NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|81870179|sp|Q564G3|]
View 

RecName: Full=Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2; AltName: Full=Degenerative spermatocyte homolog 2; AltName: Full=Sphingolipid 4-desaturase; AltName: Full=Sphingolipid C4-monooxygenase

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.02e-161

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: 451.71  E-value: 2.02e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  26 MLAKYPSIKALMRPDPNIKWTVLGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTRCAsrN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLW--N 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 106 RWFAVFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLLWLVLQPFFYSLRPLYVNPKAVTRM 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 186 EILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHVEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 81870179 265 FPSIPGCYLPLVRMIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYSRVKRK 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 7-42 2.66e-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: 2.66e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 81870179     7 RSDFEWVYSDQPHTQRRKEMLAKYPSIKALMRPDPN 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 2.02e-161

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: 451.71  E-value: 2.02e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  26 MLAKYPSIKALMRPDPNIKWTVLGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTRCAsrN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLW--N 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 106 RWFAVFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLLWLVLQPFFYSLRPLYVNPKAVTRM 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 186 EILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHVEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 81870179 265 FPSIPGCYLPLVRMIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYSRVKRK 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 9-315 2.61e-149

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 422.23  E-value: 2.61e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179    9 DFEWVYSDQPHTQRRKEMLAKYPSIKALMRPDPNIKWTVLGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAI 88
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179   89 HDISHNTAFGTrcASRNRWFAVFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLLWLVLQPF 168
Cdd:PLN02579  93 HELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  169 FYSLRPLYVNPKAVTRMEILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFLKGHETYSYYGP 248
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81870179  249 LNWITFNVGYHVEHHDFPSIPGCYLPLVRMIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYSRVKRK 315
Cdd:PLN02579 251 LNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
33-290 2.94e-26

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 105.97  E-value: 2.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  33 IKALMRPDPNIKWTVLGMVLVQVLACWLVrgLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTRCAsrNRWFAVFA 112
Cdd:COG3239  22 LRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWL--NDLLGRLL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 113 NLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLL--WLVLQPFFYSLRPLYVNP---KAVTRMEI 187
Cdd:COG3239  98 GLPLGTPY-DAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLALDFLPlrgRLELKERR 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 188 LNALVQLAFNVTIFAL------------WGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFLKGHETYSYYGPLNWITFN 255
Cdd:COG3239 177 LEALLLLLFLAALLALllalgwwavllfWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRDQLLGSRNIRGGRLLRWLFGN 256

                       250       260       270
                ....*....|....*....|....*....|....*
gi 81870179 256 VGYHVEHHDFPSIPGCYLPlvrMIAPEYYDHLPQH 290
Cdd:COG3239 257 LNYHIEHHLFPSIPWYRLP---EAHRILKELCPEY 288
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 7-42 2.66e-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: 2.66e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 81870179     7 RSDFEWVYSDQPHTQRRKEMLAKYPSIKALMRPDPN 42
Cdd:pfam08557   2 RNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-292 2.93e-15

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


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 74.31  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179    68 WLLFW-AYAFGGCINHSLTLAIHDISHNTAFGTRCASR--NRWFAVFANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDI 144
Cdd:pfam00487   2 WLALLlALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlNDLLGRLAGLPLGISY-SAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179   145 PTDFegWFFCTPARKLLWLVLQPFFYSLRPLYVNPKAVTRMEILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHP 224
Cdd:pfam00487  81 APLA--SRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179   225 ISGHFV----------------AEHYMFLKG-------HETYSYYGPLNWITFNVGYHVEHHDFPSIPGCYLPLV-RMIA 280
Cdd:pfam00487 159 LLLLWLlpllvfgfllalifnyLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLhRRLR 238

                         250
                  ....*....|..
gi 81870179   281 PEYYDHLPQHHS 292
Cdd:pfam00487 239 EALPEHGLPYRS 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 2.02e-161

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: 451.71  E-value: 2.02e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  26 MLAKYPSIKALMRPDPNIKWTVLGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTRCAsrN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLW--N 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 106 RWFAVFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLLWLVLQPFFYSLRPLYVNPKAVTRM 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 186 EILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFL-KGHETYSYYGPLNWITFNVGYHVEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 81870179 265 FPSIPGCYLPLVRMIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYSRVKRK 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 9-315 2.61e-149

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 422.23  E-value: 2.61e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179    9 DFEWVYSDQPHTQRRKEMLAKYPSIKALMRPDPNIKWTVLGMVLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAI 88
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLFLAI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179   89 HDISHNTAFGTrcASRNRWFAVFANLPIGLPYATSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLLWLVLQPF 168
Cdd:PLN02579  93 HELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  169 FYSLRPLYVNPKAVTRMEILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFLKGHETYSYYGP 248
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSYYGP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81870179  249 LNWITFNVGYHVEHHDFPSIPGCYLPLVRMIAPEYYDHLPQHHSWVKVLWDFVFEDSLGPYSRVKRK 315
Cdd:PLN02579 251 LNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
33-290 2.94e-26

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 105.97  E-value: 2.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  33 IKALMRPDPNIKWTVLGMVLVQVLACWLVrgLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTRCAsrNRWFAVFA 112
Cdd:COG3239  22 LRALLGRRDWRYLLKLALTLALLAALWLL--LSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWL--NDLLGRLL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 113 NLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDIPTDFEGWFFCTPARKLL--WLVLQPFFYSLRPLYVNP---KAVTRMEI 187
Cdd:COG3239  98 GLPLGTPY-DAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLYLFQHLLrfFLLGLGGLYWLLALDFLPlrgRLELKERR 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 188 LNALVQLAFNVTIFAL------------WGIKAIVYLLASSLLGLGLHPISGHFVAEHYMFLKGHETYSYYGPLNWITFN 255
Cdd:COG3239 177 LEALLLLLFLAALLALllalgwwavllfWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRDQLLGSRNIRGGRLLRWLFGN 256

                       250       260       270
                ....*....|....*....|....*....|....*
gi 81870179 256 VGYHVEHHDFPSIPGCYLPlvrMIAPEYYDHLPQH 290
Cdd:COG3239 257 LNYHIEHHLFPSIPWYRLP---EAHRILKELCPEY 288
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 7-42 2.66e-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: 2.66e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 81870179     7 RSDFEWVYSDQPHTQRRKEMLAKYPSIKALMRPDPN 42
Cdd:pfam08557   2 RNDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 68-292 2.93e-15

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


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 74.31  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179    68 WLLFW-AYAFGGCINHSLTLAIHDISHNTAFGTRCASR--NRWFAVFANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDI 144
Cdd:pfam00487   2 WLALLlALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlNDLLGRLAGLPLGISY-SAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179   145 PTDFegWFFCTPARKLLWLVLQPFFYSLRPLYVNPKAVTRMEILNALVQLAFNVTIFALWGIKAIVYLLASSLLGLGLHP 224
Cdd:pfam00487  81 APLA--SRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179   225 ISGHFV----------------AEHYMFLKG-------HETYSYYGPLNWITFNVGYHVEHHDFPSIPGCYLPLV-RMIA 280
Cdd:pfam00487 159 LLLLWLlpllvfgfllalifnyLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLhRRLR 238

                         250
                  ....*....|..
gi 81870179   281 PEYYDHLPQHHS 292
Cdd:pfam00487 239 EALPEHGLPYRS 250
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 68-148 1.13e-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: 52.47  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  68 WLLFWAYAFGGCInhSLTLAIHDISHNTAFGTRcaSRNRWFAVFANLPIGLPYaTSFKKYHVDHHRYLGGDGLDVDIPTD 147
Cdd:cd01060   1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRSR--WLNRLLGALLGLALGGSY-GWWRRSHRRHHRYTNTPGKDPDSAVN 75


                .
gi 81870179 148 F 148
Cdd:cd01060  76 Y 76
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 47-274 8.62e-08

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: 52.76  E-value: 8.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  47 VLGMVLVQVLACWlvrglsWRWLLFWAYAFGGCINHSLtlaIHDISHNTAFGTRCAsrNRWFAVFANLPIGLPYaTSFKK 126
Cdd:cd03511  30 VSGILIAWTWGSW------WALPAFLVYGVLYAALFAR---WHECVHGTAFATRWL--NDAVGQIAGLMILLPP-DFFRW 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 127 YHVDHHRYLGGDGLDVDI----PTDFEGWFFCTPARKLLWLVLQPFFYSLRPL-------YVNPKAVTRMeILNALVQLA 195
Cdd:cd03511  98 SHARHHRYTQIPGRDPELavprPPTLREYLLALSGLPYWWGKLRTVFRHAFGAvseaekpFIPAEERPKV-VREARAMLA 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 196 FNVTIFAL------------WGIKAIVYLLASSLLGLGLHpisGHFVAEHYMFLKGHETYSYYgPLNWITFNVGYHVEHH 263
Cdd:cd03511 177 VYAGLIALslylgspllvlvWGLPLLLGQPILRLFLLAEH---GGCPEDANDLRNTRTTLTNP-PLRFLYWNMPYHAEHH 252

                       250
                ....*....|.
gi 81870179 264 DFPSIPGCYLP 274
Cdd:cd03511 253 MYPSVPFHALP 263
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 89-284 4.02e-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: 49.95  E-value: 4.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  89 HDISHNTAFGTRCAsrNRWFAVFANLPIGLPYAtSFKKYHVDHHRYLGGDGLDVDIPTD----FEGWFFCTPARKLLWLV 164
Cdd:cd03506  19 HDAGHGQVFKNRWL--NKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTLpllaRSEPAFGKDQKKRFLHR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 165 LQPFFYSlrPLYvnpkavtrmeilnALVQLAFNVTIFALWGIKAIVYLLassllglglhpisGHFVAEHYmFLKGHETYS 244
Cdd:cd03506  96 YQHFYFF--PLL-------------ALLLLAFLVVQLAGGLWLAVVFQL-------------NHFGMPVE-DPPGESKND 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81870179 245 YY-----------GP--LNWITFNVGYHVEHHDFPSIPGCYL----PLVRMIAPEYY 284
Cdd:cd03506 147 WLerqvlttrnitGSpfLDWLHGGLNYQIEHHLFPTMPRHNYpkvaPLVRELCKKHG 203
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 54-138 5.22e-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: 46.12  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  54 QVLACWLVRGLSWRWLLFW-AYAFGGCINHSLTLAIHDISHNTAFGTRcaSRNRWFA-VFANLPIGLPYATsFKKYHVDH 131
Cdd:cd03510   4 VIAAAVALALAWPNWLAYLlAVLLIGARQRALAILMHDAAHGLLFRNR--RLNDFLGnWLAAVPIFQSLAA-YRRSHLKH 80


                ....*..
gi 81870179 132 HRYLGGD 138
Cdd:cd03510  81 HRHLGTE 87
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 51-269 5.73e-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: 37.59  E-value: 5.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179  51 VLVQVLACWLVRGLSWRWLLFWAYAFGGCINHSLTLAIHDISHNTAFGTRcaSRNRWFAVFANLPIGLPYAtSFKKYHVD 130
Cdd:cd03507  14 ILLLALLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNR--RLNDIVGHILHSPLLVPYH-SWRISHNR 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81870179 131 HHRYLGGDGLDVDIPT----DFEGWFFCTPARKLLWLVLQPFFysLRPLYVnpkavtrmeILNALVQLAFNVTIFALWgI 206
Cdd:cd03507  91 HHAHTGNLEGDEVWVPvteeEYAELPKRLPYRLYRNPFLMLSL--GWPYYL---------LLNVLLYYLIPYLVVNAW-L 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81870179 207 KAIVYLLASsllglglHPISGHFVAEHYMFLKGHET----YSYYGPLNWITFNVGYHVEHHDFPSIP 269
Cdd:cd03507 159 VLITYLQHT-------FPDIPWYRADEWNFAQAGLLgtvdRDYGGWLNWLTHIIGTHVAHHLFPRIP 218
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH