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Conserved domains on  [gi|162287184|ref|NP_445775|]
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sphingolipid delta(4)-desaturase DES1 [Rattus norvegicus]

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 ...
26-315 4.48e-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: 475.98  E-value: 4.48e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  26 ILAKYPEIKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFWSYAFGSCLNHSMTLAIHEISHNFPFGhhKAMWN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 106 RWFGMFANLSLGVPYSISFKRYHMDHHRYLGADGIDVDIPTDFEGWFFCTTLRKLVWVILQPLFYAFRPLFINPKPITHL 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 186 EVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162287184 265 FPNVPGKNLPLVRKIASEYYDNLPHYNSWIRVLYDFVMDDTISPYSRMKRP 315
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 8.27e-18

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: 75.24  E-value: 8.27e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 162287184    6 SREEFEWVYTDQPHAARRQEILAKYPEIKSLMKPDPN 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 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 4.48e-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: 475.98  E-value: 4.48e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  26 ILAKYPEIKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFWSYAFGSCLNHSMTLAIHEISHNFPFGhhKAMWN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 106 RWFGMFANLSLGVPYSISFKRYHMDHHRYLGADGIDVDIPTDFEGWFFCTTLRKLVWVILQPLFYAFRPLFINPKPITHL 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 186 EVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162287184 265 FPNVPGKNLPLVRKIASEYYDNLPHYNSWIRVLYDFVMDDTISPYSRMKRP 315
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
5-318 2.08e-157

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 442.64  E-value: 2.08e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184   5 VSREEFEWVYTDQPHAARRQEILAKYPEIKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFWSYAFGSCLNHSM 84
Cdd:PLN02579   9 VMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  85 TLAIHEISHNFPFghHKAMWNRWFGMFANLSLGVPYSISFKRYHMDHHRYLGADGIDVDIPTDFEGWFFCTTLRKLVWVI 164
Cdd:PLN02579  89 FLAIHELSHNLAF--KTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 165 LQPLFYAFRPLFINPKPITHLEVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYS 244
Cdd:PLN02579 167 LQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYS 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162287184 245 YYGPLNLLTFNVGYHNEHHDFPNVPGKNLPLVRKIASEYYDNLPHYNSWIRVLYDFVMDDTISPYSRMKRPPKG 318
Cdd:PLN02579 247 YYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRKPPK 320
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 8.27e-18

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: 75.24  E-value: 8.27e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 162287184    6 SREEFEWVYTDQPHAARRQEILAKYPEIKSLMKPDPN 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase;
68-285 4.46e-14

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 70.44  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184   68 WLMFWSYAFGSCLNHSMTLAI-HEISHNFPFGHHKAMWNRWFGMFAnLSLGVPYSiSFKRYHMDHHRYLGADGIDVDIPT 146
Cdd:pfam00487   1 WLALLLALLLGLFLLGILGVLaHEASHGALFRRRNRWLNDLLGLAG-LPLGISYS-AWRIAHLVHHRYTNGPDEDPDTAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  147 ---DFEGWF-----FCTTLRKLVWVILQPLFYAFRPLFINPKPITHLEVINTVIQVTFDVLVY--------YVFGVKSLV 210
Cdd:pfam00487  79 lasRFRGLLryllrWLLGLLVLAWLLALLLGLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWlglwlgflGLGGLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  211 YMLAASLLGLGLHPISghFIAEHYMFLKG-------HETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPLVRKIASEY 283
Cdd:pfam00487 159 WLLPLLVAGFLLALIF--NYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREA 236

                  ..
gi 162287184  284 YD 285
Cdd:pfam00487 237 LP 238
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
20-276 5.82e-12

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 65.57  E-value: 5.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  20 AARRQEILAKYPeiKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFW-SYAFGSCLNHSMTLAIHEISHNFPFG 98
Cdd:COG3239   15 AAPLDSIRARLP--KPRTRRDAIAILITFLALAGLWALLALSLAYWPSWWLLPlALLLAGLLLTGLFSVGHDCGHGSFFK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  99 HHKAmwNRWFGMFANLSLGVPYSiSFKRYHMDHHRYLGADGIDVDIPT-----------------DFEGWFFCTTLRKlv 161
Cdd:COG3239   93 NRWI--NDLIGHLAAALLLAPPV-FWRISHNQHHAHTNILDDDPETYVsypeqlrrgplrfqlirLPWLAFGFGPRWA-- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 162 WVILQPLFYAFRPLFINPKPITHLEVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISG-HFIAEHYM----- 235
Cdd:COG3239  168 LLHFELLEKLFKRSGKAPKAAALATLLAAIGLAALLALAFFWGLIPLLLVGLWLVLVLFVHHTFDLlPHHGLEDWqwsdr 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 162287184 236 FLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPLV 276
Cdd:COG3239  248 ALNARSNVDAPPLLRFLTGNINYHVEHHLFPDVPWYRLPRA 288
 
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 4.48e-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: 475.98  E-value: 4.48e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  26 ILAKYPEIKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFWSYAFGSCLNHSMTLAIHEISHNFPFGhhKAMWN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 106 RWFGMFANLSLGVPYSISFKRYHMDHHRYLGADGIDVDIPTDFEGWFFCTTLRKLVWVILQPLFYAFRPLFINPKPITHL 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 186 EVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISGHFIAEHYMFL-KGHETYSYYGPLNLLTFNVGYHNEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162287184 265 FPNVPGKNLPLVRKIASEYYDNLPHYNSWIRVLYDFVMDDTISPYSRMKRP 315
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
5-318 2.08e-157

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 442.64  E-value: 2.08e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184   5 VSREEFEWVYTDQPHAARRQEILAKYPEIKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFWSYAFGSCLNHSM 84
Cdd:PLN02579   9 VMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNHNL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  85 TLAIHEISHNFPFghHKAMWNRWFGMFANLSLGVPYSISFKRYHMDHHRYLGADGIDVDIPTDFEGWFFCTTLRKLVWVI 164
Cdd:PLN02579  89 FLAIHELSHNLAF--KTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVWVF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 165 LQPLFYAFRPLFINPKPITHLEVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYS 244
Cdd:PLN02579 167 LQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQETYS 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162287184 245 YYGPLNLLTFNVGYHNEHHDFPNVPGKNLPLVRKIASEYYDNLPHYNSWIRVLYDFVMDDTISPYSRMKRPPKG 318
Cdd:PLN02579 247 YYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRKPPK 320
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 8.27e-18

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: 75.24  E-value: 8.27e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 162287184    6 SREEFEWVYTDQPHAARRQEILAKYPEIKSLMKPDPN 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase;
68-285 4.46e-14

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 70.44  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184   68 WLMFWSYAFGSCLNHSMTLAI-HEISHNFPFGHHKAMWNRWFGMFAnLSLGVPYSiSFKRYHMDHHRYLGADGIDVDIPT 146
Cdd:pfam00487   1 WLALLLALLLGLFLLGILGVLaHEASHGALFRRRNRWLNDLLGLAG-LPLGISYS-AWRIAHLVHHRYTNGPDEDPDTAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  147 ---DFEGWF-----FCTTLRKLVWVILQPLFYAFRPLFINPKPITHLEVINTVIQVTFDVLVY--------YVFGVKSLV 210
Cdd:pfam00487  79 lasRFRGLLryllrWLLGLLVLAWLLALLLGLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWlglwlgflGLGGLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  211 YMLAASLLGLGLHPISghFIAEHYMFLKG-------HETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPLVRKIASEY 283
Cdd:pfam00487 159 WLLPLLVAGFLLALIF--NYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREA 236

                  ..
gi 162287184  284 YD 285
Cdd:pfam00487 237 LP 238
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
20-276 5.82e-12

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 65.57  E-value: 5.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  20 AARRQEILAKYPeiKSLMKPDPNLIWIVTSMLLVQLASFYLVKDLDWKWLMFW-SYAFGSCLNHSMTLAIHEISHNFPFG 98
Cdd:COG3239   15 AAPLDSIRARLP--KPRTRRDAIAILITFLALAGLWALLALSLAYWPSWWLLPlALLLAGLLLTGLFSVGHDCGHGSFFK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  99 HHKAmwNRWFGMFANLSLGVPYSiSFKRYHMDHHRYLGADGIDVDIPT-----------------DFEGWFFCTTLRKlv 161
Cdd:COG3239   93 NRWI--NDLIGHLAAALLLAPPV-FWRISHNQHHAHTNILDDDPETYVsypeqlrrgplrfqlirLPWLAFGFGPRWA-- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 162 WVILQPLFYAFRPLFINPKPITHLEVINTVIQVTFDVLVYYVFGVKSLVYMLAASLLGLGLHPISG-HFIAEHYM----- 235
Cdd:COG3239  168 LLHFELLEKLFKRSGKAPKAAALATLLAAIGLAALLALAFFWGLIPLLLVGLWLVLVLFVHHTFDLlPHHGLEDWqwsdr 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 162287184 236 FLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPLV 276
Cdd:COG3239  248 ALNARSNVDAPPLLRFLTGNINYHVEHHLFPDVPWYRLPRA 288
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
68-148 1.64e-09

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: 54.78  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  68 WLMFWSYAFGSCLnhSMTLAIHEISHNFPFGHHKamWNRWFGMFANLSLGVPYsISFKRYHMDHHRYLGADGIDVDIPTD 147
Cdd:cd01060    1 LLLALLLGLLGGL--GLTVLAHELGHRSFFRSRW--LNRLLGALLGLALGGSY-GWWRRSHRRHHRYTNTPGKDPDSAVN 75

                 .
gi 162287184 148 F 148
Cdd:cd01060   76 Y 76
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
89-279 1.28e-04

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: 42.24  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184  89 HEISHNFPFGHHKamWNRWFGMFANLSLGVPYSiSFKRYHMDHHRYLGADGIDVDIPTD----FEGWFFCTTLRKLVWVI 164
Cdd:cd03506   19 HDAGHGQVFKNRW--LNKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTLpllaRSEPAFGKDQKKRFLHR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287184 165 LQ-----PLFYAFRPLFInpkpITHL---EVINTVIQVT-FDVLVYYVFGvkslvymlaasllglglhPISGHFiAEHYM 235
Cdd:cd03506   96 YQhfyffPLLALLLLAFL----VVQLaggLWLAVVFQLNhFGMPVEDPPG------------------ESKNDW-LERQV 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 162287184 236 flkgHETYSYYGP--LNLLTFNVGYHNEHHDFPNVPGKNLPLVRKI 279
Cdd:cd03506  153 ----LTTRNITGSpfLDWLHGGLNYQIEHHLFPTMPRHNYPKVAPL 194
 
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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