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Conserved domains on  [gi|1720428126|ref|XP_030099565|]
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protein ABHD8 isoform X1 [Mus musculus]

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, ...
 163-408 1.15e-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: 131.28  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 163 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFTRYAKKRNVLIG 242
Cdd:COG0596    20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 243 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepslcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 322
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 323 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIEEGSHMVMLECPETVNT 402
Cdd:COG0596   144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                  ....*.
gi 1720428126 403 LLHEFL 408
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, ...
 163-408 1.15e-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: 131.28  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 163 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFTRYAKKRNVLIG 242
Cdd:COG0596    20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 243 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepslcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 322
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 323 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIEEGSHMVMLECPETVNT 402
Cdd:COG0596   144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                  ....*.
gi 1720428126 403 LLHEFL 408
Cdd:COG0596   213 ALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 169-395 2.97e-28

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: 111.83  E-value: 2.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 169 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFTRYAKKRNVLIGHSYGVS 248
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 249 FCTFLAHEYPDLVHKVIMINGGGPtALEPSLCSIF-------NMPTCVLHCLSP--CLAWSFLKA-GFARQGAKEKQLLK 318
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDP-PHELDEADRFilalfpgFFDGFVADFAPNplGRLVAKLLAlLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 319 EGNAFNVS--SFVLRAMMSGQYWPEGDEV----YHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIEEGSHMV 392
Cdd:pfam00561 161 NKRFPSGDyaLAKSLVTGALLFIETWSTElrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ...
gi 1720428126 393 MLE 395
Cdd:pfam00561 241 FLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 162-408 4.04e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.95  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 162 KGAQADVVLFFIHGVGGSLAIW---KEQLdffvRLGYEVVAPDLAGHGASSaPQVAAAyTFYALAEDMRAIFTRYAKKRN 238
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNWlfnHAAL----AAGRPVIALDLPGHGASS-KAVGAG-SLDELAAAVLAFLDALGIERA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 239 VLIGHSYGVSFCTFLAHEYPDLVHKVIM---------INGG-------GPT--ALEPSLCSIFNMPTCVLHclspclawS 300
Cdd:PRK14875  200 HLVGHSMGGAVALRLAARAPQRVASLTLiapaglgpeINGDyidgfvaAESrrELKPVLELLFADPALVTR--------Q 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 301 FLKAGFarqgaKEKQLlkEGnafnVSSFvLRAmMSGQYWPEG-------DEVyhAELTVPVLLVHGMHDKFVPVEEDQRM 373
Cdd:PRK14875  272 MVEDLL-----KYKRL--DG----VDDA-LRA-LADALFAGGrqrvdlrDRL--ASLAIPVLVIWGEQDRIIPAAHAQGL 336

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720428126 374 AEIlllAFLKLIEEGSHMVMLECPETVNTLLHEFL 408
Cdd:PRK14875  337 PDG---VAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 172-278 6.40e-05

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: 44.52  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 172 FIHGVGGSLAIWKEQLD-------FFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYAlAEDMRAIFT---RY-----AK 235
Cdd:cd12809    44 LIHGGGQTGTNWLNTPDgrpgwasYFLEKGYEVYIVDQPGRGRSPwNPEVGGPLAAST-AETVEQRFTapeRYnlwpqAK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 236 KRN------------------------------------------------VLIGHSYGVSFCTFLAHEYPDLVHKVImi 267
Cdd:cd12809   123 LHTqwpgtgrrgdpifdqfyasqvplltnlaeqealvraagcalldiigpaILITHSQGGPFGWLAADARPDLVKAIV-- 200

                         170
                  ....*....|.
gi 1720428126 268 ngggptALEPS 278
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, ...
 163-408 1.15e-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: 131.28  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 163 GAQADVVLFfIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPqvAAAYTFYALAEDMRAIFTRYAKKRNVLIG 242
Cdd:COG0596    20 GPDGPPVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 243 HSYGVSFCTFLAHEYPDLVHKVIMINGggptalepslcsifnmptcvlhclspclAWSFLKAGFARQGAKEKQLLKegna 322
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDE----------------------------VLAALAEPLRRPGLAPEALAA---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 323 fnvssfVLRAMMSGQYWPEgdevyHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIEEGSHMVMLECPETVNT 402
Cdd:COG0596   144 ------LLRALARTDLRER-----LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAA 212


                  ....*.
gi 1720428126 403 LLHEFL 408
Cdd:COG0596   213 ALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 169-395 2.97e-28

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: 111.83  E-value: 2.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 169 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFTRYAKKRNVLIGHSYGVS 248
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 249 FCTFLAHEYPDLVHKVIMINGGGPtALEPSLCSIF-------NMPTCVLHCLSP--CLAWSFLKA-GFARQGAKEKQLLK 318
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDP-PHELDEADRFilalfpgFFDGFVADFAPNplGRLVAKLLAlLLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 319 EGNAFNVS--SFVLRAMMSGQYWPEGDEV----YHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIEEGSHMV 392
Cdd:pfam00561 161 NKRFPSGDyaLAKSLVTGALLFIETWSTElrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240


                  ...
gi 1720428126 393 MLE 395
Cdd:pfam00561 241 FLE 243
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
164-408 9.34e-22

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 93.14  E-value: 9.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 164 AQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQvAAAYTFYALAEDMRAiFTRYAKKRN----V 239
Cdd:COG2267    25 GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPR-GHVDSFDDYVDDLRA-ALDALRARPglpvV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 240 LIGHSYGVSFCTFLAHEYPDLVHKVIMInggGPTALEPSLCSIfnmptcvlhclspclAWSFLKAGFARQGAkekqllke 319
Cdd:COG2267   103 LLGHSMGGLIALLYAARYPDRVAGLVLL---APAYRADPLLGP---------------SARWLRALRLAEAL-------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 320 gnafnvssfvlrammsgqywpegdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEILL-LAFLKLIEEGSHMVMLE-CP 397
Cdd:COG2267   157 ----------------------------ARIDVPVLVLHGGADRVVPPEAARRLAARLSpDVELVLLPGARHELLNEpAR 208

                         250
                  ....*....|.
gi 1720428126 398 ETVNTLLHEFL 408
Cdd:COG2267   209 EEVLAAILAWL 219
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
169-408 1.41e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 75.82  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 169 VLFFIHGVGGS-LAIWKEQLDFFVRLGYEVVAPDLAGHGASsapqvAAAYTFYALAEDMRAIftRYAKKRN-------VL 240
Cdd:COG1506    25 VVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGES-----AGDWGGDEVDDVLAAI--DYLAARPyvdpdriGI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 241 IGHSYGVSFCTFLAHEYPDLVHKVImingggptalepSLCSIFNMptcvlhclspclaWSFLKAGFARQGAKEKQLLKEG 320
Cdd:COG1506    98 YGHSYGGYMALLAAARHPDRFKAAV------------ALAGVSDL-------------RSYYGTTREYTERLMGGPWEDP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 321 NAFNVSSFVLRAmmsgqywpegdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAF----LKLIEEGSHMVMLEC 396
Cdd:COG1506   153 EAYAARSPLAYA---------------DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGkpveLLVYPGEGHGFSGAG 217

                         250
                  ....*....|..
gi 1720428126 397 PETVNTLLHEFL 408
Cdd:COG1506   218 APDYLERILDFL 229
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
167-408 3.08e-13

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 69.20  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 167 DVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASsaPQVAAAYTFYALAEDMRAIFtRYAKKRN---VLIGH 243
Cdd:COG1647    15 RKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAY-EILKAGYdkvIVIGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 244 SYGVSFCTFLAHEYPDlVHKVIMINgggpTALEPSLCSIFNMPtcVLHCLSPclawsFLKagfARQGAKEKQLLKEGNAF 323
Cdd:COG1647    92 SMGGLLALLLAARYPD-VAGLVLLS----PALKIDDPSAPLLP--LLKYLAR-----SLR---GIGSDIEDPEVAEYAYD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 324 NVSSFVLRAMMsgQYWPEGDEVYHaELTVPVLLVHGMHDKFVPVEEDQRMAEIL--LLAFLKLIEEGSHMVMLEC-PETV 400
Cdd:COG1647   157 RTPLRALAELQ--RLIREVRRDLP-KITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVITLDKdREEV 233


                  ....*...
gi 1720428126 401 NTLLHEFL 408
Cdd:COG1647   234 AEEILDFL 241
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 170-401 4.14e-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: 59.41  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 170 LFFIHGVGGSLAiwkeQLDFFVRLGYEVVAPDLAGHGASSAPqvaaAYTFYALAEDMRAIFTRYAKKRNVLIGHSYGvsf 249
Cdd:pfam12697   1 VVLVHGAGLSAA----PLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADLADLAALLDELGAARPVVLVGHSLG--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 250 CTFLAHEYPDLVHKVIMINGGGPTALEPSLCSIFNMPtcvlhclspcLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFV 329
Cdd:pfam12697  70 GAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLAR----------LGAALAAPAWLAAESLARGFLDDLPADAEWAAA 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720428126 330 LRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPvEEDQRMAEILLLAFLKLIEEGSHMVMLEcPETVN 401
Cdd:pfam12697 140 LARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP-ELAQRLLAALAGARLVVLPGAGHLPLDD-PEEVA 209
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 164-395 7.31e-10

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: 59.15  E-value: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 164 AQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGAsSAPQVAAAYTFYALAEDMRAiFTRYAKKRN----- 238
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGR-SDGKRGHVPSFDDYVDDLDT-FVDKIREEHpglpl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 239 VLIGHSYGVSFCTFLAHEYPDLVHKVIMInggGPtALEPSLcsifNMPTCVLHCLSPCLAWSFLKAGFA----------- 307
Cdd:pfam12146  79 FLLGHSMGGLIAALYALRYPDKVDGLILS---AP-ALKIKP----YLAPPILKLLAKLLGKLFPRLRVPnnllpdslsrd 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 308 ---RQGAKEKQLLKEGNAFNVSSFVLRAMMsgQYWPEGdevyhAELTVPVLLVHGMHDKFVPVEEDQRMAEIL--LLAFL 382
Cdd:pfam12146 151 pevVAAYAADPLVHGGISARTLYELLDAGE--RLLRRA-----AAITVPLLLLHGGADRVVDPAGSREFYERAgsTDKTL 223

                         250
                  ....*....|...
gi 1720428126 383 KLIEEGSHMVMLE 395
Cdd:pfam12146 224 KLYPGLYHELLNE 236
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 168-272 5.24e-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: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 168 VVLffIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAaaytfyALAEDMRAIFTRYAKKRNVLIGHSYG- 246
Cdd:COG1075     8 VVL--VHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAE------QLAAFVDAVLAATGAEKVDLVGHSMGg 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720428126 247 ------VSFctflaHEYPDLVHKVIMIngGGP 272
Cdd:COG1075    80 lvaryyLKR-----LGGAAKVARVVTL--GTP 104
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 162-408 4.04e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.95  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 162 KGAQADVVLFFIHGVGGSLAIW---KEQLdffvRLGYEVVAPDLAGHGASSaPQVAAAyTFYALAEDMRAIFTRYAKKRN 238
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNWlfnHAAL----AAGRPVIALDLPGHGASS-KAVGAG-SLDELAAAVLAFLDALGIERA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 239 VLIGHSYGVSFCTFLAHEYPDLVHKVIM---------INGG-------GPT--ALEPSLCSIFNMPTCVLHclspclawS 300
Cdd:PRK14875  200 HLVGHSMGGAVALRLAARAPQRVASLTLiapaglgpeINGDyidgfvaAESrrELKPVLELLFADPALVTR--------Q 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 301 FLKAGFarqgaKEKQLlkEGnafnVSSFvLRAmMSGQYWPEG-------DEVyhAELTVPVLLVHGMHDKFVPVEEDQRM 373
Cdd:PRK14875  272 MVEDLL-----KYKRL--DG----VDDA-LRA-LADALFAGGrqrvdlrDRL--ASLAIPVLVIWGEQDRIIPAAHAQGL 336

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720428126 374 AEIlllAFLKLIEEGSHMVMLECPETVNTLLHEFL 408
Cdd:PRK14875  337 PDG---VAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 168-422 1.36e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 52.61  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 168 VVLFFiHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYalaeDMRAIFtRYAKKRN-------V 239
Cdd:COG1073    39 AVVVA-HGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEgEPREEGSPERR----DARAAV-DYLRTLPgvdperiG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 240 LIGHSYGVSFCTFLAHEYPDlVHKVIMIngGGPTALEPslcsifnmptcvlhclspclawsflkagFARQGAKEKQLLKE 319
Cdd:COG1073   113 LLGISLGGGYALNAAATDPR-VKAVILD--SPFTSLED----------------------------LAAQRAKEARGAYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 320 GNAFNVSSFVLRAMMSGQYWPeGDEVyhAELTVPVLLVHGMHDKFVPVEedqrMAEILLLAF-----LKLIEEGSHMvml 394
Cdd:COG1073   162 PGVPYLPNVRLASLLNDEFDP-LAKI--EKISRPLLFIHGEKDEAVPFY----MSEDLYEAAaepkeLLIVPGAGHV--- 231

                         250       260
                  ....*....|....*....|....*...
gi 1720428126 395 ecpetvntllheFLLWEPEPEAEPKLEP 422
Cdd:COG1073   232 ------------DLYDRPEEEYFDKLAE 247
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 170-271 5.95e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 48.30  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 170 LFFIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPQvAAAYTFYALAEDMRAIFTRYAKKRNVLIGHSYGVSF 249
Cdd:PLN02679   91 VLLVHGFGASIPHWRRNIGVLAK-NYTVYAIDLLGFGASDKPP-GFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSLA 168

                          90       100
                  ....*....|....*....|...
gi 1720428126 250 CTFLAHEYP-DLVHKVIMINGGG 271
Cdd:PLN02679  169 CVIAASESTrDLVRGLVLLNCAG 191
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 190-277 6.17e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 47.66  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 190 FVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFTRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMING 269
Cdd:PRK00870   69 LAAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT 148


                  ....*...
gi 1720428126 270 GGPTALEP 277
Cdd:PRK00870  149 GLPTGDGP 156
PRK05855 PRK05855
SDR family oxidoreductase;
168-246 1.33e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 47.28  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 168 VVLffIHGVGGSLAIWKEQLDffvRLG--YEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFTRYAKKRNV-LIGHS 244
Cdd:PRK05855   28 VVL--VHGYPDNHEVWDGVAP---LLAdrFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHD 102


                  ..
gi 1720428126 245 YG 246
Cdd:PRK05855  103 WG 104
PLN02578 PLN02578
hydrolase
 162-408 2.50e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.99  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 162 KGAQADVVLffIHGVGGSLAIWKEQLDFFVRlGYEVVAPDLAGHGASSAPQVAaaYTFYALAEDMRAIFTRYAKKRNVLI 241
Cdd:PLN02578   83 QGEGLPIVL--IHGFGASAFHWRYNIPELAK-KYKVYALDLLGFGWSDKALIE--YDAMVWRDQVADFVKEVVKEPAVLV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 242 GHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSlcsifnMPTCVLHCLSPCLAWSFLKA----------GF----A 307
Cdd:PLN02578  158 GNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESR------EKEEAIVVEETVLTRFVVKPlkewfqrvvlGFlfwqA 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 308 RQGAKEKQLLKE--GNAFNVSSFVLRAMMSGQYWPEGDEVYH-------------------AELTVPVLLVHGMHDKFVP 366
Cdd:PLN02578  232 KQPSRIESVLKSvyKDKSNVDDYLVESITEPAADPNAGEVYYrlmsrflfnqsrytldsllSKLSCPLLLLWGDLDPWVG 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720428126 367 VEEDQRMAEILLLAFLKLIEEGsHMVMLECPETVNTLLHEFL 408
Cdd:PLN02578  312 PAKAEKIKAFYPDTTLVNLQAG-HCPHDEVPEQVNKALLEWL 352
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 172-278 6.40e-05

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: 44.52  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 172 FIHGVGGSLAIWKEQLD-------FFVRLGYEVVAPDLAGHGASS-APQVAAAYTFYAlAEDMRAIFT---RY-----AK 235
Cdd:cd12809    44 LIHGGGQTGTNWLNTPDgrpgwasYFLEKGYEVYIVDQPGRGRSPwNPEVGGPLAAST-AETVEQRFTapeRYnlwpqAK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 236 KRN------------------------------------------------VLIGHSYGVSFCTFLAHEYPDLVHKVImi 267
Cdd:cd12809   123 LHTqwpgtgrrgdpifdqfyasqvplltnlaeqealvraagcalldiigpaILITHSQGGPFGWLAADARPDLVKAIV-- 200

                         170
                  ....*....|.
gi 1720428126 268 ngggptALEPS 278
Cdd:cd12809   201 ------AIEPS 205
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 163-261 1.08e-04

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 44.41  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 163 GAQADVVlfFIHGVGGSLAIWKEQLdfF------VRLGYEVVAPDLAGHGASSAPqvaaAYTFYALAE--DM--RAIFTR 232
Cdd:PLN03087  199 KAKEDVL--FIHGFISSSAFWTETL--FpnfsdaAKSTYRLFAVDLLGFGRSPKP----ADSLYTLREhlEMieRSVLER 270

                          90       100
                  ....*....|....*....|....*....
gi 1720428126 233 YAKKRNVLIGHSYGVSFCTFLAHEYPDLV 261
Cdd:PLN03087  271 YKVKSFHIVAHSLGCILALALAVKHPGAV 299
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
169-291 6.02e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 41.11  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 169 VLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAP-----QVAAAYTFYALAEDMRAIFtRYAKKRN----- 238
Cdd:COG0412    31 GVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearALMGALDPELLAADLRAAL-DWLKAQPevdag 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720428126 239 --VLIGHSYGVSFCTFLAHEYPDLVhKVIMINGGGPTALEPSLCSIFNMPTCVLH 291
Cdd:COG0412   110 rvGVVGFCFGGGLALLAAARGPDLA-AAVSFYGGLPADDLLDLAARIKAPVLLLY 163
Esterase_713_like cd12806
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ...
 170-272 2.54e-03

Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains 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. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214005  Cd Length: 261  Bit Score: 39.44  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428126 170 LFFIHGVGGSLAIWKEQ-------LDFFVRLGYEVVAPDLAGHGAS----------SAPQVA-AAYTFYALAEDMRAIFT 231
Cdd:cd12806    51 LLLIHGCGLTGMTWETTpdgrmgwDNYFLRKGYSVYVVDQPGRGRSgwdtqfpvqgQAELWQqMVPDWLGAMPTPNPTVA 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720428126 232 RYAK-----KRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGP 272
Cdd:cd12806   131 ALSKladklDPTVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGC 176
 
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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