAPPgllaallallarlgaaLAAPAWLAAESLARGFLDDLPAdaewaaalarlaallaALALLP 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56090461   144 AADYARVKTPTLIVYGDQDPMGSSSFQHLKQLPNHRVLVMEGAGHpCYLDKPDE 197
Cdd:pfam12697 155 LAAWRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAGH-LPLDDPEE 207
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 10-108 2.43e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 38.05  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461   10 TIQVRGQSLFFREArpGNGQAVRFsvllLHGIRFSSETWQNLgtLHRLAEAGyRAVAIDLPGLGRSKEAAAPAPIGELAp 89
Cdd:PRK03592  11 RVEVLGSRMAYIET--GEGDPIVF----LHGNPTSSYLWRNI--IPHLAGLG-RCLAPDLIGMGASDKPDIDYTFADHA- 80

                         90
                 ....*....|....*....
gi 56090461   90 gSFLAAVVDALELGSLVVI 108
Cdd:PRK03592  81 -RYLDAWFDALGLDDVVLV 98
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
24-209 3.23e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.16  E-value: 3.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461  24 RPGNGQAVRFSVLLLHG---IRFSSETWQNLgtLHRLAE-AGYRAVAIDLPglgRSKEAAAPAPIGELApgsflAAVVDA 99
Cdd:COG0657   5 RPAGAKGPLPVVVYFHGggwVSGSKDTHDPL--ARRLAArAGAAVVSVDYR---LAPEHPFPAALEDAY-----AALRWL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090461 100 LELGSLVVISPS------------LSGMYALPFLVAPESQLRGYVPVAPICTDKINAAdYARVKT--PTLIVYGDQDPMG 165
Cdd:COG0657  75 RANAAELGIDPDriavagdsagghLAAALALRARDRGGPRPAAQVLIYPVLDLTASPL-RADLAGlpPTLIVTGEADPLV 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 56090461 166 SSS---FQHLKQL-PNHRVLVMEGAGHPCYLDKP----DEWHTGLLDFLQEL 209
Cdd:COG0657 154 DESealAAALRAAgVPVELHVYPGGGHGFGLLAGlpeaRAALAEIAAFLRRA 205
 
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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