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Conserved domains on  [gi|207113139|ref|NP_996801|]
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sphingolipid delta(4)-desaturase/C4-monooxygenase DES2 [Homo sapiens]

Protein Classification

sphingolipid delta(4)-desaturase family protein( domain architecture ID 10554096)

sphingolipid delta(4)-desaturase family protein such as sphingolipid delta(4)-desaturase (also called dihydroceramide desaturase) which generates a trans double bond at position 4 of sphinganine bases in sphingolipids

EC:  1.14.19.17
Gene Ontology:  GO:0046872|GO:0016020|GO:0008610|GO:0016717
PubMed:  9767077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 26-314 8.62e-163

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: 455.18  E-value: 8.62e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  26 ILAKYPAIKALMRPDPRLKWAVLVLVLVQMLACWLVRGLAWRWLLFWAYAFGGCVNHSLTLAIHDISHNAAFGTGRAarN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLW--N 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 106 RWLAVFANLPVGVPYAASFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLLWLVLQPFFYSLRPLCVHPKAVTRM 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 186 EVLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHVEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 207113139 265 FPSIPGYNLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYARVKR 314
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKR 288
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 6-42 4.28e-18

Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling molecules involved in many different cellular functions in eukaryotes. Sphingolipid delta 4-desaturase catalyzes the formation of (E)-sphing-4-enine. Some proteins in this family have bifunctional delta 4-desaturase/C-4-hydroxylase activity. Delta 4-desaturated sphingolipids may play a role in early signalling required for entry into meiotic and spermatid differentiation pathways during Drosophila spermatogenesis. This small domain associates with FA_desaturase pfam00487 and appears to be specific to sphingolipid delta 4-desaturase.


:

Pssm-ID: 462517  Cd Length: 37  Bit Score: 76.38  E-value: 4.28e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 207113139    6 SRSDFEWVYTDQPHTQRRKEILAKYPAIKALMRPDPR 42
Cdd:pfam08557   1 SRNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 26-314 8.62e-163

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: 455.18  E-value: 8.62e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  26 ILAKYPAIKALMRPDPRLKWAVLVLVLVQMLACWLVRGLAWRWLLFWAYAFGGCVNHSLTLAIHDISHNAAFGTGRAarN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLW--N 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 106 RWLAVFANLPVGVPYAASFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLLWLVLQPFFYSLRPLCVHPKAVTRM 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 186 EVLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHVEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 207113139 265 FPSIPGYNLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYARVKR 314
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKR 288
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 9-314 4.87e-153

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 431.86  E-value: 4.87e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139   9 DFEWVYTDQPHTQRRKEILAKYPAIKALMRPDPRLKWAVLVLVLVQMLACWLVRGLAWRWLLFWAYAFGGCVNHSLTLAI 88
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  89 HDISHNAAFGTGRAarNRWLAVFANLPVGVPYAASFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLLWLVLQPF 168
Cdd:PLN02579  93 HELSHNLAFKTPVY--NRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 169 FYSLRPLCVHPKAVTRMEVLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFVAEHYMFLKGHETYSYYGP 248
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 207113139 249 LNWITFNVGYHVEHHDFPSIPGYNLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYARVKR 314
Cdd:PLN02579 251 LNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKR 316
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
32-285 9.05e-29

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 112.90  E-value: 9.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  32 AIKALMRPDPRLKWAVLVLVLVQMLACWLVrgLAWRWLLFWAYAFGGCVNHSLTLAIHDISHNAAFGTGRAarNRWLAVF 111
Cdd:COG3239   21 RLRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWL--NDLLGRL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 112 ANLPVGVPYAAsFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLL--WLVLQPFFYSLRP---LCVHPKAVTRME 186
Cdd:COG3239   97 LGLPLGTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLAldfLPLRGRLELKER 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 187 VLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFV--AEHYMFLKGHE----------TYSYYGPLNWITF 254
Cdd:COG3239  176 RLEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLRfyLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFG 255

                        250       260       270
                 ....*....|....*....|....*....|.
gi 207113139 255 NVGYHVEHHDFPSIPGYNLPLVRKIAPEYYD 285
Cdd:COG3239  256 NLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 6-42 4.28e-18

Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling molecules involved in many different cellular functions in eukaryotes. Sphingolipid delta 4-desaturase catalyzes the formation of (E)-sphing-4-enine. Some proteins in this family have bifunctional delta 4-desaturase/C-4-hydroxylase activity. Delta 4-desaturated sphingolipids may play a role in early signalling required for entry into meiotic and spermatid differentiation pathways during Drosophila spermatogenesis. This small domain associates with FA_desaturase pfam00487 and appears to be specific to sphingolipid delta 4-desaturase.


Pssm-ID: 462517  Cd Length: 37  Bit Score: 76.38  E-value: 4.28e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 207113139    6 SRSDFEWVYTDQPHTQRRKEILAKYPAIKALMRPDPR 42
Cdd:pfam08557   1 SRNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-285 4.25e-17

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: 79.31  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139   68 WLLFWAYAFGGCVNHSLTLAI-HDISHNAAFGTGRAAR--NRWLAVFANLPVGVPYAAsFKKYHVDHHRYLGGDGLDVDv 144
Cdd:pfam00487   2 WLALLLALLLGLFLLGITGSLaHEASHGALFKKRRLNRwlNDLLGRLAGLPLGISYSA-WRIAHLVHHRYTNGPDKDPD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  145 pTRLEGWFFCTPARKLLWLVLQPFFYSLRPLCVHPKAVTRMEVLNTLVQLAADLAIFALW------------------GL 206
Cdd:pfam00487  80 -TAPLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWllllaawlglwlgflglgGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  207 KPVVYLLASSFLGLGLHPISghFVAEHYMFLKG-------HETYSYYGPLNWITFNVGYHVEHHDFPSIPGYNLPLVRKI 279
Cdd:pfam00487 159 LLLLWLLPLLVFGFLLALIF--NYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRR 236


                  ....*.
gi 207113139  280 APEYYD 285
Cdd:pfam00487 237 LREALP 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 ...
 26-314 8.62e-163

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: 455.18  E-value: 8.62e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  26 ILAKYPAIKALMRPDPRLKWAVLVLVLVQMLACWLVRGLAWRWLLFWAYAFGGCVNHSLTLAIHDISHNAAFGTGRAarN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLW--N 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 106 RWLAVFANLPVGVPYAASFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLLWLVLQPFFYSLRPLCVHPKAVTRM 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 186 EVLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHVEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 207113139 265 FPSIPGYNLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYARVKR 314
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKR 288
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 9-314 4.87e-153

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 431.86  E-value: 4.87e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139   9 DFEWVYTDQPHTQRRKEILAKYPAIKALMRPDPRLKWAVLVLVLVQMLACWLVRGLAWRWLLFWAYAFGGCVNHSLTLAI 88
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  89 HDISHNAAFGTGRAarNRWLAVFANLPVGVPYAASFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLLWLVLQPF 168
Cdd:PLN02579  93 HELSHNLAFKTPVY--NRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 169 FYSLRPLCVHPKAVTRMEVLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFVAEHYMFLKGHETYSYYGP 248
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 207113139 249 LNWITFNVGYHVEHHDFPSIPGYNLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYARVKR 314
Cdd:PLN02579 251 LNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKR 316
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
32-285 9.05e-29

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 112.90  E-value: 9.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  32 AIKALMRPDPRLKWAVLVLVLVQMLACWLVrgLAWRWLLFWAYAFGGCVNHSLTLAIHDISHNAAFGTGRAarNRWLAVF 111
Cdd:COG3239   21 RLRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWL--NDLLGRL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 112 ANLPVGVPYAAsFKKYHVDHHRYLGGDGLDVDVPTRLEGWFFCTPARKLL--WLVLQPFFYSLRP---LCVHPKAVTRME 186
Cdd:COG3239   97 LGLPLGTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLAldfLPLRGRLELKER 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 187 VLNTLVQLAADLAIFALWGLKPVVYLLASSFLGLGLHPISGHFV--AEHYMFLKGHE----------TYSYYGPLNWITF 254
Cdd:COG3239  176 RLEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLRfyLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFG 255

                        250       260       270
                 ....*....|....*....|....*....|.
gi 207113139 255 NVGYHVEHHDFPSIPGYNLPLVRKIAPEYYD 285
Cdd:COG3239  256 NLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 6-42 4.28e-18

Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling molecules involved in many different cellular functions in eukaryotes. Sphingolipid delta 4-desaturase catalyzes the formation of (E)-sphing-4-enine. Some proteins in this family have bifunctional delta 4-desaturase/C-4-hydroxylase activity. Delta 4-desaturated sphingolipids may play a role in early signalling required for entry into meiotic and spermatid differentiation pathways during Drosophila spermatogenesis. This small domain associates with FA_desaturase pfam00487 and appears to be specific to sphingolipid delta 4-desaturase.


Pssm-ID: 462517  Cd Length: 37  Bit Score: 76.38  E-value: 4.28e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 207113139    6 SRSDFEWVYTDQPHTQRRKEILAKYPAIKALMRPDPR 42
Cdd:pfam08557   1 SRNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-285 4.25e-17

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: 79.31  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139   68 WLLFWAYAFGGCVNHSLTLAI-HDISHNAAFGTGRAAR--NRWLAVFANLPVGVPYAAsFKKYHVDHHRYLGGDGLDVDv 144
Cdd:pfam00487   2 WLALLLALLLGLFLLGITGSLaHEASHGALFKKRRLNRwlNDLLGRLAGLPLGISYSA-WRIAHLVHHRYTNGPDKDPD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  145 pTRLEGWFFCTPARKLLWLVLQPFFYSLRPLCVHPKAVTRMEVLNTLVQLAADLAIFALW------------------GL 206
Cdd:pfam00487  80 -TAPLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWllllaawlglwlgflglgGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  207 KPVVYLLASSFLGLGLHPISghFVAEHYMFLKG-------HETYSYYGPLNWITFNVGYHVEHHDFPSIPGYNLPLVRKI 279
Cdd:pfam00487 159 LLLLWLLPLLVFGFLLALIF--NYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRR 236


                  ....*.
gi 207113139  280 APEYYD 285
Cdd:pfam00487 237 LREALP 242
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 54-279 1.48e-08

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: 53.44  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  54 QMLACWLVRGLAWRWLLFW-AYAFGGCVNHSLTLAIHDISHnaafgtGRAARNRWL-----AVFANLPVGVPYAAsFKKY 127
Cdd:cd03510    4 VIAAAVALALAWPNWLAYLlAVLLIGARQRALAILMHDAAH------GLLFRNRRLndflgNWLAAVPIFQSLAA-YRRS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 128 HVDHHRYLGGDgLDVDVPTRLEGWFfctparkLLWLVLQPFFYSLRPLCVHP--KAVTRMEVLNTLVQLAADLAIFalwg 205
Cdd:cd03510   77 HLKHHRHLGTE-DDPDLALYLLLWL-------VPLLTVFPLIGRIREIAEHAgvPADEDPDARNTRTTFGGWIERL---- 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 207113139 206 lkpvvyllassflglglhpisghFVAEHymflkghetysyygplnwitfNVGYHVEHHDFPSIPGYNLPLVRKI 279
Cdd:cd03510  145 -----------------------LFAPH---------------------NINYHLEHHLFPAVPFYNLPKAHRI 174
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 68-145 3.13e-08

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: 51.32  E-value: 3.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 207113139  68 WLLFWAYAFGGCVnhSLTLAIHDISHNAAFGTGRAarNRWLAVFANLPVGVPYAaSFKKYHVDHHRYLGGDGLDVDVP 145
Cdd:cd01060    1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRSRWL--NRLLGALLGLALGGSYG-WWRRSHRRHHRYTNTPGKDPDSA 73
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 89-284 2.10e-07

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: 50.72  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  89 HDISHNAAFGTGRAarNRWLAVFANLPVGVPYAaSFKKYHVDHHRYLGGDGLDVDVPT----RLEGWFFCTPARKLLWLV 164
Cdd:cd03506   19 HDAGHGQVFKNRWL--NKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTlpllARSEPAFGKDQKKRFLHR 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 165 LQPFFYSLrplcvhpkavtrmevlntlvqLAADLAIFALwglkpVVYLLASSFLGLGLHPisGHFVAEHYmFLKGHETYS 244
Cdd:cd03506   96 YQHFYFFP---------------------LLALLLLAFL-----VVQLAGGLWLAVVFQL--NHFGMPVE-DPPGESKND 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 207113139 245 YY-----------GP--LNWITFNVGYHVEHHDFPSIPGYNL----PLVRKIAPEYY 284
Cdd:cd03506  147 WLerqvlttrnitGSpfLDWLHGGLNYQIEHHLFPTMPRHNYpkvaPLVRELCKKHG 203
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 56-273 2.52e-04

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: 41.83  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  56 LACWLVRGLAWRWLLFWAYAFGGCVNHSLTLAIHDISHNAAFGTGRAarNRWLAVFANLPVGVPYAaSFKKYHVDHHRYL 135
Cdd:cd03507   19 LLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRL--NDIVGHILHSPLLVPYH-SWRISHNRHHAHT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 136 GGDGLDVD-VPTRLE---GWFFCTPARKLLWLVLQPFFYSLRPLcvhpkavtrmeVLNTLVQLAADLAIFALWgLKPVVY 211
Cdd:cd03507   96 GNLEGDEVwVPVTEEeyaELPKRLPYRLYRNPFLMLSLGWPYYL-----------LLNVLLYYLIPYLVVNAW-LVLITY 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 207113139 212 LLASsflglglHPISGHFVAEHYMFLKGHET----YSYYGPLNWITFNVGYHVEHHDFPSIPGYNL 273
Cdd:cd03507  164 LQHT-------FPDIPWYRADEWNFAQAGLLgtvdRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 66-274 2.73e-04

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: 41.58  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  66 WRWLLFWAYAFGGCVNHSLTLAIHDISHNAAfgtgraARNRWLAVF----ANLPVGVPYAAsFKKYHVDHHRYLGGDGLD 141
Cdd:cd03514   20 SYLPLWVCFILNTLSLHLAGTVIHDASHKAA------SRNRWINELighvSAFFLGFPFPV-FRRVHMQHHAHTNDPEKD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 142 VDVPTrlegwffctparkLLWLVLQPFFYSLrplcvhpkavtrmevLNTLVQLAADLAIFALWGLKpvvYLLASSFLGLG 221
Cdd:cd03514   93 PDHFL-------------LEWLVARSLFITL---------------LVIAILFGFLWELLNLWFLP---ALIVGTYLALF 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 207113139 222 LHpisghfVAEHYMFLKGH-ETYSYYGP---LNWITFNVGYHVEHHDFPSIPGYNLP 274
Cdd:cd03514  142 FD------WLPHHPFEETQrWDNSRVYPsklLNPLIMGQNYHLVHHLWPSIPWYRYP 192
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 55-274 4.19e-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: 41.20  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139  55 MLACWLvRGLAWRWLLFWAYAFGGCVNHSLtlaIHDISHNAAFGTGRAarNRWLAVFANLPVGVPYAAsFKKYHVDHHRY 134
Cdd:cd03511   33 ILIAWT-WGSWWALPAFLVYGVLYAALFAR---WHECVHGTAFATRWL--NDAVGQIAGLMILLPPDF-FRWSHARHHRY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 135 LGGDGLDVD-VPTRLEGWffctpaRKLLWLV--LQPFFYSLRPLCVHPKAVTRME-------------VLNTLVQLAADL 198
Cdd:cd03511  106 TQIPGRDPElAVPRPPTL------REYLLALsgLPYWWGKLRTVFRHAFGAVSEAekpfipaeerpkvVREARAMLAVYA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113139 199 AIFAL------------WGLKPVVYLLASSFLGLGLHpisGHFVAEHYMFLKGHETYSYYgPLNWITFNVGYHVEHHDFP 266
Cdd:cd03511  180 GLIALslylgspllvlvWGLPLLLGQPILRLFLLAEH---GGCPEDANDLRNTRTTLTNP-PLRFLYWNMPYHAEHHMYP 255


                 ....*...
gi 207113139 267 SIPGYNLP 274
Cdd:cd03511  256 SVPFHALP 263
 
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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