NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|348558148|ref|XP_003464880|]
View 

fatty acid desaturase 6 [Cavia porcellus]

Protein Classification

fatty acid desaturase family protein( domain architecture ID 1056)

fatty acid desaturase (FADS) family protein similar to membrane FADSs, which are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains, and to beta-carotene ketolase/oxygenases (CrtW-like) and hydroxylases (CrtR-like)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DesA super family cl34570
Fatty acid desaturase [Lipid transport and metabolism];
6-318 1.42e-14

Fatty acid desaturase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG3239:

Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 73.22  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148   6 APRQDGRAEQLLGELEALVKDVVRASSW--WERRGVDCAILVLSLLALPAGFLclrsenLLVFAVGIAVLGVCHYTLtvk 83
Cdd:COG3239    4 ATPLTPADEAELRALRARLRALLGRRDWryLLKLALTLALLAALWLLLSWSWL------ALLAALLLGLALAGLFSL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  84 gSHLATHNALSESKFWNNILALFFvEVCTAFPAEYAKYGHVKmHHGYTNVVGLGDSSTWKLPCLNR-------YVYMFLA 156
Cdd:COG3239   75 -GHDAGHGSLFRSRWLNDLLGRLL-GLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGVQAWRPlylfqhlLRFFLLG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 157 PFLIPIVTPLVALERLRKVGLRSALQTLGLISLGLYFHYWLLLHVSgfksPGSALACMLLTRsLLAHPYLHVNIF-QHIG 235
Cdd:COG3239  152 LGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLALG----WWAVLLFWLLPL-LVAGLLLGLRFYlEHRG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 236 LPMFSldkkPRRIHMMsLGVLNLPRLPVLDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQEKQLPYNEDSYLA 315
Cdd:COG3239  227 EDTGD----GEYRDQL-LGSRNIRGGRLLRWLFGN--LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLR 299


                 ...
gi 348558148 316 RFW 318
Cdd:COG3239  300 SYR 302
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
6-318 1.42e-14

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 73.22  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148   6 APRQDGRAEQLLGELEALVKDVVRASSW--WERRGVDCAILVLSLLALPAGFLclrsenLLVFAVGIAVLGVCHYTLtvk 83
Cdd:COG3239    4 ATPLTPADEAELRALRARLRALLGRRDWryLLKLALTLALLAALWLLLSWSWL------ALLAALLLGLALAGLFSL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  84 gSHLATHNALSESKFWNNILALFFvEVCTAFPAEYAKYGHVKmHHGYTNVVGLGDSSTWKLPCLNR-------YVYMFLA 156
Cdd:COG3239   75 -GHDAGHGSLFRSRWLNDLLGRLL-GLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGVQAWRPlylfqhlLRFFLLG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 157 PFLIPIVTPLVALERLRKVGLRSALQTLGLISLGLYFHYWLLLHVSgfksPGSALACMLLTRsLLAHPYLHVNIF-QHIG 235
Cdd:COG3239  152 LGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLALG----WWAVLLFWLLPL-LVAGLLLGLRFYlEHRG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 236 LPMFSldkkPRRIHMMsLGVLNLPRLPVLDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQEKQLPYNEDSYLA 315
Cdd:COG3239  227 EDTGD----GEYRDQL-LGSRNIRGGRLLRWLFGN--LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLR 299


                 ...
gi 348558148 316 RFW 318
Cdd:COG3239  300 SYR 302
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 85-303 3.93e-09

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583 [Multi-domain]  Cd Length: 204  Bit Score: 55.73  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  85 SHLATHNALSESKFWNNILALFFvEVCTAFPAEYAKYGHVKmHHGYTNVVGL-GDSSTwklpclnryvymflapflipiv 163
Cdd:cd03506   18 AHDAGHGQVFKNRWLNKLLGLTV-GNLLGASAGWWKNKHNV-HHAYTNILGHdPDIDT---------------------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 164 TPLVALerlrkvglRSALQTLGLISLGLYFHYWLLLHvsgfkspgsALACMLLTRSLLAH----PYLHVNIF-QHIGLPM 238
Cdd:cd03506   74 LPLLAR--------SEPAFGKDQKKRFLHRYQHFYFF---------PLLALLLLAFLVVQlaggLWLAVVFQlNHFGMPV 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348558148 239 FSLDKKPRR---IHMMSLGVlNLPRLPVLDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQE 303
Cdd:cd03506  137 EDPPGESKNdwlERQVLTTR-NITGSPFLDWLHGG--LNYQIEHHLFPTMPRHNYPKVAPLVRELCKK 201
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 65-310 6.64e-08

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 52.73  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148   65 VFAVGIAVLGVCHYTLTVKGSHLATHNALSESKF---WNNILALFFVEVCTAFPAEYAKYGHVkMHHGYTNVVGlGDSST 141
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRlnrWLNDLLGRLAGLPLGISYSAWRIAHL-VHHRYTNGPD-KDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  142 WKLPCLNRYVYMFLAPFLIPIVTPLVALERLRKVGLRSALQTLGLISLGLYFHYWL---------LLHVSGFKSPGSALA 212
Cdd:pfam00487  81 APLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIawllllaawLGLWLGFLGLGGLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  213 CMLLTRSLLAHPYLHV--NIFQHIGLPMFSLDKKPRRIHMMSLGVLNLprlpvldWAFGHSLiscHIEHHLFPTLSDNMC 290
Cdd:pfam00487 161 LLWLLPLLVFGFLLALifNYLEHYGGDWGERPVETTRSIRSPNWWLNL-------LTGNLNY---HIEHHLFPGVPWYRL 230

                         250       260
                  ....*....|....*....|
gi 348558148  291 LKVKPVVSKFLQEKQLPYNE 310
Cdd:pfam00487 231 PKLHRRLREALPEHGLPYRS 250
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 168-310 3.40e-04

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 168 ALErLRKVGLRSALqtlgLISLGLYFHY-WLLLHVSGFKSPGSALACMLLTRSLLAHPYLHVNIFQ--HIGLPMFSLDKK 244
Cdd:PLN03199 310 ALE-LEAKGLQYPL----LEKAGILLHYaWMFTLSSGFGRFSFAYSAFYFFTATASCGFFLAIVFGlgHNGMATYDADAR 384

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348558148 245 PRRIHMMSLGVLNL------PRLPVlDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQEKQLPYNE 310
Cdd:PLN03199 385 PDFWKLQVTTTRNIigghgfPQAFV-DWFCGG--LQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHE 453
 
Name Accession Description Interval E-value
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
6-318 1.42e-14

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 73.22  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148   6 APRQDGRAEQLLGELEALVKDVVRASSW--WERRGVDCAILVLSLLALPAGFLclrsenLLVFAVGIAVLGVCHYTLtvk 83
Cdd:COG3239    4 ATPLTPADEAELRALRARLRALLGRRDWryLLKLALTLALLAALWLLLSWSWL------ALLAALLLGLALAGLFSL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  84 gSHLATHNALSESKFWNNILALFFvEVCTAFPAEYAKYGHVKmHHGYTNVVGLGDSSTWKLPCLNR-------YVYMFLA 156
Cdd:COG3239   75 -GHDAGHGSLFRSRWLNDLLGRLL-GLPLGTPYDAWRRSHNR-HHAYTNDPGKDPDIGYGVQAWRPlylfqhlLRFFLLG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 157 PFLIPIVTPLVALERLRKVGLRSALQTLGLISLGLYFHYWLLLHVSgfksPGSALACMLLTRsLLAHPYLHVNIF-QHIG 235
Cdd:COG3239  152 LGGLYWLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLALG----WWAVLLFWLLPL-LVAGLLLGLRFYlEHRG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 236 LPMFSldkkPRRIHMMsLGVLNLPRLPVLDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQEKQLPYNEDSYLA 315
Cdd:COG3239  227 EDTGD----GEYRDQL-LGSRNIRGGRLLRWLFGN--LNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLR 299


                 ...
gi 348558148 316 RFW 318
Cdd:COG3239  300 SYR 302
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 85-303 3.93e-09

The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.


Pssm-ID: 239583 [Multi-domain]  Cd Length: 204  Bit Score: 55.73  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  85 SHLATHNALSESKFWNNILALFFvEVCTAFPAEYAKYGHVKmHHGYTNVVGL-GDSSTwklpclnryvymflapflipiv 163
Cdd:cd03506   18 AHDAGHGQVFKNRWLNKLLGLTV-GNLLGASAGWWKNKHNV-HHAYTNILGHdPDIDT---------------------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 164 TPLVALerlrkvglRSALQTLGLISLGLYFHYWLLLHvsgfkspgsALACMLLTRSLLAH----PYLHVNIF-QHIGLPM 238
Cdd:cd03506   74 LPLLAR--------SEPAFGKDQKKRFLHRYQHFYFF---------PLLALLLLAFLVVQlaggLWLAVVFQlNHFGMPV 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348558148 239 FSLDKKPRR---IHMMSLGVlNLPRLPVLDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQE 303
Cdd:cd03506  137 EDPPGESKNdwlERQVLTTR-NITGSPFLDWLHGG--LNYQIEHHLFPTMPRHNYPKVAPLVRELCKK 201
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 65-310 6.64e-08

Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme.


Pssm-ID: 425713 [Multi-domain]  Cd Length: 252  Bit Score: 52.73  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148   65 VFAVGIAVLGVCHYTLTVKGSHLATHNALSESKF---WNNILALFFVEVCTAFPAEYAKYGHVkMHHGYTNVVGlGDSST 141
Cdd:pfam00487   3 LALLLALLLGLFLLGITGSLAHEASHGALFKKRRlnrWLNDLLGRLAGLPLGISYSAWRIAHL-VHHRYTNGPD-KDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  142 WKLPCLNRYVYMFLAPFLIPIVTPLVALERLRKVGLRSALQTLGLISLGLYFHYWL---------LLHVSGFKSPGSALA 212
Cdd:pfam00487  81 APLASRFRGLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIawllllaawLGLWLGFLGLGGLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148  213 CMLLTRSLLAHPYLHV--NIFQHIGLPMFSLDKKPRRIHMMSLGVLNLprlpvldWAFGHSLiscHIEHHLFPTLSDNMC 290
Cdd:pfam00487 161 LLWLLPLLVFGFLLALifNYLEHYGGDWGERPVETTRSIRSPNWWLNL-------LTGNLNY---HIEHHLFPGVPWYRL 230

                         250       260
                  ....*....|....*....|
gi 348558148  291 LKVKPVVSKFLQEKQLPYNE 310
Cdd:pfam00487 231 PKLHRRLREALPEHGLPYRS 250
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 64-135 3.34e-04

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: 39.76  E-value: 3.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348558148  64 LVFAVGIAVLGVCHYTLtvkGSHLATHNALSESKFWNNILaLFFVEVCTAFPAEYAKYGHVKmHHGYTNVVG 135
Cdd:cd01060    1 LLLALLLGLLGGLGLTV---LAHELGHRSFFRSRWLNRLL-GALLGLALGGSYGWWRRSHRR-HHRYTNTPG 67
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 168-310 3.40e-04

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 168 ALErLRKVGLRSALqtlgLISLGLYFHY-WLLLHVSGFKSPGSALACMLLTRSLLAHPYLHVNIFQ--HIGLPMFSLDKK 244
Cdd:PLN03199 310 ALE-LEAKGLQYPL----LEKAGILLHYaWMFTLSSGFGRFSFAYSAFYFFTATASCGFFLAIVFGlgHNGMATYDADAR 384

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348558148 245 PRRIHMMSLGVLNL------PRLPVlDWAFGHslISCHIEHHLFPTLSDNMCLKVKPVVSKFLQEKQLPYNE 310
Cdd:PLN03199 385 PDFWKLQVTTTRNIigghgfPQAFV-DWFCGG--LQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHE 453
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 224-283 2.39e-03

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: 37.45  E-value: 2.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558148 224 PYLHVNIFQHIGLPMFSLDKKPRRIHmmslgVLNLPRLPVLDWAFGHslISCHIEHHLFP 283
Cdd:cd01060   70 PDSAVNYLEHYGGDRPFDTDGEWLRT-----TDNSRNGWLNLLLTGG--LGYHNEHHLFP 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH