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Conserved domains on  [gi|403224993|ref|NP_001258109|]
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sn-1-specific diacylglycerol lipase ABHD11 [Rattus norvegicus]

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;
61-307 1.04e-52

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 173.38  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  61 IVLLHGLFGSKSNFNSLAKALVQRtgRRVLTVDARNHGDSPHSPDASYEAMSQDLQGLLPQLGLVPSVLVGHSMGGKTAM 140
Cdd:PRK10673  19 IVLVHGLFGSLDNLGVLARDLVND--HDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 141 LLALQRPDVVERLVVVDISPAGTTPGSYLGNFiAAMKAVDIPENIPHSRARKLADEQLssvvKEASVRQFLLTNLVEvng 220
Cdd:PRK10673  97 ALTALAPDRIDKLVAIDIAPVDYHVRRHDEIF-AAINAVSEAGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVD--- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 221 rFSWRVNLDALAQQLDKILTFpQQLESYPGSTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNAGHWVHSDKPQDFMD 300
Cdd:PRK10673 169 -GEWRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246


                 ....*..
gi 403224993 301 AVISFLA 307
Cdd:PRK10673 247 AIRRYLN 253
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
61-307 1.04e-52

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 173.38  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  61 IVLLHGLFGSKSNFNSLAKALVQRtgRRVLTVDARNHGDSPHSPDASYEAMSQDLQGLLPQLGLVPSVLVGHSMGGKTAM 140
Cdd:PRK10673  19 IVLVHGLFGSLDNLGVLARDLVND--HDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 141 LLALQRPDVVERLVVVDISPAGTTPGSYLGNFiAAMKAVDIPENIPHSRARKLADEQLssvvKEASVRQFLLTNLVEvng 220
Cdd:PRK10673  97 ALTALAPDRIDKLVAIDIAPVDYHVRRHDEIF-AAINAVSEAGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVD--- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 221 rFSWRVNLDALAQQLDKILTFpQQLESYPGSTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNAGHWVHSDKPQDFMD 300
Cdd:PRK10673 169 -GEWRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246


                 ....*..
gi 403224993 301 AVISFLA 307
Cdd:PRK10673 247 AIRRYLN 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 59-307 5.39e-34

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: 123.57  E-value: 5.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  59 PAIVLLHGLFGSKSNFNSLAKALvqRTGRRVLTVDARNHGDSPHSPDA-SYEAMSQDLQGLLPQLGLVPSVLVGHSMGGK 137
Cdd:COG0596   24 PPVVLLHGLPGSSYEWRPLIPAL--AAGYRVIAPDLRGHGRSDKPAGGyTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 138 TAMLLALQRPDVVERLVVVDispagttpgsylgnfiAAMKAVDIPENIPHSRARKLADeqlssvvkeasvrqflltnLVE 217
Cdd:COG0596  102 VALELAARHPERVAGLVLVD----------------EVLAALAEPLRRPGLAPEALAA-------------------LLR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 218 VNGRFSWRvnlDALAQqldkiLTFPqqlesypgsTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNAGHWVHSDKPQD 297
Cdd:COG0596  147 ALARTDLR---ERLAR-----ITVP---------TLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEA 209

                        250
                 ....*....|
gi 403224993 298 FMDAVISFLA 307
Cdd:COG0596  210 FAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-295 1.14e-23

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: 96.80  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   59 PAIVLLHGLFGSKSNFNSLAKALvQRTGRRVLTVDARNHGDSPHSPDAS---YEAMSQDLQGLLPQLGLVPSVLVGHSMG 135
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  136 GKTAMLLALQRPDVVERLVVVDI----SPAGTTPGSYLGNFIAAMKAVDIPeNIPHSRARKLADEQLSSVVKEASVRQFL 211
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAldppHELDEADRFILALFPGFFDGFVAD-FAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  212 LTNLVEVNGRFSWRVNLDalAQQLDKILTFPQQLESYP-----GSTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNA 286
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLV--TGALLFIETWSTELRAKFlgrldEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDA 236


                  ....*....
gi 403224993  287 GHWVHSDKP 295
Cdd:pfam00561 237 GHFAFLEGP 245
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 126-162 2.07e-03

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: 214007  Cd Length: 309  Bit Score: 39.15  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 403224993 126 PSVLVGHSMGGKTAMLLALQRPDVVERlvVVDISPAG 162
Cdd:cd12808  189 PCIVVAHSQGGGFAFEAARARPDLVRA--VVALEPSG 223
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
61-307 1.04e-52

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 173.38  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  61 IVLLHGLFGSKSNFNSLAKALVQRtgRRVLTVDARNHGDSPHSPDASYEAMSQDLQGLLPQLGLVPSVLVGHSMGGKTAM 140
Cdd:PRK10673  19 IVLVHGLFGSLDNLGVLARDLVND--HDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 141 LLALQRPDVVERLVVVDISPAGTTPGSYLGNFiAAMKAVDIPENIPHSRARKLADEQLssvvKEASVRQFLLTNLVEvng 220
Cdd:PRK10673  97 ALTALAPDRIDKLVAIDIAPVDYHVRRHDEIF-AAINAVSEAGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVD--- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 221 rFSWRVNLDALAQQLDKILTFpQQLESYPGSTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNAGHWVHSDKPQDFMD 300
Cdd:PRK10673 169 -GEWRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246


                 ....*..
gi 403224993 301 AVISFLA 307
Cdd:PRK10673 247 AIRRYLN 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 59-307 5.39e-34

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: 123.57  E-value: 5.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  59 PAIVLLHGLFGSKSNFNSLAKALvqRTGRRVLTVDARNHGDSPHSPDA-SYEAMSQDLQGLLPQLGLVPSVLVGHSMGGK 137
Cdd:COG0596   24 PPVVLLHGLPGSSYEWRPLIPAL--AAGYRVIAPDLRGHGRSDKPAGGyTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 138 TAMLLALQRPDVVERLVVVDispagttpgsylgnfiAAMKAVDIPENIPHSRARKLADeqlssvvkeasvrqflltnLVE 217
Cdd:COG0596  102 VALELAARHPERVAGLVLVD----------------EVLAALAEPLRRPGLAPEALAA-------------------LLR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 218 VNGRFSWRvnlDALAQqldkiLTFPqqlesypgsTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNAGHWVHSDKPQD 297
Cdd:COG0596  147 ALARTDLR---ERLAR-----ITVP---------TLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEA 209

                        250
                 ....*....|
gi 403224993 298 FMDAVISFLA 307
Cdd:COG0596  210 FAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-295 1.14e-23

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: 96.80  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   59 PAIVLLHGLFGSKSNFNSLAKALvQRTGRRVLTVDARNHGDSPHSPDAS---YEAMSQDLQGLLPQLGLVPSVLVGHSMG 135
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  136 GKTAMLLALQRPDVVERLVVVDI----SPAGTTPGSYLGNFIAAMKAVDIPeNIPHSRARKLADEQLSSVVKEASVRQFL 211
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAldppHELDEADRFILALFPGFFDGFVAD-FAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  212 LTNLVEVNGRFSWRVNLDalAQQLDKILTFPQQLESYP-----GSTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNA 286
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLV--TGALLFIETWSTELRAKFlgrldEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDA 236


                  ....*....
gi 403224993  287 GHWVHSDKP 295
Cdd:pfam00561 237 GHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
59-307 2.87e-18

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 81.59  E-value: 2.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  59 PAIVLLHGLFGSKSNFNSLAKALVQRtGRRVLTVDARNHGDSPHSP--DASYEAMSQDLQG---LLPQLGLVPSVLVGHS 133
Cdd:COG2267   29 GTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRghVDSFDDYVDDLRAaldALRARPGLPVVLLGHS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 134 MGGKTAMLLALQRPDVVERLVVvdISPAgttpgsylgnfiaamkavdipeniphsrarkladeqlssvvkeasvrqFLLT 213
Cdd:COG2267  108 MGGLIALLYAARYPDRVAGLVL--LAPA------------------------------------------------YRAD 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 214 NLVEVNGRFSWRVNLDALAQQLDKiltfPqqlesypgsTLFLLGGNSPYVPPSHHSAI-RRLFPQTQIQTVPNAGHWVHS 292
Cdd:COG2267  138 PLLGPSARWLRALRLAEALARIDV----P---------VLVLHGGADRVVPPEAARRLaARLSPDVELVLLPGARHELLN 204

                        250
                 ....*....|....*.
gi 403224993 293 DKPQD-FMDAVISFLA 307
Cdd:COG2267  205 EPAREeVLAAILAWLE 220
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 61-301 2.63e-15

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 73.28  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   61 IVLLHGLFGSKSNFNSLAKALVqrtgrRVLTVDARNHGDSPHsPDASYEAMSQDLQGLLPQLGLVPSVLVGHSMGGKTAM 140
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAAGV-----AVLAPDLPGHGSSSP-PPLDLADLADLAALLDELGAARPVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  141 LLAlqrpdVVERLVVVDISPAGTTPGSYLGNFIAAMKAVDIPENIPHSRARKLADEQLSSVVKEAsvrqflltnlvevng 220
Cdd:pfam12697  75 AAA-----AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADA--------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  221 rfSWRVNLDALAQQLDKILTFPQQLESYPGSTLFLLGGNSPYVPPsHHSAIRRLFPQTQIQTVPNAGHWVHSDkPQDFMD 300
Cdd:pfam12697 135 --EWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPE-LAQRLLAALAGARLVVLPGAGHLPLDD-PEEVAE 210


                  .
gi 403224993  301 A 301
Cdd:pfam12697 211 A 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 54-307 7.00e-15

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 74.21  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  54 GDATLPAIVLLHGLFGSKSNFNSLAKALvqRTGRRVLTVDARNHGDS-PHSPDASYEAMSQDLQGLLPQLGLVPSVLVGH 132
Cdd:PRK14875 127 GEGDGTPVVLIHGFGGDLNNWLFNHAAL--AAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLVGH 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 133 SMGGKTAMLLALQRPDVVERLVVvdISPAGTTP---GSYLGNFIAAmkavdipeniPHSRARKLADEQLssVVKEASV-R 208
Cdd:PRK14875 205 SMGGAVALRLAARAPQRVASLTL--IAPAGLGPeinGDYIDGFVAA----------ESRRELKPVLELL--FADPALVtR 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 209 QFL--LTNLVEVNGRfswRVNLDALAQQLdkiltFP---------QQLESYPGSTLFLLGGNSPYVPPSHHSAirrLFPQ 277
Cdd:PRK14875 271 QMVedLLKYKRLDGV---DDALRALADAL-----FAggrqrvdlrDRLASLAIPVLVIWGEQDRIIPAAHAQG---LPDG 339

                        250       260       270
                 ....*....|....*....|....*....|
gi 403224993 278 TQIQTVPNAGHWVHSDKPQDFMDAVISFLA 307
Cdd:PRK14875 340 VAVHVLPGAGHMPQMEAAADVNRLLAEFLG 369
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
59-306 4.06e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 64.96  E-value: 4.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  59 PAIVLLHGLFGSKSNFNSLAKALVQRtGRRVLTVDARNHGDSP------------HSPDASYEAMSQDlqgllpqlglVP 126
Cdd:COG1647   16 KGVLLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPedllkttwedwlEDVEEAYEILKAG----------YD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 127 SV-LVGHSMGGKTAMLLALQRPDvVERLVVvdISPAGTTPGSYLGNFIAAMKAVDIPENIPHSRARKLADEQLSSVVKEA 205
Cdd:COG1647   85 KViVIGLSMGGLLALLLAARYPD-VAGLVL--LSPALKIDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 206 SVRQflLTNLVevngrfswrvnlDALAQQLDKIlTFPqqlesypgsTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTV-- 283
Cdd:COG1647  162 ALAE--LQRLI------------REVRRDLPKI-TAP---------TLIIQSRKDEVVPPESARYIYERLGSPDKELVwl 217

                        250       260
                 ....*....|....*....|....
gi 403224993 284 PNAGHWVHSDKPQD-FMDAVISFL 306
Cdd:COG1647  218 EDSGHVITLDKDREeVAEEILDFL 241
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
53-307 3.48e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 61.96  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  53 DGDATLPAIVLLHGLFGSKSN-FNSLAKALVQRtGRRVLTVDARNHGDSPHSPdasYEAMSQDLQGLLPQLGLVPSV--- 128
Cdd:COG1506   18 ADGKKYPVVVYVHGGPGSRDDsFLPLAQALASR-GYAVLAPDYRGYGESAGDW---GGDEVDDVLAAIDYLAARPYVdpd 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 129 ---LVGHSMGGKTAMLLALQRPDVVErlVVVDISPAgTTPGSYLGNFIAAMKAVdipENIPHSRARKLAdeqlssvvkea 205
Cdd:COG1506   94 rigIYGHSYGGYMALLAAARHPDRFK--AAVALAGV-SDLRSYYGTTREYTERL---MGGPWEDPEAYA----------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 206 svrqflltnlvevngRFSWRVNLDALaqqldkiltfpqqlesyPGSTLFLLGGNSPYVPPSH----HSAIRRLFPQTQIQ 281
Cdd:COG1506  157 ---------------ARSPLAYADKL-----------------KTPLLLIHGEADDRVPPEQaerlYEALKKAGKPVELL 204

                        250       260
                 ....*....|....*....|....*.
gi 403224993 282 TVPNAGHWVHSDKPQDFMDAVISFLA 307
Cdd:COG1506  205 VYPGEGHGFSGAGAPDYLERILDFLD 230
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 60-294 9.39e-11

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: 60.69  E-value: 9.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   60 AIVLLHGLFGSKSNFNSLAKALVQRtGRRVLTVDARNHGDSP----HSPdaSYEAMSQDLQ----GLLPQLGLVPSVLVG 131
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDtfvdKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  132 HSMGGKTAMLLALQRPDVVERLVVVdiSPAgTTPGSYLGNFIAAMKAVDIPENIPHSRARKLADeqLSSVVKEASVRQFL 211
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILS--APA-LKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLL--PDSLSRDPEVVAAY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  212 LTN-LVEvnGRFSWRVNLDAL-----AQQLDKILTFPqqlesypgsTLFLLGGNSPYVPPshhSAIRRLF-----PQTQI 280
Cdd:pfam12146 158 AADpLVH--GGISARTLYELLdagerLLRRAAAITVP---------LLLLHGGADRVVDP---AGSREFYeragsTDKTL 223

                         250
                  ....*....|....
gi 403224993  281 QTVPNAGHWVHSDK 294
Cdd:pfam12146 224 KLYPGLYHELLNEP 237
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 53-306 5.85e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 58.77  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  53 DGDATLPAIVLLHGLFGSKSNFNSLAKALVQRtGRRVLTVDARNHGDSPHSP--DASYEAmsQDLQGLLPQLGLVPSV-- 128
Cdd:COG1073   32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESEGEPreEGSPER--RDARAAVDYLRTLPGVdp 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 129 ----LVGHSMGGKTAMLLALQRPDVveRLVVVDispagtTPGSYLGNFIAAMKAVDIPENIPhsrarkladeqLSSVVKE 204
Cdd:COG1073  109 erigLLGISLGGGYALNAAATDPRV--KAVILD------SPFTSLEDLAAQRAKEARGAYLP-----------GVPYLPN 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 205 ASVRQFLltnlvevNGRFSwrvnldaLAQQLDKILTfPqqlesypgsTLFLLGGNSPYVPPSHhsaIRRLFPQT----QI 280
Cdd:COG1073  170 VRLASLL-------NDEFD-------PLAKIEKISR-P---------LLFIHGEKDEAVPFYM---SEDLYEAAaepkEL 222

                        250       260
                 ....*....|....*....|....*..
gi 403224993 281 QTVPNAGHWVHSDKPQD-FMDAVISFL 306
Cdd:COG1073  223 LIVPGAGHVDLYDRPEEeYFDKLAEFF 249
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 57-145 3.89e-08

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 53.30  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  57 TLPAIVLLHGLFGSKSNFNSLAKALvqrTGRRVLTVDARNHGDSPHSPDASYEAMSQDLQGLLPQLGLVPSVLVGHSMGG 136
Cdd:PRK11126   1 GLPWLVFLHGLLGSGQDWQPVGEAL---PDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGG 77


                 ....*....
gi 403224993 137 KTAMLLALQ 145
Cdd:PRK11126  78 RIAMYYACQ 86
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 55-154 6.87e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.83  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  55 DATLPAIVLLHGLFGSKSNFNSLAKALVQRtGRRVLTVdarNHGDSPHSPDASYEAMSQDLQGLLPQLGLVPSVLVGHSM 134
Cdd:COG1075    2 AATRYPVVLVHGLGGSAASWAPLAPRLRAA-GYPVYAL---NYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSM 77

                         90       100
                 ....*....|....*....|..
gi 403224993 135 GGKTA--MLLALQRPDVVERLV 154
Cdd:COG1075   78 GGLVAryYLKRLGGAAKVARVV 99
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
53-149 3.93e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.96  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  53 DGDATLPAIVLLHGLFGSKSNFNSLAKALVQRtGRRVLTVDARNHGDSPHSPDASYEAMSQDLQGLLPQL--------GL 124
Cdd:COG0412   24 AGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA-GYVVLAPDLYGRGGPGDDPDEARALMGALDPELLAADlraaldwlKA 102

                         90       100       110
                 ....*....|....*....|....*....|.
gi 403224993 125 VPSV------LVGHSMGGKTAMLLALQRPDV 149
Cdd:COG0412  103 QPEVdagrvgVVGFCFGGGLALLAAARGPDL 133
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
53-161 3.78e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 46.79  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  53 DGDATLPAIVLLHG---LFGSKSNFNSLAKALVQRTGRRVLTVDARnhgdspHSPDASYEAMSQDL-------QGLLPQL 122
Cdd:COG0657    8 GAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDYR------LAPEHPFPAALEDAyaalrwlRANAAEL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 403224993 123 GLVPS--VLVGHSMGGKTAMLLALQRPDVVERLV--VVDISPA 161
Cdd:COG0657   82 GIDPDriAVAGDSAGGHLAAALALRARDRGGPRPaaQVLIYPV 124
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 52-302 6.79e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 44.13  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  52 LDGDATLPAIVLLHGLFGSKS----NFNSLAKALvqrtgrRVLTVDARNHGDSPHsPD------ASYEAMSQDLQGLLPQ 121
Cdd:PLN02894  99 FDSKEDAPTLVMVHGYGASQGfffrNFDALASRF------RVIAIDQLGWGGSSR-PDftckstEETEAWFIDSFEEWRK 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 122 LGLVP-SVLVGHSMGGKTAMLLALQRPDVVERLVVVdiSPAGTTPGS-----YLGNFIAAMKAVDIpeniphsraRKLAD 195
Cdd:PLN02894 172 AKNLSnFILLGHSFGGYVAAKYALKHPEHVQHLILV--GPAGFSSESddkseWLTKFRATWKGAVL---------NHLWE 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 196 eqlSSVVKEASVRQF--LLTNLVE--VNGRFSWRVNLDALAQQLDKILT------------------------------F 241
Cdd:PLN02894 241 ---SNFTPQKIIRGLgpWGPNLVRryTTARFGAHSTGDILSEEESKLLTdyvyhtlaakasgelclkyifsfgafarkpL 317

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 403224993 242 PQQLESYPGSTLFLLGGNSPYVPPSHHSAIRRLFPQTQIQTVPNAGHWVHSDKPQDFMDAV 302
Cdd:PLN02894 318 LESASEWKVPTTFIYGRHDWMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAV 378
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
45-192 1.25e-04

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 42.51  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  45 LPLSYNlldgDATLPAIVLLHGLFGSKSNFnsLAKALVQRTGRR----VLTVDARNHG---DSPHSPDASY--EAM-SQD 114
Cdd:COG0627   24 LPPGYD----GRPLPVLYLLHGLTGTHENW--TRKTGAQRLAAElgviVVMPDGGQASfyvDWTQGPAGHYrwETYlTEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993 115 lqgllpqlglVPSVL---------------VGHSMGGKTAMLLALQRPDVVerLVVVDISPA---------GTTPGSYLG 170
Cdd:COG0627   98 ----------LPPLIeanfpvsadrerraiAGLSMGGHGALTLALRHPDLF--RAVAAFSGIldpsqppwgEKAFDAYFG 165

                        170       180
                 ....*....|....*....|...
gi 403224993 171 NFIAAM-KAVDIPENIPHSRARK 192
Cdd:COG0627  166 PPDRAAwAANDPLALAEKLRAGL 188
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
46-156 3.43e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.41  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  46 PLSYNLLDGDATLPAIVLLHGLFGSKSNF-NSLAKALVQRtGRRVLTVDARNHGDS-PHSP---DASY-EAMSQD----L 115
Cdd:COG4757   19 PLAARLFPPAGPPRAVVLINPATGVPQRFyRPFARYLAER-GFAVLTYDYRGIGLSrPGSLrgfDAGYrDWGELDlpavL 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 403224993 116 QGLLPQLGLVPSVLVGHSMGGKtaMLLALQRPDVVERLVVV 156
Cdd:COG4757   98 DALRARFPGLPLLLVGHSLGGQ--LLGLAPNAERVDRLVTV 136
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 59-256 7.50e-04

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: 40.06  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   59 PAIVLLHGLFGSKSNFNSLAKALvqRTGRRVLTVDARNHGdSPHSPDASYEAM-SQDLQGLLPQLGLVPSVLVGHSMGGK 137
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRL--PPPAEVLAVQYPGRG-RGEPPLNSIEALaDEYAEALRQIQPEGPYALFGHSMGGM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  138 TAMLLALQ---RPDVVERLVVVDISPAGTT--PGSY---LGNFIAAMKavDIPENIPHSRARKLADEQLSSVVKEA---- 205
Cdd:pfam00975  78 LAFEVARRlerQGEAVRSLFLSDASAPHTVryEASRapdDDEVVAEFT--DEGGTPEELLEDEELLSMLLPALRADyral 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 403224993  206 ---SVRQFLLTNLVEVNGRFSWRVNLDALAQQLDKILTFPQQLESYPGSTLFLL 256
Cdd:pfam00975 156 esySCPPLDAQSATLFYGSDDPLHDADDLAEWVRDHTPGEFDVHVFDGDHFYLI 209
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
59-160 1.00e-03

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 40.13  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  59 PAIVLLHGLFGS-KSNF-NSLAKALVQRtGRRVLTVDARNHGDSPH-SPDASYEAMSQDLQGL----LPQLGLVPSVLVG 131
Cdd:COG0429   62 PLVVLLHGLEGSsDSHYaRGLARALYAR-GWDVVRLNFRGCGGEPNlLPRLYHSGDTEDLVWVlahlRARYPYAPLYAVG 140

                         90       100       110
                 ....*....|....*....|....*....|.
gi 403224993 132 HSMGGKTAMLLALQRPDVVERL--VVVdISP 160
Cdd:COG0429  141 FSLGGNLLLKYLGEQGDDAPPLkaAVA-VSP 170
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 126-162 2.07e-03

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: 214007  Cd Length: 309  Bit Score: 39.15  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 403224993 126 PSVLVGHSMGGKTAMLLALQRPDVVERlvVVDISPAG 162
Cdd:cd12808  189 PCIVVAHSQGGGFAFEAARARPDLVRA--VVALEPSG 223
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 126-162 2.58e-03

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: 38.75  E-value: 2.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 403224993 126 PSVLVGHSMGGKTAMLLALQRPDVVERLVVVDisPAG 162
Cdd:cd12809  172 PAILITHSQGGPFGWLAADARPDLVKAIVAIE--PSG 206
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 61-160 2.84e-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: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   61 IVLLHGLFGSKSNFNSLAKALVQRTgrRVLTVDARNHGDSP---------HSPDASYEAMSQDLQGLLPQLGLVPSVLVG 131
Cdd:PLN02980 1374 VLFLHGFLGTGEDWIPIMKAISGSA--RCISIDLPGHGGSKiqnhaketqTEPTLSVELVADLLYKLIEHITPGKVTLVG 1451

                          90       100
                  ....*....|....*....|....*....
gi 403224993  132 HSMGGKTAMLLALQRPDVVERLVVVDISP 160
Cdd:PLN02980 1452 YSMGARIALYMALRFSDKIEGAVIISGSP 1480
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 5-205 3.79e-03

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: 38.92  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993   5 ARAWRVPRGTIGASSPRSSAVPVTFSSSRSSGQGNADPRPLPLsynLLDGDATLPAIVLLHGLFGSKSNFNSLAKALvqR 84
Cdd:COG3319  551 LLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLV---PLRAGGSGPPLFCVHPAGGNVLCYRPLARAL--G 625

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  85 TGRRVLTVDARNHgDSPHSPDASYEAMSQDLQGL-LPQLGLVPSVLVGHSMGGKTAMLLALQ---RPDVVERLVVVD--- 157
Cdd:COG3319  626 PDRPVYGLQAPGL-DGGEPPPASVEEMAARYVEAiRAVQPEGPYHLLGWSFGGLVAYEMARQleaQGEEVALLVLLDsya 704

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 403224993 158 -ISPAGTTPGSYLGNFIAAMKAVDIPENIPHSRARKLADEQLSSVVKEA 205
Cdd:COG3319  705 pGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERL 753
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
 128-290 7.57e-03

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


Pssm-ID: 370901  Cd Length: 261  Bit Score: 37.27  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  128 VLVGHSMGGKTAMLLALQRPD-VVERLV-----VVDI--SPAGT--TPGSYLGNFIAAMKA--VDIPENIPHSRARKLAD 195
Cdd:pfam10230  86 ILIGHSIGAYIALEVLKRLSErGIIKCVllfptIEDMarSPNGRilTRLLCYIPFLALVAGflLRVFKLLPESVKSLLIR 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403224993  196 EQLSSVvkeASVRQFLLTNLVEVNGRFSWRVNLDALAQQLDKILTFPQQ--LESYPGSTLFLLGGNSPYVPPSHHSAIRR 273
Cdd:pfam10230 166 KVMGGM---SSPPHAVQTTLKFLLNPHCVRNALHMARDEMREVREDDDEdfIKANQERLWFYYGTTDHWVPVSTRDELKE 242

                         170
                  ....*....|....*....
gi 403224993  274 LFPQTQIQ-TVPNAGH-WV 290
Cdd:pfam10230 243 LYPDGDLVvDEDGIPHaFV 261
 
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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