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Conserved domains on  [gi|27754029|ref|NP_081575|]
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sphingolipid delta(4)-desaturase/C4-monooxygenase DES2 isoform 1 [Mus musculus]

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 6.63e-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: 455.57  E-value: 6.63e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  26 MLAKYPAIKALMRPDPHIKWTVSGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTScvSRN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKP--LWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 106 RWFAIFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLLWLVLQPFFYSLRPLCVNPKVVTRM 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 186 EILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHMEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27754029 265 FPSIPGYYLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSMGPYSRVKRK 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 7-42 2.33e-16

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: 71.37  E-value: 2.33e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 27754029     7 RSDFEWVYSDQPHTQRRKEMLAKYPAIKALMRPDPH 42
Cdd:pfam08557   2 RNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 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 6.63e-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: 455.57  E-value: 6.63e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  26 MLAKYPAIKALMRPDPHIKWTVSGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTScvSRN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKP--LWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 106 RWFAIFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLLWLVLQPFFYSLRPLCVNPKVVTRM 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 186 EILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHMEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27754029 265 FPSIPGYYLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSMGPYSRVKRK 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 9-315 1.44e-148

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 420.30  E-value: 1.44e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029    9 DFEWVYSDQPHTQRRKEMLAKYPAIKALMRPDPHIKWTVSGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAI 88
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029   89 HDISHNTAFGTscVSRNRWFAIFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLLWLVLQPF 168
Cdd:PLN02579  93 HELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  169 FYSLRPLCVNPKVVTRMEILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHPISGHFVAEHYMFLKGHETYSYYGP 248
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27754029  249 LNWITFNVGYHMEHHDFPSIPGYYLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSMGPYSRVKRK 315
Cdd:PLN02579 251 LNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
32-285 4.93e-25

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 102.50  E-value: 4.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  32 AIKALMRPDPHIKWTVSGMVLVQVLACWLVrgLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTSCVsrNRWFAIF 111
Cdd:COG3239  21 RLRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWL--NDLLGRL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 112 ANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLL--WLVLQPFFYSLRP---LCVNPKVVTRME 186
Cdd:COG3239  97 LGLPLGTPY-DAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLAldfLPLRGRLELKER 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 187 ILNALVQLAFDVTIFA-LWGIKPIVYLLGSSLLGLGLHPISGH-FVAEHYMFLKGHE----------TYSYYGPLNWITF 254
Cdd:COG3239 176 RLEALLLLLFLAALLAlLLALGWWAVLLFWLLPLLVAGLLLGLrFYLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFG 255

                       250       260       270
                ....*....|....*....|....*....|.
gi 27754029 255 NVGYHMEHHDFPSIPGYYLPLVRKIAPEYYD 285
Cdd:COG3239 256 NLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 7-42 2.33e-16

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: 71.37  E-value: 2.33e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 27754029     7 RSDFEWVYSDQPHTQRRKEMLAKYPAIKALMRPDPH 42
Cdd:pfam08557   2 RNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-285 3.27e-14

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: 71.22  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029    68 WLLFW-AYAFGGCINHSLTLAIHDISHNTAFGTSCVSR--NRWFAIFANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDI 144
Cdd:pfam00487   2 WLALLlALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlNDLLGRLAGLPLGISY-SAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029   145 PTNFegWFFCTPARKLLWLVLQPFFYSLRPLCVNPKVVTRMEILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHP 224
Cdd:pfam00487  81 APLA--SRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029   225 ISGHFV----------------AEHYMFLKG-------HETYSYYGPLNWITFNVGYHMEHHDFPSIPGYYLPLVRKIAP 281
Cdd:pfam00487 159 LLLLWLlpllvfgfllalifnyLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLR 238


                  ....
gi 27754029   282 EYYD 285
Cdd:pfam00487 239 EALP 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 ...
 26-315 6.63e-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: 455.57  E-value: 6.63e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  26 MLAKYPAIKALMRPDPHIKWTVSGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTScvSRN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKP--LWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 106 RWFAIFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLLWLVLQPFFYSLRPLCVNPKVVTRM 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 186 EILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHMEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27754029 265 FPSIPGYYLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSMGPYSRVKRK 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 9-315 1.44e-148

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 420.30  E-value: 1.44e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029    9 DFEWVYSDQPHTQRRKEMLAKYPAIKALMRPDPHIKWTVSGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAI 88
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029   89 HDISHNTAFGTscVSRNRWFAIFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLLWLVLQPF 168
Cdd:PLN02579  93 HELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  169 FYSLRPLCVNPKVVTRMEILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHPISGHFVAEHYMFLKGHETYSYYGP 248
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27754029  249 LNWITFNVGYHMEHHDFPSIPGYYLPLVRKIAPEYYDHLPQHHSWVKVLWDFVFEDSMGPYSRVKRK 315
Cdd:PLN02579 251 LNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
32-285 4.93e-25

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 102.50  E-value: 4.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  32 AIKALMRPDPHIKWTVSGMVLVQVLACWLVrgLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTSCVsrNRWFAIF 111
Cdd:COG3239  21 RLRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWL--NDLLGRL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 112 ANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDIPTNFEGWFFCTPARKLL--WLVLQPFFYSLRP---LCVNPKVVTRME 186
Cdd:COG3239  97 LGLPLGTPY-DAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLAldfLPLRGRLELKER 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 187 ILNALVQLAFDVTIFA-LWGIKPIVYLLGSSLLGLGLHPISGH-FVAEHYMFLKGHE----------TYSYYGPLNWITF 254
Cdd:COG3239 176 RLEALLLLLFLAALLAlLLALGWWAVLLFWLLPLLVAGLLLGLrFYLEHRGEDTGDGeyrdqllgsrNIRGGRLLRWLFG 255

                       250       260       270
                ....*....|....*....|....*....|.
gi 27754029 255 NVGYHMEHHDFPSIPGYYLPLVRKIAPEYYD 285
Cdd:COG3239 256 NLNYHIEHHLFPSIPWYRLPEAHRILKELCP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 7-42 2.33e-16

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: 71.37  E-value: 2.33e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 27754029     7 RSDFEWVYSDQPHTQRRKEMLAKYPAIKALMRPDPH 42
Cdd:pfam08557   2 RNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-285 3.27e-14

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: 71.22  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029    68 WLLFW-AYAFGGCINHSLTLAIHDISHNTAFGTSCVSR--NRWFAIFANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDI 144
Cdd:pfam00487   2 WLALLlALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlNDLLGRLAGLPLGISY-SAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029   145 PTNFegWFFCTPARKLLWLVLQPFFYSLRPLCVNPKVVTRMEILNALVQLAFDVTIFALWGIKPIVYLLGSSLLGLGLHP 224
Cdd:pfam00487  81 APLA--SRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029   225 ISGHFV----------------AEHYMFLKG-------HETYSYYGPLNWITFNVGYHMEHHDFPSIPGYYLPLVRKIAP 281
Cdd:pfam00487 159 LLLLWLlpllvfgfllalifnyLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLR 238


                  ....
gi 27754029   282 EYYD 285
Cdd:pfam00487 239 EALP 242
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 68-148 1.71e-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: 52.09  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  68 WLLFWAYAFGGCInhSLTLAIHDISHNTAFGTSCVsrNRWFAIFANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDIPTN 147
Cdd:cd01060   1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRSRWL--NRLLGALLGLALGGSY-GWWRRSHRRHHRYTNTPGKDPDSAVN 75


                .
gi 27754029 148 F 148
Cdd:cd01060  76 Y 76
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 54-279 1.41e-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: 47.66  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  54 QVLACWLVRGLSWRWLLFW-AYAFGGCINHSLTLAIHDISHNTAFgtscvsRNRWF-----AIFANLPIGLPYATsFKKY 127
Cdd:cd03510   4 VIAAAVALALAWPNWLAYLlAVLLIGARQRALAILMHDAAHGLLF------RNRRLndflgNWLAAVPIFQSLAA-YRRS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 128 HVDHHRYLGGDgLDVDIptnfeGWFFctparkLLWLVlqpffyslrPLcvnpkvVTRMEILNALVQlafdvtifalwgik 207
Cdd:cd03510  77 HLKHHRHLGTE-DDPDL-----ALYL------LLWLV---------PL------LTVFPLIGRIRE-------------- 115

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27754029 208 pivyllgssllglglhpISGHFVAEHYMFLKGHETYSYYGplNWIT------FNVGYHMEHHDFPSIPGYYLPLVRKI 279
Cdd:cd03510 116 -----------------IAEHAGVPADEDPDARNTRTTFG--GWIErllfapHNINYHLEHHLFPAVPFYNLPKAHRI 174
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 89-284 3.62e-05

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: 44.17  E-value: 3.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  89 HDISHNTAFGTSCVsrNRWFAIFANLPIGLPYAtSFKKYHVDHHRYLGGDGLDVDIPTN----FEGWFFCTPARKLLWLV 164
Cdd:cd03506  19 HDAGHGQVFKNRWL--NKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTLpllaRSEPAFGKDQKKRFLHR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 165 LQPFFYSLrplcvnpkvvtrmeiLNALVQLAFDVTIFALWGIKPIVYLLgssllglglhpisGHFVAEHYmFLKGHETYS 244
Cdd:cd03506  96 YQHFYFFP---------------LLALLLLAFLVVQLAGGLWLAVVFQL-------------NHFGMPVE-DPPGESKND 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27754029 245 YY-----------GP--LNWITFNVGYHMEHHDFPSIPGYYL----PLVRKIAPEYY 284
Cdd:cd03506 147 WLerqvlttrnitGSpfLDWLHGGLNYQIEHHLFPTMPRHNYpkvaPLVRELCKKHG 203
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 47-274 8.89e-05

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: 43.51  E-value: 8.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029  47 VSGMVLVQVLACWlvrglsWRWLLFWAYAFGGCINHSLtlaIHDISHNTAFGTscvsrnRWF----AIFANLPIGLPYaT 122
Cdd:cd03511  30 VSGILIAWTWGSW------WALPAFLVYGVLYAALFAR---WHECVHGTAFAT------RWLndavGQIAGLMILLPP-D 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 123 SFKKYHVDHHRYLGGDGLDVDI----PTNFEGWFFCTPARKLLWLVLQPFFYSLR-----------PLCVNPKVVtrmei 187
Cdd:cd03511  94 FFRWSHARHHRYTQIPGRDPELavprPPTLREYLLALSGLPYWWGKLRTVFRHAFgavseaekpfiPAEERPKVV----- 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27754029 188 LNALVQLAFDVTIFAL------------WGIKPIVYLLGSSLLGLGLHpisGHFVAEHYMFLKGHETYSYYgPLNWITFN 255
Cdd:cd03511 169 REARAMLAVYAGLIALslylgspllvlvWGLPLLLGQPILRLFLLAEH---GGCPEDANDLRNTRTTLTNP-PLRFLYWN 244

                       250
                ....*....|....*....
gi 27754029 256 VGYHMEHHDFPSIPGYYLP 274
Cdd:cd03511 245 MPYHAEHHMYPSVPFHALP 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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