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Conserved domains on  [gi|4505193|ref|NP_003667|]
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sphingolipid delta(4)-desaturase DES1 isoform 1 [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 ...
 26-315 5.54e-177

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: 491.00  E-value: 5.54e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   26 ILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGncKAMWN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  106 RWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYL 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  186 EVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4505193  265 FPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRH 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 6-42 1.80e-19

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: 79.85  E-value: 1.80e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4505193      6 SREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPN 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 ...
 26-315 5.54e-177

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: 491.00  E-value: 5.54e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   26 ILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGncKAMWN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  106 RWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYL 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  186 EVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4505193  265 FPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRH 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 5-314 2.36e-163

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 458.05  E-value: 2.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193     5 VSREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSM 84
Cdd:PLN02579   9 VMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193    85 TLAIHEIAHNAAFGNckAMWNRWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVI 164
Cdd:PLN02579  89 FLAIHELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   165 LQPLFYAFRPLFINPKPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYS 244
Cdd:PLN02579 167 LQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYS 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   245 YYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKR 314
Cdd:PLN02579 247 YYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKR 316
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
15-285 2.51e-23

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 97.88  E-value: 2.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   15 TDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVkdLDWKWVIFGAYAFGSCINHSMTLAIHEIAHN 94
Cdd:COG3239   4 ATPLTPADEAELRALRARLRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   95 AAFGNckAMWNRWFGMFANLPIGIPYSIsFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFI--WVILQPLFYAF 172
Cdd:COG3239  82 SLFRS--RWLNDLLGRLLGLPLGTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  173 RPLFINP------KPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHpISGHFIAEHYMFLKGHE----- 241
Cdd:COG3239 159 LALDFLPlrgrleLKERRLEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLL-LGLRFYLEHRGEDTGDGeyrdq 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 4505193  242 -----TYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYD 285
Cdd:COG3239 238 llgsrNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 6-42 1.80e-19

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: 79.85  E-value: 1.80e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4505193      6 SREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPN 42
Cdd:pfam08557   1 SRNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-292 1.55e-16

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: 77.77  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193     68 WVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAM--WNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLGADGVDVDIP 145
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNrwLNDLLGRLAGLPLGISYS-AWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193    146 T---DFEGWF-----FCTAFRKFIWVILQPLFYAFRPLFINPKPI-------TYLEVINTVAQVTFDILIYYFLGIKSLV 210
Cdd:pfam00487  82 PlasRFRGLLryllrWLLGLLVLAWLLALVLPLWLRRLARRKRPIksrrrrwRLIAWLLLLAAWLGLWLGFLGLGGLLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193    211 YMLAASLLGLGLHPISGHFIAEHYMFLKGHE------TYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLV-RKIAAEY 283
Cdd:pfam00487 162 LWLLPLLVFGFLLALIFNYLEHYGGDWGERPvettrsIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLhRRLREAL 241


                  ....*....
gi 4505193    284 YDNLPHYNS 292
Cdd:pfam00487 242 PEHGLPYRS 250
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
 26-315 5.54e-177

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: 491.00  E-value: 5.54e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   26 ILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGncKAMWN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  106 RWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYL 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  186 EVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4505193  265 FPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRH 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 5-314 2.36e-163

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 458.05  E-value: 2.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193     5 VSREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSM 84
Cdd:PLN02579   9 VMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193    85 TLAIHEIAHNAAFGNckAMWNRWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVI 164
Cdd:PLN02579  89 FLAIHELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   165 LQPLFYAFRPLFINPKPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYS 244
Cdd:PLN02579 167 LQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYS 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   245 YYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKR 314
Cdd:PLN02579 247 YYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKR 316
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
15-285 2.51e-23

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 97.88  E-value: 2.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   15 TDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVkdLDWKWVIFGAYAFGSCINHSMTLAIHEIAHN 94
Cdd:COG3239   4 ATPLTPADEAELRALRARLRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   95 AAFGNckAMWNRWFGMFANLPIGIPYSIsFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFI--WVILQPLFYAF 172
Cdd:COG3239  82 SLFRS--RWLNDLLGRLLGLPLGTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  173 RPLFINP------KPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHpISGHFIAEHYMFLKGHE----- 241
Cdd:COG3239 159 LALDFLPlrgrleLKERRLEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLL-LGLRFYLEHRGEDTGDGeyrdq 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 4505193  242 -----TYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYD 285
Cdd:COG3239 238 llgsrNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 6-42 1.80e-19

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: 79.85  E-value: 1.80e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4505193      6 SREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPN 42
Cdd:pfam08557   1 SRNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-292 1.55e-16

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: 77.77  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193     68 WVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAM--WNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLGADGVDVDIP 145
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNrwLNDLLGRLAGLPLGISYS-AWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193    146 T---DFEGWF-----FCTAFRKFIWVILQPLFYAFRPLFINPKPI-------TYLEVINTVAQVTFDILIYYFLGIKSLV 210
Cdd:pfam00487  82 PlasRFRGLLryllrWLLGLLVLAWLLALVLPLWLRRLARRKRPIksrrrrwRLIAWLLLLAAWLGLWLGFLGLGGLLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193    211 YMLAASLLGLGLHPISGHFIAEHYMFLKGHE------TYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLV-RKIAAEY 283
Cdd:pfam00487 162 LWLLPLLVFGFLLALIFNYLEHYGGDWGERPvettrsIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLhRRLREAL 241


                  ....*....
gi 4505193    284 YDNLPHYNS 292
Cdd:pfam00487 242 PEHGLPYRS 250
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 68-148 1.01e-10

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: 58.25  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   68 WVIFGAYAFGSCInhSMTLAIHEIAHNAAFGNckAMWNRWFGMFANLPIGIPYsISFKRYHMDHHRYLGADGVDVDIPTD 147
Cdd:cd01060   1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRS--RWLNRLLGALLGLALGGSY-GWWRRSHRRHHRYTNTPGKDPDSAVN 75


                .
gi 4505193  148 F 148
Cdd:cd01060  76 Y 76
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 89-284 3.89e-06

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: 46.87  E-value: 3.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   89 HEIAHNAAFGNCKamWNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPL 168
Cdd:cd03506  19 HDAGHGQVFKNRW--LNKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTLPLLARSEPAFGKDQKKRFLHR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  169 FYAFrpLFInpkPITYLEVI-NTVAQ-VTFDILIYYFLGikslvymlaasllglglhpisGHFIAEHYmFLKGHETYSYY 246
Cdd:cd03506  96 YQHF--YFF---PLLALLLLaFLVVQlAGGLWLAVVFQL---------------------NHFGMPVE-DPPGESKNDWL 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4505193  247 -----------GP--LNLLTFNVGYHNEHHDFPNIPGKSL----PLVRKIAAEYY 284
Cdd:cd03506 149 erqvlttrnitGSpfLDWLHGGLNYQIEHHLFPTMPRHNYpkvaPLVRELCKKHG 203
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 89-269 3.11e-03

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: 38.36  E-value: 3.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193   89 HEIAHNAAFGNCKamWNRWFGMFANLPIGIPYSiSFKRYHMDHHRYLG-ADGVDVDIPT---DFEGWFFCTAFRKFIWVI 164
Cdd:cd03507  52 HDCGHGSFSDNRR--LNDIVGHILHSPLLVPYH-SWRISHNRHHAHTGnLEGDEVWVPVteeEYAELPKRLPYRLYRNPF 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505193  165 LQPLFYAFRPLFINpkpitylevintVAQVTFDILIYYFLGIKSLVYMLAAsllglglHPISGHFIAEHYMFLKG--HET 242
Cdd:cd03507 129 LMLSLGWPYYLLLN------------VLLYYLIPYLVVNAWLVLITYLQHT-------FPDIPWYRADEWNFAQAglLGT 189

                       170       180
                ....*....|....*....|....*....
gi 4505193  243 --YSYYGPLNLLTFNVGYHNEHHDFPNIP 269
Cdd:cd03507 190 vdRDYGGWLNWLTHIIGTHVAHHLFPRIP 218
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 82-138 8.63e-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: 36.49  E-value: 8.63e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4505193   82 HSMTLAIHEIAHNAAFGNCKamWNRWFG-MFANLPIGIPYSiSFKRYHMDHHRYLGAD 138
Cdd:cd03510  33 RALAILMHDAAHGLLFRNRR--LNDFLGnWLAAVPIFQSLA-AYRRSHLKHHRHLGTE 87
 
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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