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Conserved domains on  [gi|71999459|ref|NP_001023560|]
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Omega-3 fatty acid desaturase fat-1 [Caenorhabditis elegans]

Protein Classification

fatty acid desaturase( domain architecture ID 10131385)

fatty acid desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to delta(12) fatty acid desaturase and related proteins

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717
PubMed:  9767077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 70-338 6.84e-73

The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. 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, 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 the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.


:

Pssm-ID: 239584 [Multi-domain]  Cd Length: 222  Bit Score: 227.11  E-value: 6.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  70 RDLVKSIRYLVQDFAALTILYFAlpAFEYFGLFGYLVWNIFMGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLF 149
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALA--ASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 150 SPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDWEAMPSWKRWFNPIPFSGWLKWFPVYTLFGfcdgshfwpysslfvrn 229
Cdd:cd03507  79 VPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLL----------------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 230 servqcvisgicccvcayialtiagsysNWFWYYWVPLSFFGLMLVIVTYLQHVDDVAEVYEADEWSF-VRGQTQTIDRY 308
Cdd:cd03507 142 ----------------------------NVLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFaQAGLLGTVDRD 193

                       250       260       270
                ....*....|....*....|....*....|
gi 71999459 309 YGLGLDtTMHHITDGHVAHHFFNKIPHYHL 338
Cdd:cd03507 194 YGGWLN-WLTHIIGTHVAHHLFPRIPHYNL 222
 
Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 70-338 6.84e-73

The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. 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, 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 the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.


Pssm-ID: 239584 [Multi-domain]  Cd Length: 222  Bit Score: 227.11  E-value: 6.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  70 RDLVKSIRYLVQDFAALTILYFAlpAFEYFGLFGYLVWNIFMGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLF 149
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALA--ASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 150 SPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDWEAMPSWKRWFNPIPFSGWLKWFPVYTLFGfcdgshfwpysslfvrn 229
Cdd:cd03507  79 VPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLL----------------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 230 servqcvisgicccvcayialtiagsysNWFWYYWVPLSFFGLMLVIVTYLQHVDDVAEVYEADEWSF-VRGQTQTIDRY 308
Cdd:cd03507 142 ----------------------------NVLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFaQAGLLGTVDRD 193

                       250       260       270
                ....*....|....*....|....*....|
gi 71999459 309 YGLGLDtTMHHITDGHVAHHFFNKIPHYHL 338
Cdd:cd03507 194 YGGWLN-WLTHIIGTHVAHHLFPRIPHYNL 222
PLN02505 PLN02505
omega-6 fatty acid desaturase
 55-349 3.50e-63

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 207.61  E-value: 3.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   55 TVDAFRRAIPAHCFERDLVKSIRYLVQDFAALTIL-YFALPAFEYF-GLFGYLVWN---IFMGVFGFALFVVGHDCLHGS 129
Cdd:PLN02505  32 TLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLyYVATNYIPLLpGPLSYVAWPlywAAQGCVLTGVWVIAHECGHHA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  130 FSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDHGHVwiqDKDWEAMPSWKRWF-NP------IPFSGWL 202
Cdd:PLN02505 112 FSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFV---PKKKSALPWYSKYLnNPpgrllhIVVQLTL 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  203 KWfPVYTLFGFCD------GSHFWPYSSLFVRNsERVQCVIS--GICCCVCAYIALTIAGSysnwFWY----YWVPLSFF 270
Cdd:PLN02505 189 GW-PLYLAFNVSGrpydrfACHFDPYSPIFNDR-ERLQIYISdaGILAVSFGLYRLAAAKG----LAWvlcvYGVPLLIV 262

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71999459  271 GLMLVIVTYLQHVDDVAEVYEADEWSFVRGQTQTIDRYYGLgLDTTMHHITDGHVAHHFFNKIPHYHLIEATEGVKKVL 349
Cdd:PLN02505 263 NAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGI-LNKVFHNITDTHVAHHLFSTMPHYHAMEATKAIKPIL 340
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
43-350 2.02e-38

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 140.63  E-value: 2.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  43 QATTEEPRIQLPTVDAFRRAIPAHCFERDLvKSIRYLVQDFAALTILYFALPafeyFGLFGYLVWnIFMGVFGFALFVVG 122
Cdd:COG3239   2 TTATPLTPADEAELRALRARLRALLGRRDW-RYLLKLALTLALLAALWLLLS----WSWLALLAA-LLLGLALAGLFSLG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 123 HDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDweampSWKRWFNPIPFSGWL 202
Cdd:COG3239  76 HDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAW-----RPLYLFQHLLRFFLL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 203 KWFPVYTLFgfcdGSHFWPYSSLFVRNSERVQCVISGIccCVCAYIALTIAGSYSNWFWYYWVPLSFFGLMLVIVTYLQH 282
Cdd:COG3239 151 GLGGLYWLL----ALDFLPLRGRLELKERRLEALLLLL--FLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLRFYLEH 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71999459 283 VddVAEVYEADEWSFVRGqtqTIDRYYGLGLDTTMHHItdG-HVAHHFFNKIPHYHLIEATEGVKKVLE 350
Cdd:COG3239 225 R--GEDTGDGEYRDQLLG---SRNIRGGRLLRWLFGNL--NyHIEHHLFPSIPWYRLPEAHRILKELCP 286
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 104-351 4.33e-15

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: 74.69  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   104 YLVWNIFMGVFGFALFVVGHDCLHGSFSD----NQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDhGHVWIQ 179
Cdd:pfam00487   5 LLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKD-PDTAPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   180 DKDWEAMPSWkrwfnpipfsgWLKWFPVYTLFGFCDGSHFWPYSSLFVRNSERVQCVISGICCCVCAYIALTIAGSYSNW 259
Cdd:pfam00487  84 ASRFRGLLRY-----------LLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   260 FWYYWVPLSFFGL-MLVIVTYLQHVDDVAEVYeADEWSFVRGQTQTIDRYYGLGLDTTMHHITDgHVAHHFFNKIPHYHL 338
Cdd:pfam00487 153 LGLGGLLLLLWLLpLLVFGFLLALIFNYLEHY-GGDWGERPVETTRSIRSPNWWLNLLTGNLNY-HIEHHLFPGVPWYRL 230

                         250
                  ....*....|...
gi 71999459   339 IEATEGVKKVLEP 351
Cdd:pfam00487 231 PKLHRRLREALPE 243
 
Name Accession Description Interval E-value
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 70-338 6.84e-73

The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. 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, 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 the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.


Pssm-ID: 239584 [Multi-domain]  Cd Length: 222  Bit Score: 227.11  E-value: 6.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  70 RDLVKSIRYLVQDFAALTILYFAlpAFEYFGLFGYLVWNIFMGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLF 149
Cdd:cd03507   1 RSLFRSLSYLAPDILLLALLALA--ASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHILHSPLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 150 SPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDWEAMPSWKRWFNPIPFSGWLKWFPVYTLFGfcdgshfwpysslfvrn 229
Cdd:cd03507  79 VPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLL----------------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 230 servqcvisgicccvcayialtiagsysNWFWYYWVPLSFFGLMLVIVTYLQHVDDVAEVYEADEWSF-VRGQTQTIDRY 308
Cdd:cd03507 142 ----------------------------NVLLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRADEWNFaQAGLLGTVDRD 193

                       250       260       270
                ....*....|....*....|....*....|
gi 71999459 309 YGLGLDtTMHHITDGHVAHHFFNKIPHYHL 338
Cdd:cd03507 194 YGGWLN-WLTHIIGTHVAHHLFPRIPHYNL 222
PLN02505 PLN02505
omega-6 fatty acid desaturase
 55-349 3.50e-63

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 207.61  E-value: 3.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   55 TVDAFRRAIPAHCFERDLVKSIRYLVQDFAALTIL-YFALPAFEYF-GLFGYLVWN---IFMGVFGFALFVVGHDCLHGS 129
Cdd:PLN02505  32 TLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLyYVATNYIPLLpGPLSYVAWPlywAAQGCVLTGVWVIAHECGHHA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  130 FSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDHGHVwiqDKDWEAMPSWKRWF-NP------IPFSGWL 202
Cdd:PLN02505 112 FSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFV---PKKKSALPWYSKYLnNPpgrllhIVVQLTL 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  203 KWfPVYTLFGFCD------GSHFWPYSSLFVRNsERVQCVIS--GICCCVCAYIALTIAGSysnwFWY----YWVPLSFF 270
Cdd:PLN02505 189 GW-PLYLAFNVSGrpydrfACHFDPYSPIFNDR-ERLQIYISdaGILAVSFGLYRLAAAKG----LAWvlcvYGVPLLIV 262

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71999459  271 GLMLVIVTYLQHVDDVAEVYEADEWSFVRGQTQTIDRYYGLgLDTTMHHITDGHVAHHFFNKIPHYHLIEATEGVKKVL 349
Cdd:PLN02505 263 NAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGI-LNKVFHNITDTHVAHHLFSTMPHYHAMEATKAIKPIL 340
PLN02498 PLN02498
omega-3 fatty acid desaturase
 8-349 2.40e-51

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 178.10  E-value: 2.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459    8 GLSATAPVTggdvlvdaRASLEEKEAPRDVNANTKQATTE-EPRIQLP-TVDAFRRAIPAHCFERDLVKSIRYLVQDFAA 85
Cdd:PLN02498  62 ALNVSAPLT--------VPSGEEEEDEEGVNGVGEDEEGEfDPGAPPPfNLADIRAAIPKHCWVKNPWRSMSYVVRDVAV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   86 LtilyFALPAFEYFgLFGYLVWNIF---MGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLH 162
Cdd:PLN02498 134 V----FGLAAAAAY-FNNWVVWPLYwfaQGTMFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTH 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  163 HaftnhidKDHGHVWiQDKDWEAMPS--WKRWFNP-------IPFSgwLKWFPVYtLFGFC---DGSHFWPYSSLFVRNs 230
Cdd:PLN02498 209 H-------QNHGHVE-NDESWHPLSEkiYKSLDKVtrtlrftLPFP--MLAYPFY-LWSRSpgkKGSHFHPDSDLFVPK- 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  231 ERVQCVISGICCcvCAYIALTIAGSYS----NWFWYYWVPLSFFGLMLVIVTYLQH--VDDVAEVYEADEWSFVRGQTQT 304
Cdd:PLN02498 277 ERKDVITSTACW--TAMAALLVCLSFVmgpiQMLKLYGIPYWIFVMWLDFVTYLHHhgHEDKLPWYRGKEWSYLRGGLTT 354

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 71999459  305 IDRYYglGLDTTMHHITDGHVAHHFFNKIPHYHLIEATEGVKKVL 349
Cdd:PLN02498 355 LDRDY--GWINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVL 397
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
43-350 2.02e-38

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 140.63  E-value: 2.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  43 QATTEEPRIQLPTVDAFRRAIPAHCFERDLvKSIRYLVQDFAALTILYFALPafeyFGLFGYLVWnIFMGVFGFALFVVG 122
Cdd:COG3239   2 TTATPLTPADEAELRALRARLRALLGRRDW-RYLLKLALTLALLAALWLLLS----WSWLALLAA-LLLGLALAGLFSLG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 123 HDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDweampSWKRWFNPIPFSGWL 202
Cdd:COG3239  76 HDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAW-----RPLYLFQHLLRFFLL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 203 KWFPVYTLFgfcdGSHFWPYSSLFVRNSERVQCVISGIccCVCAYIALTIAGSYSNWFWYYWVPLSFFGLMLVIVTYLQH 282
Cdd:COG3239 151 GLGGLYWLL----ALDFLPLRGRLELKERRLEALLLLL--FLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLRFYLEH 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71999459 283 VddVAEVYEADEWSFVRGqtqTIDRYYGLGLDTTMHHItdG-HVAHHFFNKIPHYHLIEATEGVKKVLE 350
Cdd:COG3239 225 R--GEDTGDGEYRDQLLG---SRNIRGGRLLRWLFGNL--NyHIEHHLFPSIPWYRLPEAHRILKELCP 286
PLN02598 PLN02598
omega-6 fatty acid desaturase
 61-347 3.02e-23

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 100.67  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   61 RAIPAHCFERDLVKSIRYLVQDFAALTILYFALPAFEYFGLfgYLVWnIFMGVFGFALFVVGHDCLHGSFSDNQNLNDFI 140
Cdd:PLN02598  85 KTLPKEVFEIDDFKAWKTVAITVTSYALGLAAIAVAPWYLL--PLAW-AWLGTAITGFFVIGHDCGHNSFSKNQLVEDIV 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  141 GHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDWEAMPSWKRwFNPIPFSGWLKWFPVYtlfgfcdgSH-- 218
Cdd:PLN02598 162 GTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQPFRPHQFDNADPLRK-AMMRAGMGPLWWWASI--------GHwl 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  219 FWPYSSLFVRNSERVQCVISGICC---CVCAYIALTIAGSYSNWFWYYWVPLSFFGLMLVIVTYLQHVDDVAEVYEADEW 295
Cdd:PLN02598 233 FWHFDLNKFRPQEVPRVKISLAAVfafMALGLPPLLYTTGPVGFVKWWLMPWLGYHFWMSTFTMVHHTAPHIPFKQAREW 312

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71999459  296 SFVRGQTQ-TIDRYYGLGLDTTMHHITdGHVAHHFFNKIPHYHLIEATEGVKK 347
Cdd:PLN02598 313 NAAQAQLNgTVHCDYPAWIEFLCHDIS-VHIPHHISSKIPSYNLRKAHASLQE 364
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 104-351 4.33e-15

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: 74.69  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   104 YLVWNIFMGVFGFALFVVGHDCLHGSFSD----NQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDhGHVWIQ 179
Cdd:pfam00487   5 LLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKD-PDTAPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   180 DKDWEAMPSWkrwfnpipfsgWLKWFPVYTLFGFCDGSHFWPYSSLFVRNSERVQCVISGICCCVCAYIALTIAGSYSNW 259
Cdd:pfam00487  84 ASRFRGLLRY-----------LLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459   260 FWYYWVPLSFFGL-MLVIVTYLQHVDDVAEVYeADEWSFVRGQTQTIDRYYGLGLDTTMHHITDgHVAHHFFNKIPHYHL 338
Cdd:pfam00487 153 LGLGGLLLLLWLLpLLVFGFLLALIFNYLEHY-GGDWGERPVETTRSIRSPNWWLNLLTGNLNY-HIEHHLFPGVPWYRL 230

                         250
                  ....*....|...
gi 71999459   339 IEATEGVKKVLEP 351
Cdd:pfam00487 231 PKLHRRLREALPE 243
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 105-202 6.34e-15

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: 70.58  E-value: 6.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 105 LVWNIFMGVF-GFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKD---------HG 174
Cdd:cd01060   1 LLLALLLGLLgGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKDpdsavnyleHY 80

                        90       100
                ....*....|....*....|....*...
gi 71999459 175 HVWIQDKDWEAMPSWKRWFNPIPFSGWL 202
Cdd:cd01060  81 GGDRPFDTDGEWLRTTDNSRNGWLNLLL 108
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 105-214 2.25e-14

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: 71.52  E-value: 2.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 105 LVWNIFMGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDH--GHVWIQDKD 182
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDPdiDTLPLLARS 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 71999459 183 WEAMPSWKRWFNPIPFSGWLkWFPVYTLFGFC 214
Cdd:cd03506  81 EPAFGKDQKKRFLHRYQHFY-FFPLLALLLLA 111
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 102-172 2.46e-06

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: 47.28  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 102 FGYLVWNIFMGVFGF--------ALFVVGHDCLHGSFSDNQNLNDFIGHIAFS-PLFSPYFPWQKSHKLHHAFTNhIDKD 172
Cdd:cd03510  11 LALAWPNWLAYLLAVlligarqrALAILMHDAAHGLLFRNRRLNDFLGNWLAAvPIFQSLAAYRRSHLKHHRHLG-TEDD 89
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 90-346 4.94e-06

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: 47.75  E-value: 4.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459  90 YFALPAFeyfglFGYlvwnifmGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNhi 169
Cdd:cd03511  42 WWALPAF-----LVY-------GVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQ-- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 170 dkdhghvwIQDKDWE----AMPSWKRWFnpIPFSGWLKWFpvYTLFGFCDGSHF--------------WPYsslfVRNSE 231
Cdd:cd03511 108 --------IPGRDPElavpRPPTLREYL--LALSGLPYWW--GKLRTVFRHAFGavseaekpfipaeeRPK----VVREA 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71999459 232 RVQCVISGICCCVCAYIALTIAgsysnwFWYYWVPLSFFGLMLVIVTYLQHV--DDVAevyeadeWSFVRGQTQTIDRYY 309
Cdd:cd03511 172 RAMLAVYAGLIALSLYLGSPLL------VLVWGLPLLLGQPILRLFLLAEHGgcPEDA-------NDLRNTRTTLTNPPL 238

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71999459 310 GLgLDTTMHHitdgHVAHHFFNKIPHYHLIEATEGVK 346
Cdd:cd03511 239 RF-LYWNMPY----HAEHHMYPSVPFHALPKLHELIK 270
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 116-175 7.02e-05

Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the addition of hydroxyl groups to the beta-ionone rings of beta-carotene to form zeaxanthin and is found in bacteria and red algae. Carotenoids are important natural pigments; zeaxanthin and lutein are the only dietary carotenoids that accumulate in the macular region of the retina and lens. It is proposed that these carotenoids protect ocular tissues against photooxidative damage. CrtR does not show overall amino acid sequence similarity to the beta-carotene hydroxylases similar to CrtZ, an astaxanthin biosynthetic beta-carotene hydroxylase. However, CrtR does show sequence similarity to the green alga, Haematococcus pluvialis, beta-carotene ketolase (CrtW), which converts beta-carotene to canthaxanthin. Sequences of the CrtR_beta-carotene-hydroxylase domain family, as well as, the CrtW_beta-carotene-ketolase 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: 239591 [Multi-domain]  Cd Length: 207  Bit Score: 43.51  E-value: 7.02e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71999459 116 FALFVVGHDCLHGSFSDNQNLNDFIGHIAfspLFSPYFPW---QKSHKLHHAFTNHIDKDHGH 175
Cdd:cd03514  36 HLAGTVIHDASHKAASRNRWINELIGHVS---AFFLGFPFpvfRRVHMQHHAHTNDPEKDPDH 95
CrtW_beta-carotene-ketolase cd03513
Beta-carotene ketolase/oxygenase (CrtW, also known as CrtO), the carotenoid astaxanthin ...
 118-166 5.91e-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: 38.07  E-value: 5.91e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71999459 118 LFVVGHDCLHGS-FSDNQNLNDFIGHIAFSpLFS--PYFPWQKSHKLHHAFT 166
Cdd:cd03513  46 LFIIAHDAMHGSlAPGNPRLNRAIGRLCLF-LYAgfSYDRLLRKHHLHHRHP 96
 
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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