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Conserved domains on  [gi|19113199|ref|NP_596407|]
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dihydroceramide delta-4 desaturase [Schizosaccharomyces pombe]

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 ...
 45-346 1.22e-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: 454.02  E-value: 1.22e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  45 ILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLlsWKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYN 124
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSW--WKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 125 RAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLM 204
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 205 HFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTRtrliasgpgkeTPLETFSYYGPLNFFV 284
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTG-----------KGQETYSYYGPLNLLT 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113199 285 YNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRK 346
Cdd:cd03508 228 FNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 27-61 8.30e-17

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: 72.91  E-value: 8.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19113199    27 HQFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPL 61
Cdd:pfam08557   3 NDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 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 ...
 45-346 1.22e-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: 454.02  E-value: 1.22e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  45 ILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLlsWKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYN 124
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSW--WKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 125 RAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLM 204
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 205 HFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTRtrliasgpgkeTPLETFSYYGPLNFFV 284
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTG-----------KGQETYSYYGPLNLLT 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113199 285 YNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRK 346
Cdd:cd03508 228 FNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 28-351 9.95e-134

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 384.48  E-value: 9.95e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199   28 QFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLLSWkfFLTAYFIGAFCNQNLFL 107
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKI--LLVAYFFGGFLNHNLFL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  108 AIHELSHNLGFKKTLYNRAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLL 187
Cdd:PLN02579  91 AIHELSHNLAFKTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  188 FYAFRPLVVRRLPFTLMHFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTrtrliasgPGK 267
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFN--------PGQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  268 etplETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRKQ 347
Cdd:PLN02579 243 ----ETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRKP 318


                 ....
gi 19113199  348 KHAD 351
Cdd:PLN02579 319 PKKS 322
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
90-316 3.28e-17

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 81.31  E-value: 3.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  90 FFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNRAYCLFANLPVGAPFAAsFRPYHMEHHAYQGVDGMDTDLPTRAEL 169
Cdd:COG3239  56 LALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQA 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 170 ---------ILFDNVLGKAFFCTFQLLFYAF--RPLVVRRLPFTLMHFWNIIVQFSFDYLvvrYVGWR-ALAYFFMSSFL 237
Cdd:COG3239 135 wrplylfqhLLRFFLLGLGGLYWLLALDFLPlrGRLELKERRLEALLLLLFLAALLALLL---ALGWWaVLLFWLLPLLV 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 238 AGSLhpTAGHFLSEHYNMTrtrliASGPGKETPLET---FSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVRELAPEF 314
Cdd:COG3239 212 AGLL--LGLRFYLEHRGED-----TGDGEYRDQLLGsrnIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKEL 284


                ..
gi 19113199 315 YD 316
Cdd:COG3239 285 CP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 27-61 8.30e-17

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: 72.91  E-value: 8.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19113199    27 HQFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPL 61
Cdd:pfam08557   3 NDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 88-316 4.47e-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: 77.00  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199    88 WKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNR----AYCLFANLPVGAPFAAsFRPYHMEHHAYQGVDGMDTDL 163
Cdd:pfam00487   2 WLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlndLLGRLAGLPLGISYSA-WRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199   164 PTRAE---------------LILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLMHFWNIIVQFSFDYLVVRYVGWRAL 228
Cdd:pfam00487  81 APLASrfrgllryllrwllgLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199   229 AYFFMSSFLAGSLHPTAGHFLSEHYNMTRTRLIasgpgkETPLETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVR 308
Cdd:pfam00487 161 LLWLLPLLVFGFLLALIFNYLEHYGGDWGERPV------ETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLH 234


                  ....*...
gi 19113199   309 ELAPEFYD 316
Cdd:pfam00487 235 RRLREALP 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 ...
 45-346 1.22e-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: 454.02  E-value: 1.22e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  45 ILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLlsWKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYN 124
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSW--WKILLVAYFFGGTINHSLFLAIHEISHNLAFGKPLWN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 125 RAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLM 204
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 205 HFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTRtrliasgpgkeTPLETFSYYGPLNFFV 284
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTG-----------KGQETYSYYGPLNLLT 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113199 285 YNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRK 346
Cdd:cd03508 228 FNVGYHNEHHDFPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
 28-351 9.95e-134

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 384.48  E-value: 9.95e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199   28 QFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLLSWkfFLTAYFIGAFCNQNLFL 107
Cdd:PLN02579  13 DFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKI--LLVAYFFGGFLNHNLFL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  108 AIHELSHNLGFKKTLYNRAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLL 187
Cdd:PLN02579  91 AIHELSHNLAFKTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFLQLF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  188 FYAFRPLVVRRLPFTLMHFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTrtrliasgPGK 267
Cdd:PLN02579 171 FYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFN--------PGQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  268 etplETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRKQ 347
Cdd:PLN02579 243 ----ETYSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRKP 318


                 ....
gi 19113199  348 KHAD 351
Cdd:PLN02579 319 PKKS 322
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
90-316 3.28e-17

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 81.31  E-value: 3.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  90 FFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNRAYCLFANLPVGAPFAAsFRPYHMEHHAYQGVDGMDTDLPTRAEL 169
Cdd:COG3239  56 LALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRLLGLPLGTPYDA-WRRSHNRHHAYTNDPGKDPDIGYGVQA 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 170 ---------ILFDNVLGKAFFCTFQLLFYAF--RPLVVRRLPFTLMHFWNIIVQFSFDYLvvrYVGWR-ALAYFFMSSFL 237
Cdd:COG3239 135 wrplylfqhLLRFFLLGLGGLYWLLALDFLPlrGRLELKERRLEALLLLLFLAALLALLL---ALGWWaVLLFWLLPLLV 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 238 AGSLhpTAGHFLSEHYNMTrtrliASGPGKETPLET---FSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVRELAPEF 314
Cdd:COG3239 212 AGLL--LGLRFYLEHRGED-----TGDGEYRDQLLGsrnIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKEL 284


                ..
gi 19113199 315 YD 316
Cdd:COG3239 285 CP 286
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
 27-61 8.30e-17

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: 72.91  E-value: 8.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19113199    27 HQFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPL 61
Cdd:pfam08557   3 NDFYWTYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 88-316 4.47e-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: 77.00  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199    88 WKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNR----AYCLFANLPVGAPFAAsFRPYHMEHHAYQGVDGMDTDL 163
Cdd:pfam00487   2 WLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRwlndLLGRLAGLPLGISYSA-WRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199   164 PTRAE---------------LILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLMHFWNIIVQFSFDYLVVRYVGWRAL 228
Cdd:pfam00487  81 APLASrfrgllryllrwllgLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199   229 AYFFMSSFLAGSLHPTAGHFLSEHYNMTRTRLIasgpgkETPLETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVR 308
Cdd:pfam00487 161 LLWLLPLLVFGFLLALIFNYLEHYGGDWGERPV------ETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLH 234


                  ....*...
gi 19113199   309 ELAPEFYD 316
Cdd:pfam00487 235 RRLREALP 242
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 91-164 1.80e-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: 1.80e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113199  91 FLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNRAYCLFANLPVGAPFaASFRPYHMEHHAYQGVDGMDTDLP 164
Cdd:cd01060   1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSY-GWWRRSHRRHHRYTNTPGKDPDSA 73
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 91-315 3.02e-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: 50.33  E-value: 3.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  91 FLTAYFIGAFCNQNLFLAiHELSHNLGFKKTLYNRAYCLFANLPVGAPfAASFRPYHMEHHAYQGVDGMDTDLPTraeli 170
Cdd:cd03506   1 LLLAILLGLFWAQGGFLA-HDAGHGQVFKNRWLNKLLGLTVGNLLGAS-AGWWKNKHNVHHAYTNILGHDPDIDT----- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 171 lfdnvlgkaffctfqLLFYAFRPLVVRRLPFtlmHFWNIIVQFSFDYLvvryVGWRALAYFFMSSFLAGslHPTAGHFLS 250
Cdd:cd03506  74 ---------------LPLLARSEPAFGKDQK---KRFLHRYQHFYFFP----LLALLLLAFLVVQLAGG--LWLAVVFQL 129

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113199 251 EHYNMTRTRLiaSGPGKETPLE-----TFSYYGP--LNFFVYNAGYHIEHHDFPYVAWTRIGK----VRELAPEFY 315
Cdd:cd03506 130 NHFGMPVEDP--PGESKNDWLErqvltTRNITGSpfLDWLHGGLNYQIEHHLFPTMPRHNYPKvaplVRELCKKHG 203
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 88-307 9.28e-04

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: 39.57  E-value: 9.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199  88 WKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNRAYC-LFANLPVGAPFAAsFRPYHMEHHAYQGVDgMDTDLptr 166
Cdd:cd03510  18 WLAYLLAVLLIGARQRALAILMHDAAHGLLFRNRRLNDFLGnWLAAVPIFQSLAA-YRRSHLKHHRHLGTE-DDPDL--- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113199 167 aelilfdnvlgkAFFCTFQLLFYAFRPLVVRRlpftlmhfwniivqfsfdylvvryvgWRALAyffmssflagslhptag 246
Cdd:cd03510  93 ------------ALYLLLWLVPLLTVFPLIGR--------------------------IREIA----------------- 117

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113199 247 hflsEHYNMTRTRliaSGPGKETPLETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKV 307
Cdd:cd03510 118 ----EHAGVPADE---DPDARNTRTTFGGWIERLLFAPHNINYHLEHHLFPAVPFYNLPKA 171
 
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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