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Conserved domains on  [gi|1910364579|ref|XP_016013293|]
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protein ABHD8 [Rousettus aegyptiacus]

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, ...
 165-410 6.09e-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: 128.97  E-value: 6.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 165 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFKRYAKKRNVLIG 244
Cdd:COG0596    20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 245 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepsfcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 324
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 325 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNT 404
Cdd:COG0596   144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                  ....*.
gi 1910364579 405 LLHEFL 410
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, ...
 165-410 6.09e-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: 128.97  E-value: 6.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 165 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFKRYAKKRNVLIG 244
Cdd:COG0596    20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 245 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepsfcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 324
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 325 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNT 404
Cdd:COG0596   144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                  ....*.
gi 1910364579 405 LLHEFL 410
Cdd:COG0596   213 ALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 171-397 1.49e-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: 109.90  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 171 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVS 250
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 251 FCTFLAHEYPDLVHKVIMINGGGPtALEPSFCSIF-------NMPTCVLHCLSP--CLAWSFLKA-GFARQGAKEKQLLK 320
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDP-PHELDEADRFilalfpgFFDGFVADFAPNplGRLVAKLLAlLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 321 EGNAFNVS--SFVLRAMMSGQYWPEGDEV----YHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMV 394
Cdd:pfam00561 161 NKRFPSGDyaLAKSLVTGALLFIETWSTElrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ...
gi 1910364579 395 MLE 397
Cdd:pfam00561 241 FLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 164-410 5.68e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.56  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 164 KGAQADVVLFFIHGVGGSLAIW---KEQLdffvRLGYEVVAPDLAGHGASSaPQVAAAyTFYALAEDMRAIFKRYAKKRN 240
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNWlfnHAAL----AAGRPVIALDLPGHGASS-KAVGAG-SLDELAAAVLAFLDALGIERA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 241 VLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGptalepsfcsifnmptcvlhcLSPCLAWSFLKaGFARQGAKE--KQL 318
Cdd:PRK14875  200 HLVGHSMGGAVALRLAARAPQRVASLTLIAPAG---------------------LGPEINGDYID-GFVAAESRRelKPV 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 319 LKEgnAFNVSSFVLRAM-------------------MSGQYWPEG-------DEVyhAELTVPVLLVHGMHDKFVPVEED 372
Cdd:PRK14875  258 LEL--LFADPALVTRQMvedllkykrldgvddalraLADALFAGGrqrvdlrDRL--ASLAIPVLVIWGEQDRIIPAAHA 333

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1910364579 373 QRMAEIlllAFLKLIDEGSHMVMLECPETVNTLLHEFL 410
Cdd:PRK14875  334 QGLPDG---VAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 174-280 2.26e-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: 42.60  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 174 FIHGVGGSLAIWKEQLD-------FFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYAlAEDMRAIF---KRY-----AK 237
Cdd:cd12809    44 LIHGGGQTGTNWLNTPDgrpgwasYFLEKGYEVYIVDQPGRGRSPwNPEVGGPLAAST-AETVEQRFtapERYnlwpqAK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 238 KRN------------------------------------------------VLIGHSYGVSFCTFLAHEYPDLVHKVImi 269
Cdd:cd12809   123 LHTqwpgtgrrgdpifdqfyasqvplltnlaeqealvraagcalldiigpaILITHSQGGPFGWLAADARPDLVKAIV-- 200

                         170
                  ....*....|.
gi 1910364579 270 ngggptALEPS 280
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, ...
 165-410 6.09e-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: 128.97  E-value: 6.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 165 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFKRYAKKRNVLIG 244
Cdd:COG0596    20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 245 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepsfcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 324
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 325 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNT 404
Cdd:COG0596   144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                  ....*.
gi 1910364579 405 LLHEFL 410
Cdd:COG0596   213 ALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 171-397 1.49e-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: 109.90  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 171 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVS 250
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 251 FCTFLAHEYPDLVHKVIMINGGGPtALEPSFCSIF-------NMPTCVLHCLSP--CLAWSFLKA-GFARQGAKEKQLLK 320
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDP-PHELDEADRFilalfpgFFDGFVADFAPNplGRLVAKLLAlLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 321 EGNAFNVS--SFVLRAMMSGQYWPEGDEV----YHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMV 394
Cdd:pfam00561 161 NKRFPSGDyaLAKSLVTGALLFIETWSTElrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ...
gi 1910364579 395 MLE 397
Cdd:pfam00561 241 FLE 243
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
166-410 4.01e-20

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 88.52  E-value: 4.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 166 AQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQvAAAYTFYALAEDMRAIFKRYAKKRN---VL 242
Cdd:COG2267    25 GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPR-GHVDSFDDYVDDLRAALDALRARPGlpvVL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 243 IGHSYGVSFCTFLAHEYPDLVHKVIMInggGPTALEPSFCSIfnmptcvlhclspclAWSFLKAGFARQGAkekqllkeg 322
Cdd:COG2267   104 LGHSMGGLIALLYAARYPDRVAGLVLL---APAYRADPLLGP---------------SARWLRALRLAEAL--------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 323 nafnvssfvlrammsgqywpegdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEILL-LAFLKLIDEGSHMVMLE-CPE 400
Cdd:COG2267   157 ---------------------------ARIDVPVLVLHGGADRVVPPEAARRLAARLSpDVELVLLPGARHELLNEpARE 209

                         250
                  ....*....|
gi 1910364579 401 TVNTLLHEFL 410
Cdd:COG2267   210 EVLAAILAWL 219
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
171-410 6.06e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.90  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 171 VLFFIHGVGGS-LAIWKEQLDFFVRLGYEVVAPDLAGHGASsapqvAAAYTFYALAEDMRAIfkRYAKKRN-------VL 242
Cdd:COG1506    25 VVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGES-----AGDWGGDEVDDVLAAI--DYLAARPyvdpdriGI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 243 IGHSYGVSFCTFLAHEYPDLVHKVImingggptalepSFCSIFNMptcvlhclspclaWSFLKAGFARQGAKEKQLLKEG 322
Cdd:COG1506    98 YGHSYGGYMALLAAARHPDRFKAAV------------ALAGVSDL-------------RSYYGTTREYTERLMGGPWEDP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 323 NAFNVSSFVLRAmmsgqywpegdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAF----LKLIDEGSHMVMLEC 398
Cdd:COG1506   153 EAYAARSPLAYA---------------DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGkpveLLVYPGEGHGFSGAG 217

                         250
                  ....*....|..
gi 1910364579 399 PETVNTLLHEFL 410
Cdd:COG1506   218 APDYLERILDFL 229
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
169-410 5.24e-13

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 68.43  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 169 DVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASsaPQVAAAYTFYALAEDMRAIFkRYAKKRN---VLIGH 245
Cdd:COG1647    15 RKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAY-EILKAGYdkvIVIGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 246 SYGVSFCTFLAHEYPDlVHKVIMINgggpTALEPSFCSIFNMPtcVLHCLSPclawsFLKagfARQGAKEKQLLKEGNAF 325
Cdd:COG1647    92 SMGGLLALLLAARYPD-VAGLVLLS----PALKIDDPSAPLLP--LLKYLAR-----SLR---GIGSDIEDPEVAEYAYD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 326 NVSSFVLRAMMsgQYWPEGDEVYHaELTVPVLLVHGMHDKFVPVEEDQRMAEIL--LLAFLKLIDEGSHMVMLEC-PETV 402
Cdd:COG1647   157 RTPLRALAELQ--RLIREVRRDLP-KITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVITLDKdREEV 233


                  ....*...
gi 1910364579 403 NTLLHEFL 410
Cdd:COG1647   234 AEEILDFL 241
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 172-403 1.22e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 57.87  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 172 LFFIHGVGGSLAiwkeQLDFFVRLGYEVVAPDLAGHGASSAPqvaaAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGvsf 251
Cdd:pfam12697   1 VVLVHGAGLSAA----PLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADLADLAALLDELGAARPVVLVGHSLG--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 252 CTFLAHEYPDLVHKVIMINGGGPTALEPSFCSIFNMPtcvlhclspcLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFV 331
Cdd:pfam12697  70 GAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLAR----------LGAALAAPAWLAAESLARGFLDDLPADAEWAAA 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1910364579 332 LRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPvEEDQRMAEILLLAFLKLIDEGSHMVMLEcPETVN 403
Cdd:pfam12697 140 LARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP-ELAQRLLAALAGARLVVLPGAGHLPLDD-PEEVA 209
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 170-274 6.45e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 53.29  E-value: 6.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 170 VVLffIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAaaytfyALAEDMRAIFKRYAKKRNVLIGHSYG- 248
Cdd:COG1075     8 VVL--VHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAE------QLAAFVDAVLAATGAEKVDLVGHSMGg 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1910364579 249 ------VSFctflaHEYPDLVHKVIMIngGGP 274
Cdd:COG1075    80 lvaryyLKR-----LGGAAKVARVVTL--GTP 104
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 166-397 8.52e-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: 55.68  E-value: 8.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 166 AQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGAsSAPQVAAAYTFYALAEDMRAIF----KRYAKKRNV 241
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGR-SDGKRGHVPSFDDYVDDLDTFVdkirEEHPGLPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 242 LIGHSYGVSFCTFLAHEYPDLVHKVIMINgggptalePSFCSIFNMPTCVLHCLSPCLAWSFLKAGFA------------ 309
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSA--------PALKIKPYLAPPILKLLAKLLGKLFPRLRVPnnllpdslsrdp 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 310 --RQGAKEKQLLKEGNAFNVSSFVLRAMMSGQywpegdEVYHAeLTVPVLLVHGMHDKFVPVEEDQRMAEIL--LLAFLK 385
Cdd:pfam12146 152 evVAAYAADPLVHGGISARTLYELLDAGERLL------RRAAA-ITVPLLLLHGGADRVVDPAGSREFYERAgsTDKTLK 224

                         250
                  ....*....|..
gi 1910364579 386 LIDEGSHMVMLE 397
Cdd:pfam12146 225 LYPGLYHELLNE 236
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 164-410 5.68e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.56  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 164 KGAQADVVLFFIHGVGGSLAIW---KEQLdffvRLGYEVVAPDLAGHGASSaPQVAAAyTFYALAEDMRAIFKRYAKKRN 240
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNWlfnHAAL----AAGRPVIALDLPGHGASS-KAVGAG-SLDELAAAVLAFLDALGIERA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 241 VLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGptalepsfcsifnmptcvlhcLSPCLAWSFLKaGFARQGAKE--KQL 318
Cdd:PRK14875  200 HLVGHSMGGAVALRLAARAPQRVASLTLIAPAG---------------------LGPEINGDYID-GFVAAESRRelKPV 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 319 LKEgnAFNVSSFVLRAM-------------------MSGQYWPEG-------DEVyhAELTVPVLLVHGMHDKFVPVEED 372
Cdd:PRK14875  258 LEL--LFADPALVTRQMvedllkykrldgvddalraLADALFAGGrqrvdlrDRL--ASLAIPVLVIWGEQDRIIPAAHA 333

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1910364579 373 QRMAEIlllAFLKLIDEGSHMVMLECPETVNTLLHEFL 410
Cdd:PRK14875  334 QGLPDG---VAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 170-393 2.98e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 51.45  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 170 VVLFFiHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYalaeDMRAIFkRYAKKRN-------V 241
Cdd:COG1073    39 AVVVA-HGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEgEPREEGSPERR----DARAAV-DYLRTLPgvdperiG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 242 LIGHSYGVSFCTFLAHEYPDlVHKVIMINGggptalepsFCSIfnmptcvlhclspclawsflkAGFARQGAKEKQLLKE 321
Cdd:COG1073   113 LLGISLGGGYALNAAATDPR-VKAVILDSP---------FTSL---------------------EDLAAQRAKEARGAYL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910364579 322 GNAFNVSSFVLRAMMSGQYWPeGDEVyhAELTVPVLLVHGMHDKFVPVEedqrMAEILLLAF-----LKLIDEGSHM 393
Cdd:COG1073   162 PGVPYLPNVRLASLLNDEFDP-LAKI--EKISRPLLFIHGEKDEAVPFY----MSEDLYEAAaepkeLLIVPGAGHV 231
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 172-273 1.62e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 49.84  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 172 LFFIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPQvAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSF 251
Cdd:PLN02679   91 VLLVHGFGASIPHWRRNIGVLAK-NYTVYAIDLLGFGASDKPP-GFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSLA 168

                          90       100
                  ....*....|....*....|...
gi 1910364579 252 CTFLAHEYP-DLVHKVIMINGGG 273
Cdd:PLN02679  169 CVIAASESTrDLVRGLVLLNCAG 191
PLN02578 PLN02578
hydrolase
 164-410 2.06e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.45  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 164 KGAQADVVLffIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPQVAaaYTFYALAEDMRAIFKRYAKKRNVLI 243
Cdd:PLN02578   83 QGEGLPIVL--IHGFGASAFHWRYNIPELAK-KYKVYALDLLGFGWSDKALIE--YDAMVWRDQVADFVKEVVKEPAVLV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 244 GHSYGVSFCTFLAHEYPDLVHKVIMINGGGptalepSFCSIFNMPTCVLHCLSPCLAWSFLKA----------GF----A 309
Cdd:PLN02578  158 GNSLGGFTALSTAVGYPELVAGVALLNSAG------QFGSESREKEEAIVVEETVLTRFVVKPlkewfqrvvlGFlfwqA 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 310 RQGAKEKQLLKE--GNAFNVSSFVLRAMMSGQYWPEGDEVYH-------------------AELTVPVLLVHGMHDKFVP 368
Cdd:PLN02578  232 KQPSRIESVLKSvyKDKSNVDDYLVESITEPAADPNAGEVYYrlmsrflfnqsrytldsllSKLSCPLLLLWGDLDPWVG 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1910364579 369 VEEDQRMAEILLLAFLKLIDEGsHMVMLECPETVNTLLHEFL 410
Cdd:PLN02578  312 PAKAEKIKAFYPDTTLVNLQAG-HCPHDEVPEQVNKALLEWL 352
PRK05855 PRK05855
SDR family oxidoreductase;
170-248 1.07e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 47.67  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 170 VVLffIHGVGGSLAIWKEQLDffvRLG--YEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNV-LIGHS 246
Cdd:PRK05855   28 VVL--VHGYPDNHEVWDGVAP---LLAdrFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHD 102


                  ..
gi 1910364579 247 YG 248
Cdd:PRK05855  103 WG 104
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 192-279 1.36e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 46.50  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 192 FVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMING 271
Cdd:PRK00870   69 LAAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT 148


                  ....*...
gi 1910364579 272 GGPTALEP 279
Cdd:PRK00870  149 GLPTGDGP 156
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 165-263 9.60e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 44.41  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 165 GAQADVVlfFIHGVGGSLAIWKEQLdfF------VRLGYEVVAPDLAGHGASSAPqvaaAYTFYALAE--DM--RAIFKR 234
Cdd:PLN03087  199 KAKEDVL--FIHGFISSSAFWTETL--FpnfsdaAKSTYRLFAVDLLGFGRSPKP----ADSLYTLREhlEMieRSVLER 270

                          90       100
                  ....*....|....*....|....*....
gi 1910364579 235 YAKKRNVLIGHSYGVSFCTFLAHEYPDLV 263
Cdd:PLN03087  271 YKVKSFHIVAHSLGCILALALAVKHPGAV 299
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 174-280 2.26e-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: 42.60  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 174 FIHGVGGSLAIWKEQLD-------FFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYAlAEDMRAIF---KRY-----AK 237
Cdd:cd12809    44 LIHGGGQTGTNWLNTPDgrpgwasYFLEKGYEVYIVDQPGRGRSPwNPEVGGPLAAST-AETVEQRFtapERYnlwpqAK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 238 KRN------------------------------------------------VLIGHSYGVSFCTFLAHEYPDLVHKVImi 269
Cdd:cd12809   123 LHTqwpgtgrrgdpifdqfyasqvplltnlaeqealvraagcalldiigpaILITHSQGGPFGWLAADARPDLVKAIV-- 200

                         170
                  ....*....|.
gi 1910364579 270 ngggptALEPS 280
Cdd:cd12809   201 ------AIEPS 205
LIP pfam03583
Secretory lipase; These lipases are expressed and secreted during the infection cycle of these ...
 255-378 3.62e-03

Secretory lipase; These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.


Pssm-ID: 367570  Cd Length: 286  Bit Score: 38.95  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 255 LAHEYPDLvhKVIMINGGGPTALEpsfcsIFNMPTcvLHCLSPCL---AWSFLKAGFARQGAKEKQLLKEGNafnVSSFV 331
Cdd:pfam03583 136 LANEYPDF--KSILYEETNDSGRE-----ALKKLS--EMCLADALigyPGDSMFTGDNRVFESGWDILKDET---ISKTI 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1910364579 332 LRAMMSGQYWPegdevyhaelTVPVLLVHGMHDKFVPVEEDQRMAEI 378
Cdd:pfam03583 204 EDNLLSKSAVP----------QIPVFIYHGVIDEIIPIKDIKKLYQN 240
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
171-293 3.75e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.79  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 171 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAP-----QVAAAYTFYALAEDMRAIFkRYAKKRN----- 240
Cdd:COG0412    31 GVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearALMGALDPELLAADLRAAL-DWLKAQPevdag 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910364579 241 --VLIGHSYGVSFCTFLAHEYPDLVhKVIMINGGGPTALEPSFCSIFNMPTCVLH 293
Cdd:COG0412   110 rvGVVGFCFGGGLALLAAARGPDLA-AAVSFYGGLPADDLLDLAARIKAPVLLLY 163
PHA02857 PHA02857
monoglyceride lipase; Provisional
 171-284 4.99e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 38.71  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910364579 171 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAyTFYALAEDMR---AIFKR-YAKKRNVLIGHS 246
Cdd:PHA02857   27 LVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMID-DFGVYVRDVVqhvVTIKStYPGVPVFLLGHS 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1910364579 247 YGVSFCTFLAHEYPDLVHKVI----MINgggptALEPSFCSI 284
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.
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