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Conserved domains on  [gi|440213414|gb|AGB92654|]
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infertile crescent, isoform B [Drosophila melanogaster]

Protein Classification

fatty acid desaturase family protein( domain architecture ID 1056)

fatty acid desaturase (FADS) family protein similar to membrane FADSs, which are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains, and to beta-carotene ketolase/oxygenases (CrtW-like) and hydroxylases (CrtR-like)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Membrane-FADS-like super family cl00615
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 1-96 1.27e-63

The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase.


The actual alignment was detected with superfamily member cd03508:

Pssm-ID: 445012 [Multi-domain]  Cd Length: 289  Bit Score: 194.01  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440213414   1 MGLHPVAGHFISEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLY 79
Cdd:cd03508  193 GGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLY 272

                         90
                 ....*....|....*..
gi 440213414  80 DFIMDPAVGPYARVKRR 96
Cdd:cd03508  273 DFIMDDNVGPYSRVKRK 289
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 1-96 1.27e-63

The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239585 [Multi-domain]  Cd Length: 289  Bit Score: 194.01  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440213414   1 MGLHPVAGHFISEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLY 79
Cdd:cd03508  193 GGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLY 272

                         90
                 ....*....|....*..
gi 440213414  80 DFIMDPAVGPYARVKRR 96
Cdd:cd03508  273 DFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 1-96 2.96e-60

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 186.48  E-value: 2.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440213414   1 MGLHPVAGHFISEHYMFAKGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYD 80
Cdd:PLN02579 222 GGLHPMAGHFISEHYVFNPGQETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYM 301

                         90
                 ....*....|....*.
gi 440213414  81 FIMDPAVGPYARVKRR 96
Cdd:PLN02579 302 YIMDPTIGPFSRMKRK 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
10-66 7.28e-09

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 51.27  E-value: 7.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440213414  10 FISEHYMFAKGFE----------TYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 66
Cdd:COG3239  220 FYLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 23-66 8.31e-08

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 48.11  E-value: 8.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 440213414   23 TYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 66
Cdd:pfam00487 199 IRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALP 242
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 1-96 1.27e-63

The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239585 [Multi-domain]  Cd Length: 289  Bit Score: 194.01  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440213414   1 MGLHPVAGHFISEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLY 79
Cdd:cd03508  193 GGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLY 272

                         90
                 ....*....|....*..
gi 440213414  80 DFIMDPAVGPYARVKRR 96
Cdd:cd03508  273 DFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 1-96 2.96e-60

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 186.48  E-value: 2.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440213414   1 MGLHPVAGHFISEHYMFAKGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYD 80
Cdd:PLN02579 222 GGLHPMAGHFISEHYVFNPGQETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYM 301

                         90
                 ....*....|....*.
gi 440213414  81 FIMDPAVGPYARVKRR 96
Cdd:PLN02579 302 YIMDPTIGPFSRMKRK 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
10-66 7.28e-09

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 51.27  E-value: 7.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440213414  10 FISEHYMFAKGFE----------TYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 66
Cdd:COG3239  220 FYLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 23-66 8.31e-08

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 48.11  E-value: 8.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 440213414   23 TYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 66
Cdd:pfam00487 199 IRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALP 242
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 29-63 4.43e-04

This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine (3-O-methyl-scyllo-inosamine, 3-O-MSI) oxygenase, and other related proteins. It has been proposed that MocD, MocE (Rieske-like ferredoxin), and MocF (ferredoxin reductase) under the regulation of MocR, act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239588 [Multi-domain]  Cd Length: 285  Bit Score: 37.35  E-value: 4.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 440213414  29 PLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKE 63
Cdd:cd03511  237 PLRFLYWNMPYHAEHHMYPSVPFHALPKLHELIKD 271
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 30-66 5.34e-04

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583 [Multi-domain]  Cd Length: 204  Bit Score: 37.24  E-value: 5.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 440213414  30 LNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 66
Cdd:cd03506  164 LDWLHGGLNYQIEHHLFPTMPRHNYPKVAPLVRELCK 200
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 5-47 1.03e-03

The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase.


Pssm-ID: 238511 [Multi-domain]  Cd Length: 122  Bit Score: 35.52  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 440213414   5 PVAGHFISEHYMFAKGFET---------YSYYGPLNWITFN-VGYHNEHHDFP 47
Cdd:cd01060   70 PDSAVNYLEHYGGDRPFDTdgewlrttdNSRNGWLNLLLTGgLGYHNEHHLFP 122
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 36-60 3.65e-03

This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in Bradyrhizobium japonicum USDA110, and other related proteins. Dihydrorhizobitoxine desaturase is reported to be involved in the final step of rhizobitoxine biosynthesis. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239587 [Multi-domain]  Cd Length: 175  Bit Score: 34.57  E-value: 3.65e-03
                         10        20
                 ....*....|....*....|....*
gi 440213414  36 NVGYHNEHHDFPAVPGSRLPEVKRI 60
Cdd:cd03510  150 NINYHLEHHLFPAVPFYNLPKAHRI 174
CrtW_beta-carotene-ketolase cd03513
Beta-carotene ketolase/oxygenase (CrtW, also known as CrtO), the carotenoid astaxanthin ...
 35-58 4.57e-03

Beta-carotene ketolase/oxygenase (CrtW, also known as CrtO), the carotenoid astaxanthin biosynthetic enzyme, initially catalyzes the addition of two keto groups to carbons C4 and C4' of beta-carotene. Carotenoids are important natural pigments produced by many microorganisms and plants. Astaxanthin is reported to be an antioxidant, an anti-cancer agent, and an immune system stimulant. A number of bacteria and green algae can convert beta-carotene into astaxanthin by using several ketocarotenoids as intermediates and CrtW and a beta-carotene hydroxylase (CrtZ). CrtW initially converts beta-carotene to canthaxanthin via echinenone, and CrtZ initially mediates the conversion of beta-carotene to zeaxanthin via beta-cryptoxanthin. After a few more intermediates are formed, CrtW and CrtZ act in combination to produce astaxanthin. Sequences of this domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that are capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239590 [Multi-domain]  Cd Length: 225  Bit Score: 34.60  E-value: 4.57e-03
                         10        20
                 ....*....|....*....|....
gi 440213414  35 FNVGYHNEHHDFPAVPGSRLPEVK 58
Cdd:cd03513  202 YHFGYHHEHHLSPSTPWWRLPELR 225
DesA_FADS-like cd03509
Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, ...
 28-65 7.38e-03

Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, DesA-like, yet uncharacterized subgroup of membrane fatty acid desaturase proteins found in alpha-, beta-, and gamma-proteobacteria. Sequences of this domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239586 [Multi-domain]  Cd Length: 288  Bit Score: 33.87  E-value: 7.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440213414  28 GPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFY 65
Cdd:cd03509  220 GPLRLLFLNNNLHVVHHDLPTLPWYDLPRLYRARRDAY 257
 
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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