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Conserved domains on  [gi|17540134|ref|NP_501256|]
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Putative sphingolipid delta(4)-desaturase [Caenorhabditis elegans]

Protein Classification

Lipid_DES and Delta4-sphingolipid-FADS-like domain-containing protein (domain architecture ID 10554096)

Lipid_DES and Delta4-sphingolipid-FADS-like domain-containing protein

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 ...
27-316 1.63e-171

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  Cd Length: 289  Bit Score: 478.68  E-value: 1.63e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  27 ILAKYPQIKELFGQDKAFRPVVVCMVIAQIVFAYLLRDSDWLLILFQAYFVSGTINHSLTLAVHEISHNQAFGtnRPLAN 106
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 107 RIFGFIANLPMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTEFEAKVFRTWLGKMIWMSLQPLFYGIRPFMLYPKSMTDL 186
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 187 ELINVAIQLLFSTFIYTQFGAKSFFFLFGGLVLGMGLHPCAGHFVSEHYVF-KKDQETYSYYGPINMVVFNVGYHVEHHD 265
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFtGKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17540134 266 FPYITGSNLPKVREIAPEYYQDWQTHDSWVGMMADFIFNPKMTLRKRIKRK 316
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
7-41 2.33e-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: 312157  Cd Length: 37  Bit Score: 74.47  E-value: 2.33e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 17540134     7 KEEDFSWAYTEEPHASRRKEILAKYPQIKELFGQD 41
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPD 35
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
27-316 1.63e-171

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  Cd Length: 289  Bit Score: 478.68  E-value: 1.63e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  27 ILAKYPQIKELFGQDKAFRPVVVCMVIAQIVFAYLLRDSDWLLILFQAYFVSGTINHSLTLAVHEISHNQAFGtnRPLAN 106
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 107 RIFGFIANLPMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTEFEAKVFRTWLGKMIWMSLQPLFYGIRPFMLYPKSMTDL 186
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 187 ELINVAIQLLFSTFIYTQFGAKSFFFLFGGLVLGMGLHPCAGHFVSEHYVF-KKDQETYSYYGPINMVVFNVGYHVEHHD 265
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFtGKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17540134 266 FPYITGSNLPKVREIAPEYYQDWQTHDSWVGMMADFIFNPKMTLRKRIKRK 316
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
7-316 5.26e-149

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 423.00  E-value: 5.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134    7 KEEDFSWAYTEEPHASRRKEILAKYPQIKELFGQDKAFRPVVVCMVIAQIVFAYLLRDSDWLLILFQAYFVSGTINHSLT 86
Cdd:PLN02579  10 MATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134   87 LAVHEISHNQAFGTnrPLANRIFGFIANLPMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTEFEAKVFRTWLGKMIWMSL 166
Cdd:PLN02579  90 LAIHELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  167 QPLFYGIRPFMLYPKSMTDLELINVAIQLLFSTFIYTQFGAKSFFFLFGGLVLGMGLHPCAGHFVSEHYVFKKDQETYSY 246
Cdd:PLN02579 168 QLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSY 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  247 YGPINMVVFNVGYHVEHHDFPYITGSNLPKVREIAPEYYQDWQTHDSWVGMMADFIFNPKMTLRKRIKRK 316
Cdd:PLN02579 248 YGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
7-41 2.33e-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: 312157  Cd Length: 37  Bit Score: 74.47  E-value: 2.33e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 17540134     7 KEEDFSWAYTEEPHASRRKEILAKYPQIKELFGQD 41
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPD 35
FA_desaturase pfam00487
Fatty acid desaturase;
67-287 2.92e-14

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 71.60  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134    67 WLLILFqaYFVSGTINHSLTLAV-HEISHNQAFGTNRPLANRIFGFIAnLPMCIPMSiSFKKYHLEHHRNLGEDVIDTDV 145
Cdd:pfam00487   1 WLALLL--ALLLGLFLLGILGVLaHEASHGALFRRRNRWLNDLLGLAG-LPLGISYS-AWRIAHLVHHRYTNGPDEDPDT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134   146 PT------EFEAKVFRTWLG--KMIWMSLQPLFYGIRPFMLYPKSMTDLELINVAIQLLFSTFIYTQFGAkSFFFLFGGL 217
Cdd:pfam00487  77 APlasrfrGLLRYLLRWLLGllVLAWLLALLLGLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWL-GFLGLGGLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134   218 VLGMGLHPCAGHFV-------SEHYVFKKDQETY-------SYYGPINMVVFNVGYHVEHHDFPYITGSNLPKVREIAPE 283
Cdd:pfam00487 156 LLLWLLPLLVAGFLlalifnyLEHYGGDWGERPVettrsirSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLRE 235

                  ....
gi 17540134   284 YYQD 287
Cdd:pfam00487 236 ALPE 239
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
21-335 1.58e-09

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 58.26  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  21 ASRRKEILAKYPqiKELFGQDKAFRPVVVCMVIAQIVFAYL---LRDSDWLLILFQAYFvsGTINHSLTLAVHEISHNQA 97
Cdd:COG3239  15 AAPLDSIRARLP--KPRTRRDAIAILITFLALAGLWALLALslaYWPSWWLLPLALLLA--GLLLTGLFSVGHDCGHGSF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  98 FGtnRPLANRIFGFIANLpMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTE------------FEAKVFRTWLGKM---I 162
Cdd:COG3239  91 FK--NRWINDLIGHLAAA-LLLAPPVFWRISHNQHHAHTNILDDDPETYVSypeqlrrgplrfQLIRLPWLAFGFGprwA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 163 WMSLQPLFYGIRPFMLYPKSMTDLELINV-------AIQLLFSTFIYTQFGAKSFFFLFGGLVLG-MGLHPCAGHFVSEH 234
Cdd:COG3239 168 LLHFELLEKLFKRSGKAPKAAALATLLAAiglaallALAFFWGLIPLLLVGLWLVLVLFVHHTFDlLPHHGLEDWQWSDR 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 235 YVFkkdQETYSYYGPI-NMVVFNVGYHVEHHDFPYITGSNLPKV-REIAPEY-YQDWQTHDSWVGMMADFIFnpkmtlrk 311
Cdd:COG3239 248 ALN---ARSNVDAPPLlRFLTGNINYHVEHHLFPDVPWYRLPRAhRLIKEALgERGLTIYTGYREFKLATLW-------- 316
                       330       340
                ....*....|....*....|....
gi 17540134 312 riKRKYAKPDQFSFYGTGPYETSH 335
Cdd:COG3239 317 --QLRGEIFLPKREAPETAGPTRS 338
 
Name Accession Description Interval E-value
Delta4-sphingolipid-FADS-like cd03508
The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the ...
27-316 1.63e-171

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  Cd Length: 289  Bit Score: 478.68  E-value: 1.63e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  27 ILAKYPQIKELFGQDKAFRPVVVCMVIAQIVFAYLLRDSDWLLILFQAYFVSGTINHSLTLAVHEISHNQAFGtnRPLAN 106
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 107 RIFGFIANLPMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTEFEAKVFRTWLGKMIWMSLQPLFYGIRPFMLYPKSMTDL 186
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 187 ELINVAIQLLFSTFIYTQFGAKSFFFLFGGLVLGMGLHPCAGHFVSEHYVF-KKDQETYSYYGPINMVVFNVGYHVEHHD 265
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFtGKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17540134 266 FPYITGSNLPKVREIAPEYYQDWQTHDSWVGMMADFIFNPKMTLRKRIKRK 316
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
7-316 5.26e-149

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 423.00  E-value: 5.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134    7 KEEDFSWAYTEEPHASRRKEILAKYPQIKELFGQDKAFRPVVVCMVIAQIVFAYLLRDSDWLLILFQAYFVSGTINHSLT 86
Cdd:PLN02579  10 MATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNLF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134   87 LAVHEISHNQAFGTnrPLANRIFGFIANLPMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTEFEAKVFRTWLGKMIWMSL 166
Cdd:PLN02579  90 LAIHELSHNLAFKT--PVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVFL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  167 QPLFYGIRPFMLYPKSMTDLELINVAIQLLFSTFIYTQFGAKSFFFLFGGLVLGMGLHPCAGHFVSEHYVFKKDQETYSY 246
Cdd:PLN02579 168 QLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYSY 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  247 YGPINMVVFNVGYHVEHHDFPYITGSNLPKVREIAPEYYQDWQTHDSWVGMMADFIFNPKMTLRKRIKRK 316
Cdd:PLN02579 248 YGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
7-41 2.33e-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: 312157  Cd Length: 37  Bit Score: 74.47  E-value: 2.33e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 17540134     7 KEEDFSWAYTEEPHASRRKEILAKYPQIKELFGQD 41
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPD 35
FA_desaturase pfam00487
Fatty acid desaturase;
67-287 2.92e-14

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 71.60  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134    67 WLLILFqaYFVSGTINHSLTLAV-HEISHNQAFGTNRPLANRIFGFIAnLPMCIPMSiSFKKYHLEHHRNLGEDVIDTDV 145
Cdd:pfam00487   1 WLALLL--ALLLGLFLLGILGVLaHEASHGALFRRRNRWLNDLLGLAG-LPLGISYS-AWRIAHLVHHRYTNGPDEDPDT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134   146 PT------EFEAKVFRTWLG--KMIWMSLQPLFYGIRPFMLYPKSMTDLELINVAIQLLFSTFIYTQFGAkSFFFLFGGL 217
Cdd:pfam00487  77 APlasrfrGLLRYLLRWLLGllVLAWLLALLLGLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWL-GFLGLGGLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134   218 VLGMGLHPCAGHFV-------SEHYVFKKDQETY-------SYYGPINMVVFNVGYHVEHHDFPYITGSNLPKVREIAPE 283
Cdd:pfam00487 156 LLLWLLPLLVAGFLlalifnyLEHYGGDWGERPVettrsirSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLRE 235

                  ....
gi 17540134   284 YYQD 287
Cdd:pfam00487 236 ALPE 239
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
21-335 1.58e-09

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 58.26  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  21 ASRRKEILAKYPqiKELFGQDKAFRPVVVCMVIAQIVFAYL---LRDSDWLLILFQAYFvsGTINHSLTLAVHEISHNQA 97
Cdd:COG3239  15 AAPLDSIRARLP--KPRTRRDAIAILITFLALAGLWALLALslaYWPSWWLLPLALLLA--GLLLTGLFSVGHDCGHGSF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  98 FGtnRPLANRIFGFIANLpMCIPMSISFKKYHLEHHRNLGEDVIDTDVPTE------------FEAKVFRTWLGKM---I 162
Cdd:COG3239  91 FK--NRWINDLIGHLAAA-LLLAPPVFWRISHNQHHAHTNILDDDPETYVSypeqlrrgplrfQLIRLPWLAFGFGprwA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 163 WMSLQPLFYGIRPFMLYPKSMTDLELINV-------AIQLLFSTFIYTQFGAKSFFFLFGGLVLG-MGLHPCAGHFVSEH 234
Cdd:COG3239 168 LLHFELLEKLFKRSGKAPKAAALATLLAAiglaallALAFFWGLIPLLLVGLWLVLVLFVHHTFDlLPHHGLEDWQWSDR 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 235 YVFkkdQETYSYYGPI-NMVVFNVGYHVEHHDFPYITGSNLPKV-REIAPEY-YQDWQTHDSWVGMMADFIFnpkmtlrk 311
Cdd:COG3239 248 ALN---ARSNVDAPPLlRFLTGNINYHVEHHLFPDVPWYRLPRAhRLIKEALgERGLTIYTGYREFKLATLW-------- 316
                       330       340
                ....*....|....*....|....
gi 17540134 312 riKRKYAKPDQFSFYGTGPYETSH 335
Cdd:COG3239 317 --QLRGEIFLPKREAPETAGPTRS 338
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
69-146 5.28e-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: 50.55  E-value: 5.28e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17540134  69 LILFQAYFVSGTInhSLTLAVHEISHNQAFGTNRPlaNRIFGFIANLPMCIPmSISFKKYHLEHHRNLGEDVIDTDVP 146
Cdd:cd01060   1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRSRWL--NRLLGALLGLALGGS-YGWWRRSHRRHHRYTNTPGKDPDSA 73
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
74-285 2.14e-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  Cd Length: 204  Bit Score: 44.55  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  74 AYFVSGTINHSLTLAVHEISHNQAFGTnrPLANRIFGFIANLPMCIPMSiSFKKYHLEHHRN---LGEDV-IDTDVPTEF 149
Cdd:cd03506   3 LAILLGLFWAQGGFLAHDAGHGQVFKN--RWLNKLLGLTVGNLLGASAG-WWKNKHNVHHAYtniLGHDPdIDTLPLLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 150 EAKVFRTWLGKMIWMSLQ-PLFYGIRPFMLypksmtdleLINVAIQLLFSTFIytqfgakSFFFLFGGLvlGMGLHPCAG 228
Cdd:cd03506  80 SEPAFGKDQKKRFLHRYQhFYFFPLLALLL---------LAFLVVQLAGGLWL-------AVVFQLNHF--GMPVEDPPG 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17540134 229 HfVSEHYVFKKDQETYSYYGPINMVVFNVG--YHVEHHDFPYITGSNLPK----VREIAPEYY 285
Cdd:cd03506 142 E-SKNDWLERQVLTTRNITGSPFLDWLHGGlnYQIEHHLFPTMPRHNYPKvaplVRELCKKHG 203
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
52-269 6.16e-05

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  Cd Length: 222  Bit Score: 43.37  E-value: 6.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  52 VIAQIVFAYLLRDSDWLLILFQAYFVSGTINHSLTLAVHEISHnQAFGTNRpLANRIFGFIANLPMCIPMSiSFKKYHLE 131
Cdd:cd03507  14 ILLLALLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGH-GSFSDNR-RLNDIVGHILHSPLLVPYH-SWRISHNR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 132 HHRNLGEDVIDTDVPT----EFEAKVFRTWLGKMIWMSLQPLFYGIRPFMLypksmtdlelinVAIQLLFSTFIYTQFGA 207
Cdd:cd03507  91 HHAHTGNLEGDEVWVPvteeEYAELPKRLPYRLYRNPFLMLSLGWPYYLLL------------NVLLYYLIPYLVVNAWL 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17540134 208 KSFFFLfgglvlgMGLHPCAGHFVSEHYVFKKDQET----YSYYGPINMVVFNVGYHVEHHDFPYI 269
Cdd:cd03507 159 VLITYL-------QHTFPDIPWYRADEWNFAQAGLLgtvdRDYGGWLNWLTHIIGTHVAHHLFPRI 217
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
74-134 8.15e-04

This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine (3-O-methyl-scyllo-inosamine, 3-O-MSI) oxygenase, and other related proteins. It has been proposed that MocD, MocE (Rieske-like ferredoxin), and MocF (ferredoxin reductase) under the regulation of MocR, act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239588  Cd Length: 285  Bit Score: 40.43  E-value: 8.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17540134  74 AYFVSGTINHSLTLAVHEISHNQAFGTNRplANRIFGFIANLpMCIPMSISFKKYHLEHHR 134
Cdd:cd03511  47 AFLVYGVLYAALFARWHECVHGTAFATRW--LNDAVGQIAGL-MILLPPDFFRWSHARHHR 104
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
51-277 8.96e-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  Cd Length: 175  Bit Score: 39.57  E-value: 8.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134  51 MVIAQIVFAYLLRDSDWLLILfqAYFVSGTINHSLTLAVHEISHNqAFGTNRPLANrifgFIANLPMCIPMSISFKKY-- 128
Cdd:cd03510   3 LVIAAAVALALAWPNWLAYLL--AVLLIGARQRALAILMHDAAHG-LLFRNRRLND----FLGNWLAAVPIFQSLAAYrr 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 129 -HLEHHRNLGEDViDTDvptefeakvfrTWLGKMIWmslqplfygirpfmLYPksmtdlelinvaiqlLFSTFiytqfga 207
Cdd:cd03510  76 sHLKHHRHLGTED-DPD-----------LALYLLLW--------------LVP---------------LLTVF------- 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540134 208 ksffflfgglvlgmglhPCAGHF--VSEHYVFKKDQE-----TYSYY-GPINMVVF---NVGYHVEHHDFPYITGSNLPK 276
Cdd:cd03510 108 -----------------PLIGRIreIAEHAGVPADEDpdarnTRTTFgGWIERLLFaphNINYHLEHHLFPAVPFYNLPK 170

                .
gi 17540134 277 V 277
Cdd:cd03510 171 A 171
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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