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Conserved domains on  [gi|7297049|gb|AAF52318|]
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infertile crescent, isoform A [Drosophila melanogaster]

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 0e+00

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: 506.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   26 ILEKYPQIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYCFGGIINHSLMLAVHEISHNLAFGhsRPMHN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  106 RILGFICNLPIGLPMSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFLWVCLQPFFYIFRPLIINPKPPTRL 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  186 EIINTVVQLTFNALIVYFLGWKPLAYLLIGSILAMGLHPVAGHFISEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 7297049  265 FPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRR 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 2.06e-21

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: 84.87  E-value: 2.06e-21
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7297049      6 SRTDFEWVYTEEPHASRRKIILEKYPQIKKLFGHDPN 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 0e+00

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: 506.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   26 ILEKYPQIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYCFGGIINHSLMLAVHEISHNLAFGhsRPMHN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  106 RILGFICNLPIGLPMSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFLWVCLQPFFYIFRPLIINPKPPTRL 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  186 EIINTVVQLTFNALIVYFLGWKPLAYLLIGSILAMGLHPVAGHFISEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 7297049  265 FPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRR 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
3-315 2.88e-170

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 475.00  E-value: 2.88e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049     3 QKVSRTDFEWVYTEEPHASRRKIILEKYPQIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYCFGGIINH 82
Cdd:PLN02579   7 EGVMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049    83 SLMLAVHEISHNLAFghSRPMHNRILGFICNLPIGLPMSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFLW 162
Cdd:PLN02579  87 NLFLAIHELSHNLAF--KTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   163 VCLQPFFYIFRPLIINPKPPTRLEIINTVVQLTFNALIVYFLGWKPLAYLLIGSILAMGLHPVAGHFISEHYMFAKGFET 242
Cdd:PLN02579 165 VFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQET 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7297049   243 YSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRR 315
Cdd:PLN02579 245 YSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 2.06e-21

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: 84.87  E-value: 2.06e-21
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7297049      6 SRTDFEWVYTEEPHASRRKIILEKYPQIKKLFGHDPN 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase;
68-285 1.22e-18

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 83.54  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049     68 WLIVAAYCFGGIINHSL-MLAVHEISHNLAFGHSRPMHNRILGFiCNLPIGLPMSiSFKKYHLEHHRYQGDEAIDTDIPT 146
Cdd:pfam00487   1 WLALLLALLLGLFLLGIlGVLAHEASHGALFRRRNRWLNDLLGL-AGLPLGISYS-AWRIAHLVHHRYTNGPDEDPDTAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049    147 LLEAR----------LFDTTFGKFLWVCLQPF---FYIFRPLIINPKPPTRLEIINTVVQLTFNALIVYFLGWKPLAYLL 213
Cdd:pfam00487  79 LASRFrgllryllrwLLGLLVLAWLLALLLGLwlrRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049    214 IG-SILAMGLHPVAGHFISEHYMFAKG-------FETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 285
Cdd:pfam00487 159 WLlPLLVAGFLLALIFNYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALP 238
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
32-287 4.38e-17

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 80.60  E-value: 4.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   32 QIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYC-FGGIINHSLMLAVHEISHNLAFghSRPMHNRILGF 110
Cdd:COG3239  25 LPKPRTRRDAIAILITFLALAGLWALLALSLAYWPSWWLLPLALlLAGLLLTGLFSVGHDCGHGSFF--KNRWINDLIGH 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  111 ICNLPIGLPmSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFL---WVCLQPFFYIFRPLIINPKPPT--RL 185
Cdd:COG3239 103 LAAALLLAP-PVFWRISHNQHHAHTNILDDDPETYVSYPEQLRRGPLRFQLirlPWLAFGFGPRWALLHFELLEKLfkRS 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  186 EIINTVVQLTFNALIVYFLGWKPLAYL-----LIGSILAMGLHPVAGHFISE--HYMFAKGFE--------TYSYYGP-L 249
Cdd:COG3239 182 GKAPKAAALATLLAAIGLAALLALAFFwglipLLLVGLWLVLVLFVHHTFDLlpHHGLEDWQWsdralnarSNVDAPPlL 261
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 7297049  250 NWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTM 287
Cdd:COG3239 262 RFLTGNINYHVEHHLFPDVPWYRLPRAHRLIKEALGER 299
 
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 0e+00

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: 506.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   26 ILEKYPQIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYCFGGIINHSLMLAVHEISHNLAFGhsRPMHN 105
Cdd:cd03508   1 ILAKYPEIKKLFGPDPLTKWVVLGVVLLQIITAYLLRDSSWWKILLVAYFFGGTINHSLFLAIHEISHNLAFG--KPLWN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  106 RILGFICNLPIGLPMSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFLWVCLQPFFYIFRPLIINPKPPTRL 185
Cdd:cd03508  79 RLFGIFANLPIGVPYSISFKKYHLEHHRYLGEDGLDTDIPTEFEGKLFSTVLGKAIWVTLQPFFYALRPLFVRPKPPTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  186 EIINTVVQLTFNALIVYFLGWKPLAYLLIGSILAMGLHPVAGHFISEHYMFA-KGFETYSYYGPLNWITFNVGYHNEHHD 264
Cdd:cd03508 159 EVINIVVQITFDYLIYYFFGWKSLAYLLLGSFLGGGLHPLAGHFISEHYVFTgKGQETYSYYGPLNLLTFNVGYHNEHHD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 7297049  265 FPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRR 315
Cdd:cd03508 239 FPYIPGTRLPKLRKIAPEFYDNLPQHTSWPRVLYDFIMDDNVGPYSRVKRK 289
PLN02579 PLN02579
sphingolipid delta-4 desaturase
3-315 2.88e-170

sphingolipid delta-4 desaturase


Pssm-ID: 215316 [Multi-domain]  Cd Length: 323  Bit Score: 475.00  E-value: 2.88e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049     3 QKVSRTDFEWVYTEEPHASRRKIILEKYPQIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYCFGGIINH 82
Cdd:PLN02579   7 EGVMATDFFWSYTDEPHASRRREILSKYPQIKELFGPDPWAFPKIAAVVLLQLCTATLLHDAGWPKILLVAYFFGGFLNH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049    83 SLMLAVHEISHNLAFghSRPMHNRILGFICNLPIGLPMSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFLW 162
Cdd:PLN02579  87 NLFLAIHELSHNLAF--KTPVYNRWLGIFANLPIGIPMSVTFQKYHLEHHRFQGVDGIDMDIPSQGEARLVRNTLSKIVW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   163 VCLQPFFYIFRPLIINPKPPTRLEIINTVVQLTFNALIVYFLGWKPLAYLLIGSILAMGLHPVAGHFISEHYMFAKGFET 242
Cdd:PLN02579 165 VFLQLFFYALRPLFVNPKPPGLWEFINLLTQIAFDAALVYFAGWKSLAYLILSTFLGGGLHPMAGHFISEHYVFNPGQET 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7297049   243 YSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRR 315
Cdd:PLN02579 245 YSYYGPLNLLTWNVGYHNEHHDFPRIPGSKLHKVKEIAPEYYDNLKSYKSWSQVIYMYIMDPTIGPFSRMKRK 317
Lipid_DES pfam08557
Sphingolipid Delta4-desaturase (DES); Sphingolipids are important membrane signalling ...
6-42 2.06e-21

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: 84.87  E-value: 2.06e-21
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7297049      6 SRTDFEWVYTEEPHASRRKIILEKYPQIKKLFGHDPN 42
Cdd:pfam08557   1 SRNDFYWSYTEEPHASRRKEILKKHPEIKKLMGPDPL 37
FA_desaturase pfam00487
Fatty acid desaturase;
68-285 1.22e-18

Fatty acid desaturase;


Pssm-ID: 334106 [Multi-domain]  Cd Length: 248  Bit Score: 83.54  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049     68 WLIVAAYCFGGIINHSL-MLAVHEISHNLAFGHSRPMHNRILGFiCNLPIGLPMSiSFKKYHLEHHRYQGDEAIDTDIPT 146
Cdd:pfam00487   1 WLALLLALLLGLFLLGIlGVLAHEASHGALFRRRNRWLNDLLGL-AGLPLGISYS-AWRIAHLVHHRYTNGPDEDPDTAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049    147 LLEAR----------LFDTTFGKFLWVCLQPF---FYIFRPLIINPKPPTRLEIINTVVQLTFNALIVYFLGWKPLAYLL 213
Cdd:pfam00487  79 LASRFrgllryllrwLLGLLVLAWLLALLLGLwlrRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFLGLGGLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049    214 IG-SILAMGLHPVAGHFISEHYMFAKG-------FETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 285
Cdd:pfam00487 159 WLlPLLVAGFLLALIFNYLEHYGGDWGerpvettRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRLPKLHRRLREALP 238
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
32-287 4.38e-17

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 225779 [Multi-domain]  Cd Length: 343  Bit Score: 80.60  E-value: 4.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   32 QIKKLFGHDPNFKWVAGAMVLTQILALFVVKDLSWSWLIVAAYC-FGGIINHSLMLAVHEISHNLAFghSRPMHNRILGF 110
Cdd:COG3239  25 LPKPRTRRDAIAILITFLALAGLWALLALSLAYWPSWWLLPLALlLAGLLLTGLFSVGHDCGHGSFF--KNRWINDLIGH 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  111 ICNLPIGLPmSISFKKYHLEHHRYQGDEAIDTDIPTLLEARLFDTTFGKFL---WVCLQPFFYIFRPLIINPKPPT--RL 185
Cdd:COG3239 103 LAAALLLAP-PVFWRISHNQHHAHTNILDDDPETYVSYPEQLRRGPLRFQLirlPWLAFGFGPRWALLHFELLEKLfkRS 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  186 EIINTVVQLTFNALIVYFLGWKPLAYL-----LIGSILAMGLHPVAGHFISE--HYMFAKGFE--------TYSYYGP-L 249
Cdd:COG3239 182 GKAPKAAALATLLAAIGLAALLALAFFwglipLLLVGLWLVLVLFVHHTFDLlpHHGLEDWQWsdralnarSNVDAPPlL 261
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 7297049  250 NWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTM 287
Cdd:COG3239 262 RFLTGNINYHVEHHLFPDVPWYRLPRAHRLIKEALGER 299
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
67-282 3.97e-10

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: 59.31  E-value: 3.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   67 SWLIVAAYCFGGIINHSLMLAVHEISHNLAFgHSRPMhNRILGFICNLPIGLPmSISFKKYHLEHHRYQGDEAIDTDI-- 144
Cdd:cd03511  41 SWWALPAFLVYGVLYAALFARWHECVHGTAF-ATRWL-NDAVGQIAGLMILLP-PDFFRWSHARHHRYTQIPGRDPELav 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  145 ---PTLLEarLFDTTFGKFLW------VCLQPFFYIF---RPLIinPKPPTRLEIINTVVQLTFNALIV---YFLGWkPL 209
Cdd:cd03511 118 prpPTLRE--YLLALSGLPYWwgklrtVFRHAFGAVSeaeKPFI--PAEERPKVVREARAMLAVYAGLIalsLYLGS-PL 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  210 AYLLIGSILAMGlHPVAGHFI-SEH-------YMFAKGFETYSYYgPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAK 281
Cdd:cd03511 193 LVLVWGLPLLLG-QPILRLFLlAEHggcpedaNDLRNTRTTLTNP-PLRFLYWNMPYHAEHHMYPSVPFHALPKLHELIK 270

                .
gi 7297049  282 E 282
Cdd:cd03511 271 D 271
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
68-145 5.78e-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: 53.24  E-value: 5.78e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7297049   68 WLIVAAYCFGGIInhSLMLAVHEISHNLAFGHSRPmhNRILGFICNLPIGLPmSISFKKYHLEHHRYQGDEAIDTDIP 145
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: ...
71-285 2.87e-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: 53.03  E-value: 2.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   71 VAAYCFGGIINHSLMLAVHEISHNLAFGHSRpmHNRILGFICNLPIGLPMSiSFKKYHLEHHRYQGDEAIDTDIPTLLEA 150
Cdd:cd03506   1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRW--LNKLLGLTVGNLLGASAG-WWKNKHNVHHAYTNILGHDPDIDTLPLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  151 RLFDTTFG----KFLWVCLQPFFYIFrpliinpkpptrleiintvvqLTFNALIVYFLgwkplAYLLIGSILAMGLHPva 226
Cdd:cd03506  78 ARSEPAFGkdqkKRFLHRYQHFYFFP---------------------LLALLLLAFLV-----VQLAGGLWLAVVFQL-- 129
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7297049  227 GHFISEHYMFAKGFE----------TYSYYGP--LNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 285
Cdd:cd03506 130 NHFGMPVEDPPGESKndwlerqvltTRNITGSpfLDWLHGGLNYQIEHHLFPTMPRHNYPKVAPLVRELCK 200
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
55-273 4.24e-04

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: 40.67  E-value: 4.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   55 ILALFVVKDLSWSWLIVAAYCFGGIINHSLMLAvHEISHNlAFGHSRPMhNRILGFICNLPIGLPMSiSFKKYHLEHHRY 134
Cdd:cd03507  19 LLALAASLLLSWWLWPLYWIVQGLFLTGLFVLG-HDCGHG-SFSDNRRL-NDIVGHILHSPLLVPYH-SWRISHNRHHAH 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  135 QGDEAIDTDIPTLLEarlfdttfgkflwvclqpffYIFRPLiinPKPPTRLEIINTVVQLTFNALIVYFLGWKpLAYLLI 214
Cdd:cd03507  95 TGNLEGDEVWVPVTE--------------------EEYAEL---PKRLPYRLYRNPFLMLSLGWPYYLLLNVL-LYYLIP 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7297049  215 GSILAMGL---------HPVAGHFISEHYMFAKGFET----YSYYGPLNWITFNVGYHNEHHDFPAVPGSRL 273
Cdd:cd03507 151 YLVVNAWLvlitylqhtFPDIPWYRADEWNFAQAGLLgtvdRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
54-279 4.61e-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: 39.96  E-value: 4.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   54 QILALFVVKDLSWSWLI-VAAYCFGGIINHSLMLAVHEISHNLAFghsrpmHNRILG-FICNLPIGLPMSISFKKY---H 128
Cdd:cd03510   4 VIAAAVALALAWPNWLAyLLAVLLIGARQRALAILMHDAAHGLLF------RNRRLNdFLGNWLAAVPIFQSLAAYrrsH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  129 LEHHRYQGDEAiDTDIPTLLearlfdttfgkFLWvclqpffyiFRPLIinpkpptrleiinTVVQLtfnalivyfLGWkp 208
Cdd:cd03510  78 LKHHRHLGTED-DPDLALYL-----------LLW---------LVPLL-------------TVFPL---------IGR-- 112
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7297049  209 layllIGSILAMGLHPVAGHFISEHymfakgfeTYSYYGplNWIT------FNVGYHNEHHDFPAVPGSRLPEVKRI 279
Cdd:cd03510 113 -----IREIAEHAGVPADEDPDARN--------TRTTFG--GWIErllfapHNINYHLEHHLFPAVPFYNLPKAHRI 174
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
66-285 4.83e-04

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: 40.43  E-value: 4.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049   66 WSWLIVAAYCFG--GIINHSLMLAVHEISHNLAfgHSRPMHNRILGFICNLPIGLPMSIsFKKYHLEHHRYQGDEAIDTD 143
Cdd:cd03514  18 VISYLPLWVCFIlnTLSLHLAGTVIHDASHKAA--SRNRWINELIGHVSAFFLGFPFPV-FRRVHMQHHAHTNDPEKDPD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297049  144 IpTLLEarlfdttfgkfLWVCLQPFFYIFRPLIinpkpptrleiintvvqLTFNALIVYFLGWKPlaYLLIGSILAMGLH 223
Cdd:cd03514  95 H-FLLE-----------WLVARSLFITLLVIAI-----------------LFGFLWELLNLWFLP--ALIVGTYLALFFD 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7297049  224 pvaghfISEHYMF-AKGFETYSYYGP---LNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYD 285
Cdd:cd03514 144 ------WLPHHPFeETQRWDNSRVYPsklLNPLIMGQNYHLVHHLWPSIPWYRYPEAYYANKPLLD 203
 
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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