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Conserved domains on  [gi|157014714|gb|EAA13016|]
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AGAP011402-PA [Anopheles gambiae str. PEST]

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 9.15e-172

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: 9.15e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  26 MVKKYPHIKKLFGPDPKFKYIVSAMVLTQIAMLYVMQHQSWPMIVLVAYCFGGVINHSLMLANHEISHNMAFGyaRPLAN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 106 RYFGMWCNLPIGVPMSVSFKKYHNLHHRHLADDDLDPDVPTLVEAKLFCTTFGKFVWVCLQPFFYGLRPLFVNPLPVTKL 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 186 ELINTAVQLTFNALVVLVFGWRMMAYLLIGSVLAMGLHPVAGHFIAEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157014714 265 FPAIPGSRLPELKKIAPEYYETMPQHTSWVRVLYDFITDPAVGPYARIKRK 315
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 1.72e-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: 77.17  E-value: 1.72e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 157014714    6 SRTDFEWVYDDQPHTRRRQEMVKKYPHIKKLFGPDPK 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 9.15e-172

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: 9.15e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  26 MVKKYPHIKKLFGPDPKFKYIVSAMVLTQIAMLYVMQHQSWPMIVLVAYCFGGVINHSLMLANHEISHNMAFGyaRPLAN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 106 RYFGMWCNLPIGVPMSVSFKKYHNLHHRHLADDDLDPDVPTLVEAKLFCTTFGKFVWVCLQPFFYGLRPLFVNPLPVTKL 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 186 ELINTAVQLTFNALVVLVFGWRMMAYLLIGSVLAMGLHPVAGHFIAEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157014714 265 FPAIPGSRLPELKKIAPEYYETMPQHTSWVRVLYDFITDPAVGPYARIKRK 315
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
3-315 1.77e-162

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 456.51  E-value: 1.77e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714   3 QRVSRTDFEWVYDDQPHTRRRQEMVKKYPHIKKLFGPDPKFKYIVSAMVLTQIAMLYVMQHQSWPMIVLVAYCFGGVINH 82
Cdd:PLN02579   7 EGVMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  83 SLMLANHEISHNMAFgyARPLANRYFGMWCNLPIGVPMSVSFKKYHNLHHRHLADDDLDPDVPTLVEAKLFCTTFGKFVW 162
Cdd:PLN02579  87 NLFLAIHELSHNLAF--KTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 163 VCLQPFFYGLRPLFVNPLPVTKLELINTAVQLTFNALVVLVFGWRMMAYLLIGSVLAMGLHPVAGHFIAEHYMFAKGFET 242
Cdd:PLN02579 165 VFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQET 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157014714 243 YSYYGPLNWITFNVGYHNEHHDFPAIPGSRLPELKKIAPEYYETMPQHTSWVRVLYDFITDPAVGPYARIKRK 315
Cdd:PLN02579 245 YSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
FA_desaturase pfam00487
Fatty acid desaturase;
66-285 1.01e-20

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 89.70  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714   66 WPMIVLVAYCFGGVinhsLMLANHEISHNMAFGYARPLANRYFGMwCNLPIGVPMSvSFKKYHNLHHRHLADDDLDPDVP 145
Cdd:pfam00487   4 LLLALLLGLFLLGI----LGVLAHEASHGALFRRRNRWLNDLLGL-AGLPLGISYS-AWRIAHLVHHRYTNGPDEDPDTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  146 TLVEAK--------LFCTTFGKFVWVCLQPFFYGLRPLFVNPLPVTKLELINT-----AVQLTFNALVVLVFGWRMMAYL 212
Cdd:pfam00487  78 PLASRFrgllryllRWLLGLLVLAWLLALLLGLWLRRLARRKRPIKSRRRRWRliawlLLLAAWLGLWLGFLGLGGLLLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  213 LIG-SVLAMGLHPVAGHFIAEHYMFAKG-------FETYSYYGPLNWITFNVGYHNEHHDFPAIPGSRLPELKKIAPEYY 284
Cdd:pfam00487 158 LWLlPLLVAGFLLALIFNYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREAL 237

                  .
gi 157014714  285 E 285
Cdd:pfam00487 238 P 238
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 1.72e-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: 77.17  E-value: 1.72e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 157014714    6 SRTDFEWVYDDQPHTRRRQEMVKKYPHIKKLFGPDPK 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
20-287 4.32e-17

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 80.98  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  20 TRRRQEMVKKYPhiKKLFGPDPKFKYIVSAMVLTQIAMLYVMQH--QSWPMIVLvAYCFGGVINHSLMLANHEISHNMAF 97
Cdd:COG3239   15 AAPLDSIRARLP--KPRTRRDAIAILITFLALAGLWALLALSLAywPSWWLLPL-ALLLAGLLLTGLFSVGHDCGHGSFF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  98 GyaRPLANRYFGMWCNLPIGVPmSVSFKKYHNLHHRHLADDDLDPDVPT------------LVEAKLFCTTFGKFVWVcl 165
Cdd:COG3239   92 K--NRWINDLIGHLAAALLLAP-PVFWRISHNQHHAHTNILDDDPETYVsypeqlrrgplrFQLIRLPWLAFGFGPRW-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 166 qpFFYGLRPLFVNPLPVTKLELINTAV----QLTFNALVVLVFGWRMMAYLLIGSVLAMGLhpVAGHFIAE--HYMFAKG 239
Cdd:COG3239  167 --ALLHFELLEKLFKRSGKAPKAAALAtllaAIGLAALLALAFFWGLIPLLLVGLWLVLVL--FVHHTFDLlpHHGLEDW 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157014714 240 FE--------TYSYYGP-LNWITFNVGYHNEHHDFPAIPGSRLPE----LKKIAPEYYETM 287
Cdd:COG3239  243 QWsdralnarSNVDAPPlLRFLTGNINYHVEHHLFPDVPWYRLPRahrlIKEALGERGLTI 303
 
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 9.15e-172

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: 9.15e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  26 MVKKYPHIKKLFGPDPKFKYIVSAMVLTQIAMLYVMQHQSWPMIVLVAYCFGGVINHSLMLANHEISHNMAFGyaRPLAN 105
Cdd:cd03508    1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 106 RYFGMWCNLPIGVPMSVSFKKYHNLHHRHLADDDLDPDVPTLVEAKLFCTTFGKFVWVCLQPFFYGLRPLFVNPLPVTKL 185
Cdd:cd03508   79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 186 ELINTAVQLTFNALVVLVFGWRMMAYLLIGSVLAMGLHPVAGHFIAEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHD 264
Cdd:cd03508  159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157014714 265 FPAIPGSRLPELKKIAPEYYETMPQHTSWVRVLYDFITDPAVGPYARIKRK 315
Cdd:cd03508  239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
3-315 1.77e-162

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 456.51  E-value: 1.77e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714   3 QRVSRTDFEWVYDDQPHTRRRQEMVKKYPHIKKLFGPDPKFKYIVSAMVLTQIAMLYVMQHQSWPMIVLVAYCFGGVINH 82
Cdd:PLN02579   7 EGVMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  83 SLMLANHEISHNMAFgyARPLANRYFGMWCNLPIGVPMSVSFKKYHNLHHRHLADDDLDPDVPTLVEAKLFCTTFGKFVW 162
Cdd:PLN02579  87 NLFLAIHELSHNLAF--KTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 163 VCLQPFFYGLRPLFVNPLPVTKLELINTAVQLTFNALVVLVFGWRMMAYLLIGSVLAMGLHPVAGHFIAEHYMFAKGFET 242
Cdd:PLN02579 165 VFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQET 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157014714 243 YSYYGPLNWITFNVGYHNEHHDFPAIPGSRLPELKKIAPEYYETMPQHTSWVRVLYDFITDPAVGPYARIKRK 315
Cdd:PLN02579 245 YSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
FA_desaturase pfam00487
Fatty acid desaturase;
66-285 1.01e-20

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 89.70  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714   66 WPMIVLVAYCFGGVinhsLMLANHEISHNMAFGYARPLANRYFGMwCNLPIGVPMSvSFKKYHNLHHRHLADDDLDPDVP 145
Cdd:pfam00487   4 LLLALLLGLFLLGI----LGVLAHEASHGALFRRRNRWLNDLLGL-AGLPLGISYS-AWRIAHLVHHRYTNGPDEDPDTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  146 TLVEAK--------LFCTTFGKFVWVCLQPFFYGLRPLFVNPLPVTKLELINT-----AVQLTFNALVVLVFGWRMMAYL 212
Cdd:pfam00487  78 PLASRFrgllryllRWLLGLLVLAWLLALLLGLWLRRLARRKRPIKSRRRRWRliawlLLLAAWLGLWLGFLGLGGLLLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  213 LIG-SVLAMGLHPVAGHFIAEHYMFAKG-------FETYSYYGPLNWITFNVGYHNEHHDFPAIPGSRLPELKKIAPEYY 284
Cdd:pfam00487 158 LWLlPLLVAGFLLALIFNYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREAL 237

                  .
gi 157014714  285 E 285
Cdd:pfam00487 238 P 238
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 1.72e-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: 77.17  E-value: 1.72e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 157014714    6 SRTDFEWVYDDQPHTRRRQEMVKKYPHIKKLFGPDPK 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
20-287 4.32e-17

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 80.98  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  20 TRRRQEMVKKYPhiKKLFGPDPKFKYIVSAMVLTQIAMLYVMQH--QSWPMIVLvAYCFGGVINHSLMLANHEISHNMAF 97
Cdd:COG3239   15 AAPLDSIRARLP--KPRTRRDAIAILITFLALAGLWALLALSLAywPSWWLLPL-ALLLAGLLLTGLFSVGHDCGHGSFF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  98 GyaRPLANRYFGMWCNLPIGVPmSVSFKKYHNLHHRHLADDDLDPDVPT------------LVEAKLFCTTFGKFVWVcl 165
Cdd:COG3239   92 K--NRWINDLIGHLAAALLLAP-PVFWRISHNQHHAHTNILDDDPETYVsypeqlrrgplrFQLIRLPWLAFGFGPRW-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 166 qpFFYGLRPLFVNPLPVTKLELINTAV----QLTFNALVVLVFGWRMMAYLLIGSVLAMGLhpVAGHFIAE--HYMFAKG 239
Cdd:COG3239  167 --ALLHFELLEKLFKRSGKAPKAAALAtllaAIGLAALLALAFFWGLIPLLLVGLWLVLVL--FVHHTFDLlpHHGLEDW 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157014714 240 FE--------TYSYYGP-LNWITFNVGYHNEHHDFPAIPGSRLPE----LKKIAPEYYETM 287
Cdd:COG3239  243 QWsdralnarSNVDAPPlLRFLTGNINYHVEHHLFPDVPWYRLPRahrlIKEALGERGLTI 303
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
69-145 3.16e-10

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: 57.09  E-value: 3.16e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157014714  69 IVLVAYCFGGVInhSLMLANHEISHNMAFGyaRPLANRYFGMWCNLPIGVPMSvSFKKYHNLHHRHLADDDLDPDVP 145
Cdd:cd01060    2 LLALLLGLLGGL--GLTVLAHELGHRSFFR--SRWLNRLLGALLGLALGGSYG-WWRRSHRRHHRYTNTPGKDPDSA 73
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
71-279 1.60e-08

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: 53.80  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  71 LVAYCFGGVINHSLMLANHEISHNMAFGyaRPLANRYFGMWCNLPIGVPMSvSFKKYHNLHH----RHLADDDLDPDVPT 146
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFK--NRWLNKLLGLTVGNLLGASAG-WWKNKHNVHHaytnILGHDPDIDTLPLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 147 LVEAKLFCTTFGKFVWVCLQPFFYglrplfvnpLPVTKLELI-NTAVQLTFNALVVLVFgwrmmayllIGSVLAMGLHPV 225
Cdd:cd03506   78 ARSEPAFGKDQKKRFLHRYQHFYF---------FPLLALLLLaFLVVQLAGGLWLAVVF---------QLNHFGMPVEDP 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157014714 226 AGHFIAEHYMfaKGFETYSYYGP---LNWITFNVGYHNEHHDFPAIPGSRLPELKKI 279
Cdd:cd03506  140 PGESKNDWLE--RQVLTTRNITGspfLDWLHGGLNYQIEHHLFPTMPRHNYPKVAPL 194
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
49-273 9.90e-06

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: 45.68  E-value: 9.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  49 AMVLTQIAMLYVMQHQ--SWPMIVLVAYCFGGVINHSLMLAnHEISHNMAFGYARplANRYFGMWCNLPIGVPMSvSFKK 126
Cdd:cd03507   11 APDILLLALLALAASLllSWWLWPLYWIVQGLFLTGLFVLG-HDCGHGSFSDNRR--LNDIVGHILHSPLLVPYH-SWRI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 127 YHNLHHRHLADDDLDpdvptlveaklfcttfgkFVWVCLQPFFYGLRPLFVnplpvTKLELINTAVQLTFNALVVLVFGW 206
Cdd:cd03507   87 SHNRHHAHTGNLEGD------------------EVWVPVTEEEYAELPKRL-----PYRLYRNPFLMLSLGWPYYLLLNV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 207 rMMAYLLIGSVLAMGL---------HPVAGHFIAEHYMFAKGFET----YSYYGPLNWITFNVGYHNEHHDFPAIPGSRL 273
Cdd:cd03507  144 -LLYYLIPYLVVNAWLvlitylqhtFPDIPWYRADEWNFAQAGLLgtvdRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
55-279 4.36e-05

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


Pssm-ID: 239588  Cd Length: 285  Bit Score: 44.28  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  55 IAMLYVMQHQSWpmIVLVAYCFGGVINHSLMLANHEISHNMAFgyARPLANRYFGMWCNLPIGVPMSVsFKKYHNLHHRH 134
Cdd:cd03511   31 SGILIAWTWGSW--WALPAFLVYGVLYAALFARWHECVHGTAF--ATRWLNDAVGQIAGLMILLPPDF-FRWSHARHHRY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 135 LADDDLDPDV-----PTLVEakLFCTTFG-KFVWVCLQPFFYGLRPL-------FVNPLPVTKLELINTAVQLTFNALVV 201
Cdd:cd03511  106 TQIPGRDPELavprpPTLRE--YLLALSGlPYWWGKLRTVFRHAFGAvseaekpFIPAEERPKVVREARAMLAVYAGLIA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 202 LVFGWRMMAYLLIGSVLAMGLHPVAGHFI-AEH-------YMFAKGFETYSYYgPLNWITFNVGYHNEHHDFPAIPGSRL 273
Cdd:cd03511  184 LSLYLGSPLLVLVWGLPLLLGQPILRLFLlAEHggcpedaNDLRNTRTTLTNP-PLRFLYWNMPYHAEHHMYPSVPFHAL 262

                 ....*.
gi 157014714 274 PELKKI 279
Cdd:cd03511  263 PKLHEL 268
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
64-279 7.15e-05

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: 42.66  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  64 QSWPMIVLVAYCFGGVInHSLMLANHEISHNMAFgyARPLANRYFGMW-CNLPIGVPMSvSFKKYHNLHHRHLADDDlDP 142
Cdd:cd03510   16 PNWLAYLLAVLLIGARQ-RALAILMHDAAHGLLF--RNRRLNDFLGNWlAAVPIFQSLA-AYRRSHLKHHRHLGTED-DP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 143 DVptlveaklfcttfgkfVWVCLqpfFYGLrPLFvnplpvtklelintavqltfnaLVVLVFGWrmmayllIGSVLAMGL 222
Cdd:cd03510   91 DL----------------ALYLL---LWLV-PLL----------------------TVFPLIGR-------IREIAEHAG 121
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157014714 223 HPVAGHFIAEHymfakgfeTYSYYGplNWIT------FNVGYHNEHHDFPAIPGSRLPELKKI 279
Cdd:cd03510  122 VPADEDPDARN--------TRTTFG--GWIErllfapHNINYHLEHHLFPAVPFYNLPKAHRI 174
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
49-275 1.07e-03

Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the addition of hydroxyl groups to the beta-ionone rings of beta-carotene to form zeaxanthin and is found in bacteria and red algae. Carotenoids are important natural pigments; zeaxanthin and lutein are the only dietary carotenoids that accumulate in the macular region of the retina and lens. It is proposed that these carotenoids protect ocular tissues against photooxidative damage. CrtR does not show overall amino acid sequence similarity to the beta-carotene hydroxylases similar to CrtZ, an astaxanthin biosynthetic beta-carotene hydroxylase. However, CrtR does show sequence similarity to the green alga, Haematococcus pluvialis, beta-carotene ketolase (CrtW), which converts beta-carotene to canthaxanthin. Sequences of the CrtR_beta-carotene-hydroxylase domain family, as well as, the CrtW_beta-carotene-ketolase domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common 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: 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: 239591  Cd Length: 207  Bit Score: 39.66  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714  49 AMVLTQIAMLYVMQHQSW---PMIVLVAYCFGGVInhslmlanHEISHNMAfgYARPLANRYFGMWCNLPIGVPMSVsFK 125
Cdd:cd03514    8 ALVWLSTWGYVISYLPLWvcfILNTLSLHLAGTVI--------HDASHKAA--SRNRWINELIGHVSAFFLGFPFPV-FR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157014714 126 KYHNLHHRHLADDDLDPD---VPTLVEAKLFCTTFGKFVWvclqpffyglrplfvnplpvtklelintavqltFNALVVL 202
Cdd:cd03514   77 RVHMQHHAHTNDPEKDPDhflLEWLVARSLFITLLVIAIL---------------------------------FGFLWEL 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157014714 203 VFGWrMMAYLLIGSVLAMGLHpvaghfIAEHYMF-AKGFETYSYYGP---LNWITFNVGYHNEHHDFPAIPGSRLPE 275
Cdd:cd03514  124 LNLW-FLPALIVGTYLALFFD------WLPHHPFeETQRWDNSRVYPsklLNPLIMGQNYHLVHHLWPSIPWYRYPE 193
 
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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