NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145611434|ref|NP_078803|]
View 

protein ABHD8 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 171-416 2.13e-35

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: 130.51  E-value: 2.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 171 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFKRYAKKRNVLIG 250
Cdd:COG0596   20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 251 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepsfcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 330
Cdd:COG0596   96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 331 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNT 410
Cdd:COG0596  144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                 ....*.
gi 145611434 411 LLHEFL 416
Cdd:COG0596  213 ALRDFL 218
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 171-416 2.13e-35

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: 130.51  E-value: 2.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 171 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFKRYAKKRNVLIG 250
Cdd:COG0596   20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 251 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepsfcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 330
Cdd:COG0596   96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 331 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNT 410
Cdd:COG0596  144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                 ....*.
gi 145611434 411 LLHEFL 416
Cdd:COG0596  213 ALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 177-403 1.08e-27

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: 110.29  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  177 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVS 256
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  257 FCTFLAHEYPDLVHKVIMINGGGPtALEPSFCSIF-------NMPTCVLHCLSP--CLAWSFLKA-GFARQGAKEKQLLK 326
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDP-PHELDEADRFilalfpgFFDGFVADFAPNplGRLVAKLLAlLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  327 EGNAFNVS--SFVLRAMMSGQYWPEGDEV----YHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMV 400
Cdd:pfam00561 161 NKRFPSGDyaLAKSLVTGALLFIETWSTElrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ...
gi 145611434  401 MLE 403
Cdd:pfam00561 241 FLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 170-416 2.83e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.34  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 170 KGAQADVVLFFIHGVGGSLAIW---KEQLdffvRLGYEVVAPDLAGHGASSaPQVAAAyTFYALAEDMRAIFKRYAKKRN 246
Cdd:PRK14875 126 LGEGDGTPVVLIHGFGGDLNNWlfnHAAL----AAGRPVIALDLPGHGASS-KAVGAG-SLDELAAAVLAFLDALGIERA 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 247 VLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGptalepsfcsifnmptcvlhcLSPCLAWSFLKaGFARQGAKE--KQL 324
Cdd:PRK14875 200 HLVGHSMGGAVALRLAARAPQRVASLTLIAPAG---------------------LGPEINGDYID-GFVAAESRRelKPV 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 325 LKEgnAFNVSSFVLRAM-------------------MSGQYWPEG-------DEVyhAELTVPVLLVHGMHDKFVPVEED 378
Cdd:PRK14875 258 LEL--LFADPALVTRQMvedllkykrldgvddalraLADALFAGGrqrvdlrDRL--ASLAIPVLVIWGEQDRIIPAAHA 333

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 145611434 379 QRMAEIlllAFLKLIDEGSHMVMLECPETVNTLLHEFL 416
Cdd:PRK14875 334 QGLPDG---VAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 180-286 1.50e-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: 214008  Cd Length: 280  Bit Score: 43.37  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 180 FIHGVGGSLAIWKEQLD-------FFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYAlAEDMRAIF---KRY-----AK 243
Cdd:cd12809   44 LIHGGGQTGTNWLNTPDgrpgwasYFLEKGYEVYIVDQPGRGRSPwNPEVGGPLAAST-AETVEQRFtapERYnlwpqAK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 244 KRN------------------------------------------------VLIGHSYGVSFCTFLAHEYPDLVHKVImi 275
Cdd:cd12809  123 LHTqwpgtgrrgdpifdqfyasqvplltnlaeqealvraagcalldiigpaILITHSQGGPFGWLAADARPDLVKAIV-- 200

                        170
                 ....*....|.
gi 145611434 276 ngggptALEPS 286
Cdd:cd12809  201 ------AIEPS 205
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 171-416 2.13e-35

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: 130.51  E-value: 2.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 171 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFKRYAKKRNVLIG 250
Cdd:COG0596   20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 251 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepsfcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 330
Cdd:COG0596   96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 331 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNT 410
Cdd:COG0596  144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                 ....*.
gi 145611434 411 LLHEFL 416
Cdd:COG0596  213 ALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 177-403 1.08e-27

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: 110.29  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  177 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVS 256
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  257 FCTFLAHEYPDLVHKVIMINGGGPtALEPSFCSIF-------NMPTCVLHCLSP--CLAWSFLKA-GFARQGAKEKQLLK 326
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDP-PHELDEADRFilalfpgFFDGFVADFAPNplGRLVAKLLAlLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  327 EGNAFNVS--SFVLRAMMSGQYWPEGDEV----YHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMV 400
Cdd:pfam00561 161 NKRFPSGDyaLAKSLVTGALLFIETWSTElrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ...
gi 145611434  401 MLE 403
Cdd:pfam00561 241 FLE 243
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
172-416 1.87e-20

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 89.29  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 172 AQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQvAAAYTFYALAEDMRAIFKRYAKKRN---VL 248
Cdd:COG2267   25 GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPR-GHVDSFDDYVDDLRAALDALRARPGlpvVL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 249 IGHSYGVSFCTFLAHEYPDLVHKVIMInggGPTALEPSFCSIfnmptcvlhclspclAWSFLKAGFARQGAkekqllkeg 328
Cdd:COG2267  104 LGHSMGGLIALLYAARYPDRVAGLVLL---APAYRADPLLGP---------------SARWLRALRLAEAL--------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 329 nafnvssfvlrammsgqywpegdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEILL-LAFLKLIDEGSHMVMLE-CPE 406
Cdd:COG2267  157 ---------------------------ARIDVPVLVLHGGADRVVPPEAARRLAARLSpDVELVLLPGARHELLNEpARE 209

                        250
                 ....*....|
gi 145611434 407 TVNTLLHEFL 416
Cdd:COG2267  210 EVLAAILAWL 219
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
177-416 3.94e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 74.28  E-value: 3.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 177 VLFFIHGVGGS-LAIWKEQLDFFVRLGYEVVAPDLAGHGASsapqvAAAYTFYALAEDMRAIfkRYAKKRN-------VL 248
Cdd:COG1506   25 VVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGES-----AGDWGGDEVDDVLAAI--DYLAARPyvdpdriGI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 249 IGHSYGVSFCTFLAHEYPDLVHKVImingggptalepSFCSIFNMptcvlhclspclaWSFLKAGFARQGAKEKQLLKEG 328
Cdd:COG1506   98 YGHSYGGYMALLAAARHPDRFKAAV------------ALAGVSDL-------------RSYYGTTREYTERLMGGPWEDP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 329 NAFNVSSFVLRAmmsgqywpegdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAF----LKLIDEGSHMVMLEC 404
Cdd:COG1506  153 EAYAARSPLAYA---------------DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGkpveLLVYPGEGHGFSGAG 217

                        250
                 ....*....|..
gi 145611434 405 PETVNTLLHEFL 416
Cdd:COG1506  218 APDYLERILDFL 229
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
175-416 3.93e-13

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 68.81  E-value: 3.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 175 DVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASsaPQVAAAYTFYALAEDMRAIFkRYAKKRN---VLIGH 251
Cdd:COG1647   15 RKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAY-EILKAGYdkvIVIGL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 252 SYGVSFCTFLAHEYPDlVHKVIMINgggpTALEPSFCSIFNMPtcVLHCLSPclawsFLKagfARQGAKEKQLLKEGNAF 331
Cdd:COG1647   92 SMGGLLALLLAARYPD-VAGLVLLS----PALKIDDPSAPLLP--LLKYLAR-----SLR---GIGSDIEDPEVAEYAYD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 332 NVSSFVLRAMMsgQYWPEGDEVYHaELTVPVLLVHGMHDKFVPVEEDQRMAEIL--LLAFLKLIDEGSHMVMLEC-PETV 408
Cdd:COG1647  157 RTPLRALAELQ--RLIREVRRDLP-KITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVITLDKdREEV 233


                 ....*...
gi 145611434 409 NTLLHEFL 416
Cdd:COG1647  234 AEEILDFL 241
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 178-409 4.72e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 59.02  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  178 LFFIHGVGGSLAiwkeQLDFFVRLGYEVVAPDLAGHGASSAPqvaaAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGvsf 257
Cdd:pfam12697   1 VVLVHGAGLSAA----PLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADLADLAALLDELGAARPVVLVGHSLG--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  258 CTFLAHEYPDLVHKVIMINGGGPTALEPSFCSIFNMPtcvlhclspcLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFV 337
Cdd:pfam12697  70 GAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLAR----------LGAALAAPAWLAAESLARGFLDDLPADAEWAAA 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145611434  338 LRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPvEEDQRMAEILLLAFLKLIDEGSHMVMLEcPETVN 409
Cdd:pfam12697 140 LARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP-ELAQRLLAALAGARLVVLPGAGHLPLDD-PEEVA 209
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 176-280 4.35e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 53.68  E-value: 4.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 176 VVLffIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAaaytfyALAEDMRAIFKRYAKKRNVLIGHSYG- 254
Cdd:COG1075    8 VVL--VHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAE------QLAAFVDAVLAATGAEKVDLVGHSMGg 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 145611434 255 ------VSFctflaHEYPDLVHKVIMIngGGP 280
Cdd:COG1075   80 lvaryyLKR-----LGGAAKVARVVTL--GTP 104
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 172-403 5.41e-09

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: 56.45  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  172 AQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGAsSAPQVAAAYTFYALAEDMRAIF----KRYAKKRNV 247
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGR-SDGKRGHVPSFDDYVDDLDTFVdkirEEHPGLPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  248 LIGHSYGVSFCTFLAHEYPDLVHKVIMINgggptalePSFCSIFNMPTCVLHCLSPCLAWSFLKAGFA------------ 315
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSA--------PALKIKPYLAPPILKLLAKLLGKLFPRLRVPnnllpdslsrdp 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434  316 --RQGAKEKQLLKEGNAFNVSSFVLRAMMSGQywpegdEVYHAeLTVPVLLVHGMHDKFVPVEEDQRMAEIL--LLAFLK 391
Cdd:pfam12146 152 evVAAYAADPLVHGGISARTLYELLDAGERLL------RRAAA-ITVPLLLLHGGADRVVDPAGSREFYERAgsTDKTLK 224

                         250
                  ....*....|..
gi 145611434  392 LIDEGSHMVMLE 403
Cdd:pfam12146 225 LYPGLYHELLNE 236
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 170-416 2.83e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.34  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 170 KGAQADVVLFFIHGVGGSLAIW---KEQLdffvRLGYEVVAPDLAGHGASSaPQVAAAyTFYALAEDMRAIFKRYAKKRN 246
Cdd:PRK14875 126 LGEGDGTPVVLIHGFGGDLNNWlfnHAAL----AAGRPVIALDLPGHGASS-KAVGAG-SLDELAAAVLAFLDALGIERA 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 247 VLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGptalepsfcsifnmptcvlhcLSPCLAWSFLKaGFARQGAKE--KQL 324
Cdd:PRK14875 200 HLVGHSMGGAVALRLAARAPQRVASLTLIAPAG---------------------LGPEINGDYID-GFVAAESRRelKPV 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 325 LKEgnAFNVSSFVLRAM-------------------MSGQYWPEG-------DEVyhAELTVPVLLVHGMHDKFVPVEED 378
Cdd:PRK14875 258 LEL--LFADPALVTRQMvedllkykrldgvddalraLADALFAGGrqrvdlrDRL--ASLAIPVLVIWGEQDRIIPAAHA 333

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 145611434 379 QRMAEIlllAFLKLIDEGSHMVMLECPETVNTLLHEFL 416
Cdd:PRK14875 334 QGLPDG---VAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 176-399 1.99e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 51.84  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 176 VVLFFiHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYalaeDMRAIFkRYAKKRN-------V 247
Cdd:COG1073   39 AVVVA-HGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEgEPREEGSPERR----DARAAV-DYLRTLPgvdperiG 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 248 LIGHSYGVSFCTFLAHEYPDlVHKVIMINGggptalepsFCSIfnmptcvlhclspclawsflkAGFARQGAKEKQLLKE 327
Cdd:COG1073  113 LLGISLGGGYALNAAATDPR-VKAVILDSP---------FTSL---------------------EDLAAQRAKEARGAYL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145611434 328 GNAFNVSSFVLRAMMSGQYWPeGDEVyhAELTVPVLLVHGMHDKFVPVEedqrMAEILLLAF-----LKLIDEGSHM 399
Cdd:COG1073  162 PGVPYLPNVRLASLLNDEFDP-LAKI--EKISRPLLFIHGEKDEAVPFY----MSEDLYEAAaepkeLLIVPGAGHV 231
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 178-279 1.51e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 49.84  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 178 LFFIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPQvAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSF 257
Cdd:PLN02679  91 VLLVHGFGASIPHWRRNIGVLAK-NYTVYAIDLLGFGASDKPP-GFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSLA 168

                         90       100
                 ....*....|....*....|...
gi 145611434 258 CTFLAHEYP-DLVHKVIMINGGG 279
Cdd:PLN02679 169 CVIAASESTrDLVRGLVLLNCAG 191
PLN02578 PLN02578
hydrolase
 170-416 1.90e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.45  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 170 KGAQADVVLffIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPQVAaaYTFYALAEDMRAIFKRYAKKRNVLI 249
Cdd:PLN02578  83 QGEGLPIVL--IHGFGASAFHWRYNIPELAK-KYKVYALDLLGFGWSDKALIE--YDAMVWRDQVADFVKEVVKEPAVLV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 250 GHSYGVSFCTFLAHEYPDLVHKVIMINGGGptalepSFCSIFNMPTCVLHCLSPCLAWSFLKA----------GF----A 315
Cdd:PLN02578 158 GNSLGGFTALSTAVGYPELVAGVALLNSAG------QFGSESREKEEAIVVEETVLTRFVVKPlkewfqrvvlGFlfwqA 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 316 RQGAKEKQLLKE--GNAFNVSSFVLRAMMSGQYWPEGDEVYH-------------------AELTVPVLLVHGMHDKFVP 374
Cdd:PLN02578 232 KQPSRIESVLKSvyKDKSNVDDYLVESITEPAADPNAGEVYYrlmsrflfnqsrytldsllSKLSCPLLLLWGDLDPWVG 311

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 145611434 375 VEEDQRMAEILLLAFLKLIDEGsHMVMLECPETVNTLLHEFL 416
Cdd:PLN02578 312 PAKAEKIKAFYPDTTLVNLQAG-HCPHDEVPEQVNKALLEWL 352
PRK05855 PRK05855
SDR family oxidoreductase;
176-254 8.19e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 48.05  E-value: 8.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 176 VVLffIHGVGGSLAIWKEQLDffvRLG--YEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNV-LIGHS 252
Cdd:PRK05855  28 VVL--VHGYPDNHEVWDGVAP---LLAdrFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHD 102


                 ..
gi 145611434 253 YG 254
Cdd:PRK05855 103 WG 104
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 198-285 1.25e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 46.89  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 198 FVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMING 277
Cdd:PRK00870  69 LAAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT 148


                 ....*...
gi 145611434 278 GGPTALEP 285
Cdd:PRK00870 149 GLPTGDGP 156
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 171-269 9.23e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 44.80  E-value: 9.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 171 GAQADVVlfFIHGVGGSLAIWKEQLdfF------VRLGYEVVAPDLAGHGASSAPqvaaAYTFYALAE--DM--RAIFKR 240
Cdd:PLN03087 199 KAKEDVL--FIHGFISSSAFWTETL--FpnfsdaAKSTYRLFAVDLLGFGRSPKP----ADSLYTLREhlEMieRSVLER 270

                         90       100
                 ....*....|....*....|....*....
gi 145611434 241 YAKKRNVLIGHSYGVSFCTFLAHEYPDLV 269
Cdd:PLN03087 271 YKVKSFHIVAHSLGCILALALAVKHPGAV 299
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 180-286 1.50e-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: 214008  Cd Length: 280  Bit Score: 43.37  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 180 FIHGVGGSLAIWKEQLD-------FFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYAlAEDMRAIF---KRY-----AK 243
Cdd:cd12809   44 LIHGGGQTGTNWLNTPDgrpgwasYFLEKGYEVYIVDQPGRGRSPwNPEVGGPLAAST-AETVEQRFtapERYnlwpqAK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 244 KRN------------------------------------------------VLIGHSYGVSFCTFLAHEYPDLVHKVImi 275
Cdd:cd12809  123 LHTqwpgtgrrgdpifdqfyasqvplltnlaeqealvraagcalldiigpaILITHSQGGPFGWLAADARPDLVKAIV-- 200

                        170
                 ....*....|.
gi 145611434 276 ngggptALEPS 286
Cdd:cd12809  201 ------AIEPS 205
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
177-299 2.36e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.18  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 177 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAP-----QVAAAYTFYALAEDMRAIFkRYAKKRN----- 246
Cdd:COG0412   31 GVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearALMGALDPELLAADLRAAL-DWLKAQPevdag 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145611434 247 --VLIGHSYGVSFCTFLAHEYPDLVhKVIMINGGGPTALEPSFCSIFNMPTCVLH 299
Cdd:COG0412  110 rvGVVGFCFGGGLALLAAARGPDLA-AAVSFYGGLPADDLLDLAARIKAPVLLLY 163
PHA02857 PHA02857
monoglyceride lipase; Provisional
 177-290 4.61e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 38.71  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611434 177 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAyTFYALAEDMR---AIFKR-YAKKRNVLIGHS 252
Cdd:PHA02857  27 LVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMID-DFGVYVRDVVqhvVTIKStYPGVPVFLLGHS 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145611434 253 YGVSFCTFLAHEYPDLVHKVI----MINgggptALEPSFCSI 290
Cdd:PHA02857 106 MGATISILAAYKNPNLFTAMIlmspLVN-----AEAVPRLNL 142
 
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