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Conserved domains on  [gi|254281213|ref|NP_001122119|]
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sn-1-specific diacylglycerol lipase ABHD11 [Xenopus tropicalis]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 1001822)

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

CATH:  3.40.50.1820
Gene Ontology:  GO:0016787
PubMed:  12369917|15381402|1409539
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 super family cl30399
esterase;
69-318 7.46e-58

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 186.86  E-value: 7.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  69 PPLVLLHGLFGSKSNFQSIARALVrkTGRKVLTLDARNHGCSPHDDIMTYPAMSADVCQILHKLQITSCVLIGHSMGGKT 148
Cdd:PRK10673  17 SPIVLVHGLFGSLDNLGVLARDLV--NDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 149 AMTVALQEPKLVERFVSVDISPAATvpQTGFPHYI-AAMQKVHLEGKIPRSTARRLAEEQLsstvKEASIRQFLLTNLVQ 227
Cdd:PRK10673  95 VMALTALAPDRIDKLVAIDIAPVDY--HVRRHDEIfAAINAVSEAGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 228 EngtfKWRVNLEVISQHLQDLLDFPEFqEPYPGPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAGHWVHADKTHD 307
Cdd:PRK10673 169 G----EWRFNVPVLWDQYPHIVGWEKI-PAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDA 243

                        250
                 ....*....|.
gi 254281213 308 FLNSICNFVES 318
Cdd:PRK10673 244 VLRAIRRYLND 254
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
69-318 7.46e-58

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 186.86  E-value: 7.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  69 PPLVLLHGLFGSKSNFQSIARALVrkTGRKVLTLDARNHGCSPHDDIMTYPAMSADVCQILHKLQITSCVLIGHSMGGKT 148
Cdd:PRK10673  17 SPIVLVHGLFGSLDNLGVLARDLV--NDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 149 AMTVALQEPKLVERFVSVDISPAATvpQTGFPHYI-AAMQKVHLEGKIPRSTARRLAEEQLsstvKEASIRQFLLTNLVQ 227
Cdd:PRK10673  95 VMALTALAPDRIDKLVAIDIAPVDY--HVRRHDEIfAAINAVSEAGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 228 EngtfKWRVNLEVISQHLQDLLDFPEFqEPYPGPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAGHWVHADKTHD 307
Cdd:PRK10673 169 G----EWRFNVPVLWDQYPHIVGWEKI-PAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDA 243

                        250
                 ....*....|.
gi 254281213 308 FLNSICNFVES 318
Cdd:PRK10673 244 VLRAIRRYLND 254
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-319 1.45e-31

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: 117.41  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  68 GPPLVLLHGLFGSKSNFQSIARALVRktGRKVLTLDARNHGCSPH-DDIMTYPAMSADVCQILHKLQITSCVLIGHSMGG 146
Cdd:COG0596   23 GPPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 147 KTAMTVALQEPKLVERFVSVDispaatvpqtgfphyiAAMQKVHLEGKIPRSTARRLAEeqlsstvkeasirqflltnLV 226
Cdd:COG0596  101 MVALELAARHPERVAGLVLVD----------------EVLAALAEPLRRPGLAPEALAA-------------------LL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 227 QENGTFKWRVNLEVISQhlqdlldfpefqepypgPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAGHWVHADKTH 306
Cdd:COG0596  146 RALARTDLRERLARITV-----------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPE 208

                        250
                 ....*....|...
gi 254281213 307 DFLNSICNFVESA 319
Cdd:COG0596  209 AFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-305 1.19e-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: 107.98  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213   69 PPLVLLHGLFGSKSNFQSIARALVRKtGRKVLTLDARNHGCS---PHDDIMTYPAMSADVCQILHKLQITSCVLIGHSMG 145
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSsrpKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  146 GKTAMTVALQEPKLVERFVSVDISPAATVPQTGFPHyiAAMQKVHLEGKIPRSTARRLAEEQLSSTVKEASIRQFLLTNL 225
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEADRF--ILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  226 VQENGTFK---WRVNLEVISQHLQDLLDFPEFQEPYP-----GPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAG 297
Cdd:pfam00561 158 PLLNKRFPsgdYALAKSLVTGALLFIETWSTELRAKFlgrldEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237


                  ....*...
gi 254281213  298 HWVHADKT 305
Cdd:pfam00561 238 HFAFLEGP 245
Esterase_713 cd12807
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ...
 117-204 1.69e-03

Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It 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: 214006  Cd Length: 315  Bit Score: 39.61  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 117 TYPAMS--ADvcqilhklQITSCVLIGHSMGGKTAMTVALQEPKLVERFVSVDI--SPAATVPQtgfphyIAAMQKV--- 189
Cdd:cd12807  177 TPNALAalAD--------KLGGAVLLGHSQSGPFPLEAALLRPAGVKGIVSVEPgcCPAPTADQ------IKTLAKIpil 242

                         90       100
                 ....*....|....*....|
gi 254281213 190 -----HLEGKIPRSTARRLA 204
Cdd:cd12807  243 vvfgdHLDAASGPTWQQRLQ 262
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
69-318 7.46e-58

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 186.86  E-value: 7.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  69 PPLVLLHGLFGSKSNFQSIARALVrkTGRKVLTLDARNHGCSPHDDIMTYPAMSADVCQILHKLQITSCVLIGHSMGGKT 148
Cdd:PRK10673  17 SPIVLVHGLFGSLDNLGVLARDLV--NDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 149 AMTVALQEPKLVERFVSVDISPAATvpQTGFPHYI-AAMQKVHLEGKIPRSTARRLAEEQLsstvKEASIRQFLLTNLVQ 227
Cdd:PRK10673  95 VMALTALAPDRIDKLVAIDIAPVDY--HVRRHDEIfAAINAVSEAGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 228 EngtfKWRVNLEVISQHLQDLLDFPEFqEPYPGPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAGHWVHADKTHD 307
Cdd:PRK10673 169 G----EWRFNVPVLWDQYPHIVGWEKI-PAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDA 243

                        250
                 ....*....|.
gi 254281213 308 FLNSICNFVES 318
Cdd:PRK10673 244 VLRAIRRYLND 254
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-319 1.45e-31

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: 117.41  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  68 GPPLVLLHGLFGSKSNFQSIARALVRktGRKVLTLDARNHGCSPH-DDIMTYPAMSADVCQILHKLQITSCVLIGHSMGG 146
Cdd:COG0596   23 GPPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 147 KTAMTVALQEPKLVERFVSVDispaatvpqtgfphyiAAMQKVHLEGKIPRSTARRLAEeqlsstvkeasirqflltnLV 226
Cdd:COG0596  101 MVALELAARHPERVAGLVLVD----------------EVLAALAEPLRRPGLAPEALAA-------------------LL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 227 QENGTFKWRVNLEVISQhlqdlldfpefqepypgPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAGHWVHADKTH 306
Cdd:COG0596  146 RALARTDLRERLARITV-----------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPE 208

                        250
                 ....*....|...
gi 254281213 307 DFLNSICNFVESA 319
Cdd:COG0596  209 AFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-305 1.19e-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: 107.98  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213   69 PPLVLLHGLFGSKSNFQSIARALVRKtGRKVLTLDARNHGCS---PHDDIMTYPAMSADVCQILHKLQITSCVLIGHSMG 145
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSsrpKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  146 GKTAMTVALQEPKLVERFVSVDISPAATVPQTGFPHyiAAMQKVHLEGKIPRSTARRLAEEQLSSTVKEASIRQFLLTNL 225
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEADRF--ILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  226 VQENGTFK---WRVNLEVISQHLQDLLDFPEFQEPYP-----GPALFLGGANSPYISSENYPEIERLFPCANVEYIFGAG 297
Cdd:pfam00561 158 PLLNKRFPsgdYALAKSLVTGALLFIETWSTELRAKFlgrldEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237


                  ....*...
gi 254281213  298 HWVHADKT 305
Cdd:pfam00561 238 HFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
65-187 1.71e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 74.27  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  65 SAPGPPLVLLHGLFGSKSNFQSIARALVRKtGRKVLTLDARNHGCS--PHDDIMTYPAMSADVCQILHKLQI---TSCVL 139
Cdd:COG2267   25 GSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSdgPRGHVDSFDDYVDDLRAALDALRArpgLPVVL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 254281213 140 IGHSMGGKTAMTVALQEPKLVERFVSvdISPA-ATVPQTGFP-HYIAAMQ 187
Cdd:COG2267  104 LGHSMGGLIALLYAARYPDRVAGLVL--LAPAyRADPLLGPSaRWLRALR 151
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 64-319 3.69e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 69.20  E-value: 3.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  64 GSAPGPPLVLLHGLFGSKSNFQSIARALVRktGRKVLTLDARNHGCSPHD-DIMTYPAMSADVCQILHKLQITSCVLIGH 142
Cdd:PRK14875 127 GEGDGTPVVLIHGFGGDLNNWLFNHAALAA--GRPVIALDLPGHGASSKAvGAGSLDELAAAVLAFLDALGIERAHLVGH 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 143 SMGGKTAMTVALQEPKLVeRFVSVdISPAATVPQ--TGFphyiaamqkvhLEGKIPRSTARRLA---------EEQLSST 211
Cdd:PRK14875 205 SMGGAVALRLAARAPQRV-ASLTL-IAPAGLGPEinGDY-----------IDGFVAAESRRELKpvlellfadPALVTRQ 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 212 VKEASIRQFLLtNLVQEngtfkwrvNLEVISQHL-------QDLLDfpEFQEpYPGPALFLGGANSPYISSENypeIERL 284
Cdd:PRK14875 272 MVEDLLKYKRL-DGVDD--------ALRALADALfaggrqrVDLRD--RLAS-LAIPVLVIWGEQDRIIPAAH---AQGL 336

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 254281213 285 FPCANVEYIFGAGHWVHADKTHDFLNSICNFVESA 319
Cdd:PRK14875 337 PDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 71-303 4.83e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 61.34  E-value: 4.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213   71 LVLLHGLFGSKSNFQSIARALVRktgrkVLTLDARNHGCSPHDDImTYPAMsADVCQILHKLQITS-CVLIGHSMGGKTA 149
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAAGVA-----VLAPDLPGHGSSSPPPL-DLADL-ADLAALLDELGAARpVVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  150 MTVAlqepkLVERFVSVDISPAATVPQTGFPHYIAAMQKVHLEGKIPRSTARRLAEEQLSSTVKEAsirqflltnlvqen 229
Cdd:pfam12697  74 LAAA-----AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADA-------------- 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254281213  230 gtfKWRVNLEVISQHLQDLLDFPEFQEPYPGPALFLGGANSPYISSEnYPEIERLFPCANVEYIFGAGHWVHAD 303
Cdd:pfam12697 135 ---EWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPEL-AQRLLAALAGARLVVLPGAGHLPLDD 204
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 64-265 2.04e-10

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 61.64  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  64 GSAPGPPLVLLHGLFGSKSNFQSIARALvrKTGRKVLTLDAR--NHGCSPHDDImtyPAMSADVCQILHKLQITS-CVLI 140
Cdd:COG3319  597 AGGSGPPLFCVHPAGGNVLCYRPLARAL--GPDRPVYGLQAPglDGGEPPPASV---EEMAARYVEAIRAVQPEGpYHLL 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 141 GHSMGGKTAMTVALQ-----EPklVERFVSVDISPAATVPQTGFPHYIAAMQKVHLEGK---IPRSTARRLAEEQLSSTV 212
Cdd:COG3319  672 GWSFGGLVAYEMARQleaqgEE--VALLVLLDSYAPGALARLDEAELLAALLRDLARGVdlpLDAEELRALDPEERLARL 749

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254281213 213 KEASIRQFLLTNLVQENgtfkWRVNLEVISQHLQDLLDF-PefqEPYPGPALFL 265
Cdd:COG3319  750 LERLREAGLPAGLDAER----LRRLLRVFRANLRALRRYrP---RPYDGPVLLF 796
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 68-155 5.52e-10

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 58.70  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  68 GPPLVLLHGLFGSKSNFQSIARALvrkTGRKVLTLDARNHGCSPHDDIMTYPAMSADVCQILHKLQITSCVLIGHSMGGK 147
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQPVGEAL---PDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGR 78


                 ....*...
gi 254281213 148 TAMTVALQ 155
Cdd:PRK11126  79 IAMYYACQ 86
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
61-318 2.99e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 56.49  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  61 LYDGSAPGppLVLLHGLFGSKSNFQSIARALVRKtGRKVLTLDARNHGCSPHDDI-MTYPAMSADVCQILHKLQiTSC-- 137
Cdd:COG1647   10 FLEGGRKG--VLLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPEDLLkTTWEDWLEDVEEAYEILK-AGYdk 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 138 -VLIGHSMGGKTAMTVALQEPKlVERFVSvdISPAATVPQTGFP-----HYIAAMQKvhlegKIPRSTARRLAEEQLSST 211
Cdd:COG1647   86 vIVIGLSMGGLLALLLAARYPD-VAGLVL--LSPALKIDDPSAPllpllKYLARSLR-----GIGSDIEDPEVAEYAYDR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 212 VKEASIRQflLTNLVQEngtfkWRVNLEVISQhlqdlldfpefqepypgPALFLGGANSPYISSENYPEIERLFPCANVE 291
Cdd:COG1647  158 TPLRALAE--LQRLIRE-----VRRDLPKITA-----------------PTLIIQSRKDEVVPPESARYIYERLGSPDKE 213

                        250       260       270
                 ....*....|....*....|....*....|
gi 254281213 292 YIF--GAGHWVHADKTHDFL-NSICNFVES 318
Cdd:COG1647  214 LVWleDSGHVITLDKDREEVaEEILDFLER 243
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 66-166 6.66e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 52.91  E-value: 6.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  66 APGPPLVLLHGLFGSKSNFQSIARALvRKTGRKVLTLDarnhgcsphddimtYPAMSADVCQILHKL--QITSC------ 137
Cdd:COG1075    3 ATRYPVVLVHGLGGSAASWAPLAPRL-RAAGYPVYALN--------------YPSTNGSIEDSAEQLaaFVDAVlaatga 67

                         90       100       110
                 ....*....|....*....|....*....|....
gi 254281213 138 ---VLIGHSMGGKTAMTVA--LQEPKLVERFVSV 166
Cdd:COG1075   68 ekvDLVGHSMGGLVARYYLkrLGGAAKVARVVTL 101
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 71-171 4.06e-08

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: 52.99  E-value: 4.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213   71 LVLLHGLFGSKSNFQSIARALVRKtGRKVLTLDARNHGCSP--HDDIMTYPAMSADVCQILHKLQ----ITSCVLIGHSM 144
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRSDgkRGHVPSFDDYVDDLDTFVDKIReehpGLPLFLLGHSM 85

                          90       100
                  ....*....|....*....|....*..
gi 254281213  145 GGKTAMTVALQEPKLVERFVSVdiSPA 171
Cdd:pfam12146  86 GGLIAALYALRYPDKVDGLILS--APA 110
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 69-191 2.61e-07

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 50.46  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213   69 PPLVLLHGLFGSKSNFQSIARALVRKTGRKVLTLDARNHGCSPHDDImtyPAMSADVCQILHKLQ-ITSCVLIGHSMGGK 147
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSI---EALADEYAEALRQIQpEGPYALFGHSMGGM 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 254281213  148 TAMTVALQepkLVER-------FVSvDISPAATVPQTGfPHYIAAMQKVHL 191
Cdd:pfam00975  78 LAFEVARR---LERQgeavrslFLS-DASAPHTVRYEA-SRAPDDDEVVAE 123
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
60-171 6.80e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 46.02  E-value: 6.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  60 DLY---DGSAPGPPLVLLHG---LFGSKSNFQSIARALVRKTGRKVLTLD---ARNHgcsphddimTYPAMSADVCQILH 130
Cdd:COG0657    2 DVYrpaGAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDyrlAPEH---------PFPAALEDAYAALR 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254281213 131 KL------------QItscVLIGHSMGGKTAMTVALQ-----EPKLveRFVsVDISPA 171
Cdd:COG0657   73 WLranaaelgidpdRI---AVAGDSAGGHLAAALALRardrgGPRP--AAQ-VLIYPV 124
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
55-166 1.15e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.78  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  55 VDLSYDLY--DGSAPGPPLVLLHGLFGSKSN-FQSIARALVRKtGRKVLTLDARNHGCSPHDdimTYPAMSADVCQILHK 131
Cdd:COG1506    8 TTLPGWLYlpADGKKYPVVVYVHGGPGSRDDsFLPLAQALASR-GYAVLAPDYRGYGESAGD---WGGDEVDDVLAAIDY 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 254281213 132 LQITSCV------LIGHSMGGKTAMTVALQEPKLVERFVSV 166
Cdd:COG1506   84 LAARPYVdpdrigIYGHSYGGYMALLAAARHPDRFKAAVAL 124
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
63-159 6.41e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.42  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  63 DGSAPGPPLVLLHGLFGSKSNFQSIARALVRKtGRKVLTLD--ARNHGCSPHDDIMTY------PAMSADVCQILHKLQ- 133
Cdd:COG0412   24 AGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA-GYVVLAPDlyGRGGPGDDPDEARALmgaldpELLAADLRAALDWLKa 102

                         90       100       110
                 ....*....|....*....|....*....|.
gi 254281213 134 ----ITSCV-LIGHSMGGKTAMTVALQEPKL 159
Cdd:COG0412  103 qpevDAGRVgVVGFCFGGGLALLAAARGPDL 133
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 55-157 9.55e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 42.98  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213  55 VDLSYDLY---DGSAPGPPLVLLHGLFGSKSNFQSIARALVRKtGRKVLTLDARNHGCS---PHDdiMTYPAMsADVCQI 128
Cdd:COG1073   21 IKLAGDLYlpaGASKKYPAVVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESegePRE--EGSPER-RDARAA 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 254281213 129 LHKL---------QItscVLIGHSMGGKTAMTVALQEP 157
Cdd:COG1073   97 VDYLrtlpgvdpeRI---GLLGISLGGGYALNAAATDP 131
Esterase_713 cd12807
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ...
 117-204 1.69e-03

Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It 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: 214006  Cd Length: 315  Bit Score: 39.61  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213 117 TYPAMS--ADvcqilhklQITSCVLIGHSMGGKTAMTVALQEPKLVERFVSVDI--SPAATVPQtgfphyIAAMQKV--- 189
Cdd:cd12807  177 TPNALAalAD--------KLGGAVLLGHSQSGPFPLEAALLRPAGVKGIVSVEPgcCPAPTADQ------IKTLAKIpil 242

                         90       100
                 ....*....|....*....|
gi 254281213 190 -----HLEGKIPRSTARRLA 204
Cdd:cd12807  243 vvfgdHLDAASGPTWQQRLQ 262
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 72-170 2.75e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 39.45  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281213   72 VLLHGLFGSKSNFQSIARALvrKTGRKVLTLDARNHGCS-----PHDDImTYPAMSAD-VCQILHKL--QIT--SCVLIG 141
Cdd:PLN02980 1375 LFLHGFLGTGEDWIPIMKAI--SGSARCISIDLPGHGGSkiqnhAKETQ-TEPTLSVElVADLLYKLieHITpgKVTLVG 1451

                          90       100
                  ....*....|....*....|....*....
gi 254281213  142 HSMGGKTAMTVALQEPKLVERFVSVDISP 170
Cdd:PLN02980 1452 YSMGARIALYMALRFSDKIEGAVIISGSP 1480
 
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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