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Conserved domains on  [gi|1951328976|ref|XP_038566890|]
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hormone-sensitive lipase isoform X1 [Micropterus salmoides]

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 ...
37-348 2.62e-178

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: 515.65  E-value: 2.62e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976  37 VFAAVYSVCEENATFYSGGAKGPQGdaarRLVDAMKLIKEHARGLEPVISGFASVYHHFDFDPHIPANGYRSLVKVVRCC 116
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEGDSSENGQ----RLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 117 LLHIIQKGRYITANRRSIFFRVAHNAGEMEAYCSALCQLRALLYLAQRMLHDNSHGNLFFqDENGLSESFVREYSSMHKG 196
Cdd:pfam06350  77 LLHIIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFP-SEDHSSEELLREYETINQY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 197 CFYGRCLGFQFTPGIRPCLQTIAIGLVAFGENYKRHQSGIGVAASSFFTSGKYAIDPELRGAEFERITQNLDVHFWKAFW 276
Cdd:pfam06350 156 CFYGRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFW 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1951328976 277 NITETEVLSSLASMTSTQVKVNRALSVPSVAFDLPLaANHRTSVTIAPPSAHIGTAPVQMRLISYDLREGQD 348
Cdd:pfam06350 236 NLTESELLSSLPSIVSPSVAVNRVISIPPEPLTLPL-SDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
381-526 6.86e-36

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: 135.03  E-value: 6.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 381 LIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVCLAGDSA 460
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1951328976 461 GGNLSVTTSMRAAAFGVRMPDGIVAAYPATLLTAyASPSRLLTLM--DPLLPLSVLSKCLSAYAGNAP 526
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRT-ESPSYLAREFadGPLLTRAAMDWFWRLYLPGAD 147
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
707-796 3.04e-13

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 69.52  E-value: 3.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 707 SPVVkDPFCSPLLAPdsmLKGLPPVHIVACALDPMLDDSVMFAKRLRNIDQPVTLCVVDDLPHGFLSLSqLSKETREAAN 786
Cdd:COG0657   122 YPVL-DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLA-GLPEARAALA 196
                          90
                  ....*....|
gi 1951328976 787 VCVERIRAVF 796
Cdd:COG0657   197 EIAAFLRRAL 206
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
37-348 2.62e-178

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: 515.65  E-value: 2.62e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976  37 VFAAVYSVCEENATFYSGGAKGPQGdaarRLVDAMKLIKEHARGLEPVISGFASVYHHFDFDPHIPANGYRSLVKVVRCC 116
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEGDSSENGQ----RLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 117 LLHIIQKGRYITANRRSIFFRVAHNAGEMEAYCSALCQLRALLYLAQRMLHDNSHGNLFFqDENGLSESFVREYSSMHKG 196
Cdd:pfam06350  77 LLHIIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFP-SEDHSSEELLREYETINQY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 197 CFYGRCLGFQFTPGIRPCLQTIAIGLVAFGENYKRHQSGIGVAASSFFTSGKYAIDPELRGAEFERITQNLDVHFWKAFW 276
Cdd:pfam06350 156 CFYGRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFW 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1951328976 277 NITETEVLSSLASMTSTQVKVNRALSVPSVAFDLPLaANHRTSVTIAPPSAHIGTAPVQMRLISYDLREGQD 348
Cdd:pfam06350 236 NLTESELLSSLPSIVSPSVAVNRVISIPPEPLTLPL-SDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
381-526 6.86e-36

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: 135.03  E-value: 6.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 381 LIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVCLAGDSA 460
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1951328976 461 GGNLSVTTSMRAAAFGVRMPDGIVAAYPATLLTAyASPSRLLTLM--DPLLPLSVLSKCLSAYAGNAP 526
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRT-ESPSYLAREFadGPLLTRAAMDWFWRLYLPGAD 147
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
380-500 7.96e-33

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.14  E-value: 7.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 380 LLIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVCLAGDS 459
Cdd:COG0657    15 VVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPDRIAVAGDS 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1951328976 460 AGGNLSVTTSMRAAAFGVRMPDGIVAAYPATLLTayASPSR 500
Cdd:COG0657    95 AGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT--ASPLR 133
PRK10162 PRK10162
acetyl esterase;
375-502 2.00e-15

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 78.22  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 375 PSSPCLLIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVC 454
Cdd:PRK10162   78 PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIG 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1951328976 455 LAGDSAGGNLSVttsmrAAAFGVRmPDGIVAAYPATLLTAYA------SPSRLL 502
Cdd:PRK10162  158 FAGDSAGAMLAL-----ASALWLR-DKQIDCGKVAGVLLWYGlyglrdSVSRRL 205
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
707-796 3.04e-13

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 69.52  E-value: 3.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 707 SPVVkDPFCSPLLAPdsmLKGLPPVHIVACALDPMLDDSVMFAKRLRNIDQPVTLCVVDDLPHGFLSLSqLSKETREAAN 786
Cdd:COG0657   122 YPVL-DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLA-GLPEARAALA 196
                          90
                  ....*....|
gi 1951328976 787 VCVERIRAVF 796
Cdd:COG0657   197 EIAAFLRRAL 206
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
37-348 2.62e-178

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: 515.65  E-value: 2.62e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976  37 VFAAVYSVCEENATFYSGGAKGPQGdaarRLVDAMKLIKEHARGLEPVISGFASVYHHFDFDPHIPANGYRSLVKVVRCC 116
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEGDSSENGQ----RLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 117 LLHIIQKGRYITANRRSIFFRVAHNAGEMEAYCSALCQLRALLYLAQRMLHDNSHGNLFFqDENGLSESFVREYSSMHKG 196
Cdd:pfam06350  77 LLHIIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFP-SEDHSSEELLREYETINQY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 197 CFYGRCLGFQFTPGIRPCLQTIAIGLVAFGENYKRHQSGIGVAASSFFTSGKYAIDPELRGAEFERITQNLDVHFWKAFW 276
Cdd:pfam06350 156 CFYGRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFW 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1951328976 277 NITETEVLSSLASMTSTQVKVNRALSVPSVAFDLPLaANHRTSVTIAPPSAHIGTAPVQMRLISYDLREGQD 348
Cdd:pfam06350 236 NLTESELLSSLPSIVSPSVAVNRVISIPPEPLTLPL-SDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
381-526 6.86e-36

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: 135.03  E-value: 6.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 381 LIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVCLAGDSA 460
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1951328976 461 GGNLSVTTSMRAAAFGVRMPDGIVAAYPATLLTAyASPSRLLTLM--DPLLPLSVLSKCLSAYAGNAP 526
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRT-ESPSYLAREFadGPLLTRAAMDWFWRLYLPGAD 147
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
380-500 7.96e-33

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.14  E-value: 7.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 380 LLIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVCLAGDS 459
Cdd:COG0657    15 VVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPDRIAVAGDS 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1951328976 460 AGGNLSVTTSMRAAAFGVRMPDGIVAAYPATLLTayASPSR 500
Cdd:COG0657    95 AGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT--ASPLR 133
PRK10162 PRK10162
acetyl esterase;
375-502 2.00e-15

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 78.22  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 375 PSSPCLLIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVC 454
Cdd:PRK10162   78 PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIG 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1951328976 455 LAGDSAGGNLSVttsmrAAAFGVRmPDGIVAAYPATLLTAYA------SPSRLL 502
Cdd:PRK10162  158 FAGDSAGAMLAL-----ASALWLR-DKQIDCGKVAGVLLWYGlyglrdSVSRRL 205
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
707-796 3.04e-13

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 69.52  E-value: 3.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 707 SPVVkDPFCSPLLAPdsmLKGLPPVHIVACALDPMLDDSVMFAKRLRNIDQPVTLCVVDDLPHGFLSLSqLSKETREAAN 786
Cdd:COG0657   122 YPVL-DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLA-GLPEARAALA 196
                          90
                  ....*....|
gi 1951328976 787 VCVERIRAVF 796
Cdd:COG0657   197 EIAAFLRRAL 206
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
380-465 2.69e-07

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: 52.18  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 380 LLIHFHGGGFVAQTSKSHEPYLKSWSQDL---GVPILSVDYSLAPEAPFPRALEECFYAYCWaLRNH-HLLGWTGEKVCL 455
Cdd:pfam20434  15 VVIWIHGGGWNSGDKEADMGFMTNTVKALlkaGYAVASINYRLSTDAKFPAQIQDVKAAIRF-LRANaAKYGIDTNKIAL 93
                          90
                  ....*....|
gi 1951328976 456 AGDSAGGNLS 465
Cdd:pfam20434  94 MGFSAGGHLA 103
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
375-464 3.82e-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: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951328976 375 PSSPCLLIHFHGGGFVAQTSKSHEPYLKSWSQDLG-VPILSVDYSLAPEAP----FPRALEECFYAYCWALRNhhlLGWT 449
Cdd:pfam10340 119 PKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPdMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYLTLT---KGCK 195
                          90
                  ....*....|....*
gi 1951328976 450 geKVCLAGDSAGGNL 464
Cdd:pfam10340 196 --NVTLMGDSAGGNL 208
 
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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