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Conserved domains on  [gi|2462565424|ref|XP_054177000|]
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hormone-sensitive lipase isoform X4 [Homo sapiens]

Protein Classification

hormone-sensitive lipase( domain architecture ID 10533829)

hormone-sensitive lipase displays broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters; belongs to the alpha/beta hydrolase superfamily

EC:  3.1.1.-
Gene Symbol:  LIPE
Gene Ontology:  GO:0016787|GO:0016298

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
69-377 4.29e-163

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


:

Pssm-ID: 461882  Cd Length: 306  Bit Score: 473.28  E-value: 4.29e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424  69 MTQSLVTLAEDNIAFFSSqGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAH 148
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 149 LLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDeGLTADFLREYVTLHKGCFY 228
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 229 GRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNIT 308
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565424 309 EMEVLSSLANMASATVRVSRLLSLPPEAFEMPlTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQD 377
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
409-713 8.93e-31

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam07859:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 208  Bit Score: 120.01  E-value: 8.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 409 IVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAKTEDhsnsdqka 488
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 489 LGMMGlvrrDTAlllrdfrlGASswlnsflelsgrksqkmsepIAepmrrsvseAALAQPQGPLGTDSLKNLTLrdlslr 568
Cdd:pfam07859  73 IAVAG----DSA--------GGN--------------------LA---------AAVALRARDEGLPKPAGQVL------ 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 569 gnsetssdtpemslsaetLSPSTpsDVNFLLPPEDAGEEAEAKnELSPMDRGLGVRAAFPEgfHPRRssqgatqmplyss 648
Cdd:pfam07859 106 ------------------IYPGT--DLRTESPSYLAREFADGP-LLTRAAMDWFWRLYLPG--ADRD------------- 149
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462565424 649 pivkNPFMSPLLAPDsmLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFL 713
Cdd:pfam07859 150 ----DPLASPLFASD--LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
69-377 4.29e-163

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 473.28  E-value: 4.29e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424  69 MTQSLVTLAEDNIAFFSSqGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAH 148
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 149 LLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDeGLTADFLREYVTLHKGCFY 228
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 229 GRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNIT 308
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565424 309 EMEVLSSLANMASATVRVSRLLSLPPEAFEMPlTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQD 377
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
409-713 8.93e-31

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 120.01  E-value: 8.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 409 IVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAKTEDhsnsdqka 488
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 489 LGMMGlvrrDTAlllrdfrlGASswlnsflelsgrksqkmsepIAepmrrsvseAALAQPQGPLGTDSLKNLTLrdlslr 568
Cdd:pfam07859  73 IAVAG----DSA--------GGN--------------------LA---------AAVALRARDEGLPKPAGQVL------ 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 569 gnsetssdtpemslsaetLSPSTpsDVNFLLPPEDAGEEAEAKnELSPMDRGLGVRAAFPEgfHPRRssqgatqmplyss 648
Cdd:pfam07859 106 ------------------IYPGT--DLRTESPSYLAREFADGP-LLTRAAMDWFWRLYLPG--ADRD------------- 149
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462565424 649 pivkNPFMSPLLAPDsmLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFL 713
Cdd:pfam07859 150 ----DPLASPLFASD--LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
398-737 3.47e-25

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 103.80  E-value: 3.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 398 RPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAk 477
Cdd:COG0657     5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGI- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 478 tedhsnsDQKALGMMGlvrrDTAlllrdfrlGAsswlnsflelsgrksqkmsepiaepmrrsvseaalaqpqgplgtdsl 557
Cdd:COG0657    84 -------DPDRIAVAG----DSA--------GG----------------------------------------------- 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 558 kNLTLrdlslrgnsetssdtpemslsaetlspstpsdvnfllppedageeaeaknelspmdrGLGVRAAFPEGFHPRRss 637
Cdd:COG0657    98 -HLAA---------------------------------------------------------ALALRARDRGGPRPAA-- 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 638 qgatQMPLYssPIVkNPFMSPLLAPdsmLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFLtLAA 717
Cdd:COG0657   118 ----QVLIY--PVL-DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFG-LLA 186
                         330       340
                  ....*....|....*....|
gi 2462565424 718 LCRETRQAAELCVERIRLVL 737
Cdd:COG0657   187 GLPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
398-713 2.40e-15

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 77.84  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 398 RPQqaPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAK 477
Cdd:PRK10162   75 YPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGIN 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 478 TEDHSNSDQKALGMMGLVrrdTALLLRDFRLGASS------WLNSFlelsgrksqkmsepiaePMRRSVSEAALAQPqgp 551
Cdd:PRK10162  153 MSRIGFAGDSAGAMLALA---SALWLRDKQIDCGKvagvllWYGLY-----------------GLRDSVSRRLLGGV--- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 552 lgtdsLKNLTLRDLSLRgnsetssdtpemslsaetlspstpsdvnfllppedagEEAEAKNelsPMDRglgvraafpegf 631
Cdd:PRK10162  210 -----WDGLTQQDLQMY-------------------------------------EEAYLSN---DADR------------ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 632 hprrssqgatqmplysspivKNPFMSPLLapDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHG 711
Cdd:PRK10162  233 --------------------ESPYYCLFN--NDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHA 290

                  ..
gi 2462565424 712 FL 713
Cdd:PRK10162  291 FL 292
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
69-377 4.29e-163

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 473.28  E-value: 4.29e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424  69 MTQSLVTLAEDNIAFFSSqGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAH 148
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 149 LLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDeGLTADFLREYVTLHKGCFY 228
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 229 GRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNIT 308
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565424 309 EMEVLSSLANMASATVRVSRLLSLPPEAFEMPlTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQD 377
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
409-713 8.93e-31

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 120.01  E-value: 8.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 409 IVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAKTEDhsnsdqka 488
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 489 LGMMGlvrrDTAlllrdfrlGASswlnsflelsgrksqkmsepIAepmrrsvseAALAQPQGPLGTDSLKNLTLrdlslr 568
Cdd:pfam07859  73 IAVAG----DSA--------GGN--------------------LA---------AAVALRARDEGLPKPAGQVL------ 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 569 gnsetssdtpemslsaetLSPSTpsDVNFLLPPEDAGEEAEAKnELSPMDRGLGVRAAFPEgfHPRRssqgatqmplyss 648
Cdd:pfam07859 106 ------------------IYPGT--DLRTESPSYLAREFADGP-LLTRAAMDWFWRLYLPG--ADRD------------- 149
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462565424 649 pivkNPFMSPLLAPDsmLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFL 713
Cdd:pfam07859 150 ----DPLASPLFASD--LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
398-737 3.47e-25

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 103.80  E-value: 3.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 398 RPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAk 477
Cdd:COG0657     5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGI- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 478 tedhsnsDQKALGMMGlvrrDTAlllrdfrlGAsswlnsflelsgrksqkmsepiaepmrrsvseaalaqpqgplgtdsl 557
Cdd:COG0657    84 -------DPDRIAVAG----DSA--------GG----------------------------------------------- 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 558 kNLTLrdlslrgnsetssdtpemslsaetlspstpsdvnfllppedageeaeaknelspmdrGLGVRAAFPEGFHPRRss 637
Cdd:COG0657    98 -HLAA---------------------------------------------------------ALALRARDRGGPRPAA-- 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 638 qgatQMPLYssPIVkNPFMSPLLAPdsmLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFLtLAA 717
Cdd:COG0657   118 ----QVLIY--PVL-DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFG-LLA 186
                         330       340
                  ....*....|....*....|
gi 2462565424 718 LCRETRQAAELCVERIRLVL 737
Cdd:COG0657   187 GLPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
398-713 2.40e-15

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 77.84  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 398 RPQqaPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGAK 477
Cdd:PRK10162   75 YPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGIN 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 478 TEDHSNSDQKALGMMGLVrrdTALLLRDFRLGASS------WLNSFlelsgrksqkmsepiaePMRRSVSEAALAQPqgp 551
Cdd:PRK10162  153 MSRIGFAGDSAGAMLALA---SALWLRDKQIDCGKvagvllWYGLY-----------------GLRDSVSRRLLGGV--- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 552 lgtdsLKNLTLRDLSLRgnsetssdtpemslsaetlspstpsdvnfllppedagEEAEAKNelsPMDRglgvraafpegf 631
Cdd:PRK10162  210 -----WDGLTQQDLQMY-------------------------------------EEAYLSN---DADR------------ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565424 632 hprrssqgatqmplysspivKNPFMSPLLapDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHG 711
Cdd:PRK10162  233 --------------------ESPYYCLFN--NDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHA 290

                  ..
gi 2462565424 712 FL 713
Cdd:PRK10162  291 FL 292
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
399-460 1.61e-05

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 46.79  E-value: 1.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462565424 399 PQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQEL---GAPIISIDYSLAPEAPFPRALEEC 460
Cdd:pfam20434   6 PKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALlkaGYAVASINYRLSTDAKFPAQIQDV 70
 
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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