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Conserved domains on  [gi|115533410|ref|NP_001041228|]
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Hormone-sensitive lipase [Caenorhabditis elegans]

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

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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 ...
60-365 2.22e-119

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: 366.19  E-value: 2.22e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410   60 ILELIVQMCSDNATHFEKLAQSGANgyneRMPVVQTALQTAIETLKGNIKKLQEVAPKYDYDEKTPGNGYRSLICICDTT 139
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEGDSSENGQ----RLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  140 LLHVVSLQKAVFEQRGYLIFRISHFCKELEAYATVIDYLNkfipLCLETERNMR-----GSLFPPLDGnyeTYQEILRVM 214
Cdd:pfam06350  77 LLHIIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLR----ACLQHLQTLLswsepGDLFPSEDH---SSEELLREY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  215 EKLDSSVFFGRPIGFQFSPSINKIFRIIGVVLATYSLSWEKGHGAIG----SLINTGRFFLSPEQRAERIIKVTKEADID 290
Cdd:pfam06350 150 ETINQYCFYGRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGraasSLFTSGKYALDPELRARRIVNITQNADVD 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533410  291 FCKGFWNL--SELSNNMPKFFCPNMALNELREIPLDgAIPMEG-KSGEMVMVPEPSAHTGPRPVQYRILSTVHREKMS 365
Cdd:pfam06350 230 FCKAFWNLteSELLSSLPSIVSPSVAVNRVISIPPE-PLTLPLsDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
380-487 4.17e-29

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: 115.39  E-value: 4.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  380 VLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIVMVGDSA 459
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100
                  ....*....|....*....|....*...
gi 115533410  460 GGNLIMSVNLRLIQLNIKRqPDGLVLCY 487
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPK-PAGQVLIY 107
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
850-912 2.25e-08

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: 55.29  E-value: 2.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533410  850 RDPLISPMYAdnETMCQLPPCYFMACHMDPLLDDTISFAGKLRDAGGKVMSVdLLSSVPHGFL 912
Cdd:pfam07859 149 DDPLASPLFA--SDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELI-EYPGMPHGFH 208
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
60-365 2.22e-119

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: 366.19  E-value: 2.22e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410   60 ILELIVQMCSDNATHFEKLAQSGANgyneRMPVVQTALQTAIETLKGNIKKLQEVAPKYDYDEKTPGNGYRSLICICDTT 139
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEGDSSENGQ----RLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  140 LLHVVSLQKAVFEQRGYLIFRISHFCKELEAYATVIDYLNkfipLCLETERNMR-----GSLFPPLDGnyeTYQEILRVM 214
Cdd:pfam06350  77 LLHIIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLR----ACLQHLQTLLswsepGDLFPSEDH---SSEELLREY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  215 EKLDSSVFFGRPIGFQFSPSINKIFRIIGVVLATYSLSWEKGHGAIG----SLINTGRFFLSPEQRAERIIKVTKEADID 290
Cdd:pfam06350 150 ETINQYCFYGRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGraasSLFTSGKYALDPELRARRIVNITQNADVD 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533410  291 FCKGFWNL--SELSNNMPKFFCPNMALNELREIPLDgAIPMEG-KSGEMVMVPEPSAHTGPRPVQYRILSTVHREKMS 365
Cdd:pfam06350 230 FCKAFWNLteSELLSSLPSIVSPSVAVNRVISIPPE-PLTLPLsDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
380-487 4.17e-29

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: 115.39  E-value: 4.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  380 VLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIVMVGDSA 459
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100
                  ....*....|....*....|....*...
gi 115533410  460 GGNLIMSVNLRLIQLNIKRqPDGLVLCY 487
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPK-PAGQVLIY 107
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
379-487 3.98e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 112.66  E-value: 3.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410 379 LVLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIVMVGDS 458
Cdd:COG0657   15 VVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPDRIAVAGDS 94
                         90       100
                 ....*....|....*....|....*....
gi 115533410 459 AGGNLIMSVNLRLIQLNIKRqPDGLVLCY 487
Cdd:COG0657   95 AGGHLAAALALRARDRGGPR-PAAQVLIY 122
PRK10162 PRK10162
acetyl esterase;
374-471 1.54e-12

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 69.75  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410 374 PPSKYLVLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIV 453
Cdd:PRK10162  78 PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIG 157
                         90
                 ....*....|....*...
gi 115533410 454 MVGDSAGGNLIMSVNLRL 471
Cdd:PRK10162 158 FAGDSAGAMLALASALWL 175
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
850-912 2.25e-08

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: 55.29  E-value: 2.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533410  850 RDPLISPMYAdnETMCQLPPCYFMACHMDPLLDDTISFAGKLRDAGGKVMSVdLLSSVPHGFL 912
Cdd:pfam07859 149 DDPLASPLFA--SDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELI-EYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
851-937 2.86e-08

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 54.88  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410 851 DPLISPMYADNEtmcQLPPCYFMACHMDPLLDDTISFAGKLRDAGGKVmSVDLLSSVPHGFLNFTLIsPECKKSGQVCIN 930
Cdd:COG0657  126 DLTASPLRADLA---GLPPTLIVTGEADPLVDESEALAAALRAAGVPV-ELHVYPGGGHGFGLLAGL-PEARAALAEIAA 200

                 ....*..
gi 115533410 931 RLKEALG 937
Cdd:COG0657  201 FLRRALA 207
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
60-365 2.22e-119

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: 366.19  E-value: 2.22e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410   60 ILELIVQMCSDNATHFEKLAQSGANgyneRMPVVQTALQTAIETLKGNIKKLQEVAPKYDYDEKTPGNGYRSLICICDTT 139
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEGDSSENGQ----RLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  140 LLHVVSLQKAVFEQRGYLIFRISHFCKELEAYATVIDYLNkfipLCLETERNMR-----GSLFPPLDGnyeTYQEILRVM 214
Cdd:pfam06350  77 LLHIIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLR----ACLQHLQTLLswsepGDLFPSEDH---SSEELLREY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  215 EKLDSSVFFGRPIGFQFSPSINKIFRIIGVVLATYSLSWEKGHGAIG----SLINTGRFFLSPEQRAERIIKVTKEADID 290
Cdd:pfam06350 150 ETINQYCFYGRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGraasSLFTSGKYALDPELRARRIVNITQNADVD 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533410  291 FCKGFWNL--SELSNNMPKFFCPNMALNELREIPLDgAIPMEG-KSGEMVMVPEPSAHTGPRPVQYRILSTVHREKMS 365
Cdd:pfam06350 230 FCKAFWNLteSELLSSLPSIVSPSVAVNRVISIPPE-PLTLPLsDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
380-487 4.17e-29

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: 115.39  E-value: 4.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  380 VLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIVMVGDSA 459
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100
                  ....*....|....*....|....*...
gi 115533410  460 GGNLIMSVNLRLIQLNIKRqPDGLVLCY 487
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPK-PAGQVLIY 107
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
379-487 3.98e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 112.66  E-value: 3.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410 379 LVLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIVMVGDS 458
Cdd:COG0657   15 VVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPDRIAVAGDS 94
                         90       100
                 ....*....|....*....|....*....
gi 115533410 459 AGGNLIMSVNLRLIQLNIKRqPDGLVLCY 487
Cdd:COG0657   95 AGGHLAAALALRARDRGGPR-PAAQVLIY 122
PRK10162 PRK10162
acetyl esterase;
374-471 1.54e-12

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 69.75  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410 374 PPSKYLVLHCHGGGYVATSSKSHETYLRQWSKALNCPVVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIV 453
Cdd:PRK10162  78 PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIG 157
                         90
                 ....*....|....*...
gi 115533410 454 MVGDSAGGNLIMSVNLRL 471
Cdd:PRK10162 158 FAGDSAGAMLALASALWL 175
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
850-912 2.25e-08

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: 55.29  E-value: 2.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533410  850 RDPLISPMYAdnETMCQLPPCYFMACHMDPLLDDTISFAGKLRDAGGKVMSVdLLSSVPHGFL 912
Cdd:pfam07859 149 DDPLASPLFA--SDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELI-EYPGMPHGFH 208
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
379-463 2.59e-08

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: 55.26  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  379 LVLHCHGGGYVATSSKSHETYLRQWSKALNCP---VVSVEYSLAPENPFPRPTEEVLFAYSWIINNPAAVGWTGEKIVMV 455
Cdd:pfam20434  15 VVIWIHGGGWNSGDKEADMGFMTNTVKALLKAgyaVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGIDTNKIALM 94

                  ....*...
gi 115533410  456 GDSAGGNL 463
Cdd:pfam20434  95 GFSAGGHL 102
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
851-937 2.86e-08

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 54.88  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410 851 DPLISPMYADNEtmcQLPPCYFMACHMDPLLDDTISFAGKLRDAGGKVmSVDLLSSVPHGFLNFTLIsPECKKSGQVCIN 930
Cdd:COG0657  126 DLTASPLRADLA---GLPPTLIVTGEADPLVDESEALAAALRAAGVPV-ELHVYPGGGHGFGLLAGL-PEARAALAEIAA 200

                 ....*..
gi 115533410 931 RLKEALG 937
Cdd:COG0657  201 FLRRALA 207
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
371-475 5.02e-04

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 43.67  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533410  371 TTHPPSKYLVLHCHGGGYVATSSKSHETYLRQWSKAL-NCPVVSVEYSLAPENP----FPRPTEEVLFAYSWIINnpaAV 445
Cdd:pfam10340 116 TFDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFpDMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYLTL---TK 192
                          90       100       110
                  ....*....|....*....|....*....|
gi 115533410  446 GWTgeKIVMVGDSAGGNLIMSVNLRLIQLN 475
Cdd:pfam10340 193 GCK--NVTLMGDSAGGNLVLNILLYLHKCN 220
 
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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