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Conserved domains on  [gi|31543675|ref|NP_033153|]
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acyl-CoA desaturase 1 [Mus musculus]

Protein Classification

acyl-CoA desaturase (domain architecture ID 10131286)

acyl-CoA desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to acyl-CoA delta(9) desaturase and acyl-CoA delta(11) desaturase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
93-333 9.03e-83

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. 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: HXXXXH, HXXHH, and H/QXXHH. These 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. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


:

Pssm-ID: 239582  Cd Length: 178  Bit Score: 249.01  E-value: 9.03e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  93 KLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRG 172
Cdd:cd03505   1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 173 FFFSHVGWLLVrkhpavkekggkldmsdlkaeklvmfqrryykpglllmcfilptlvpwycwgetfvnslfvstFLRYTL 252
Cdd:cd03505  81 FWFSHVGWLGG---------------------------------------------------------------LLRIVL 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 253 VLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFIDCMAALGLAYDR 332
Cdd:cd03505  98 VLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDL 177

                .
gi 31543675 333 K 333
Cdd:cd03505 178 K 178
 
Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
93-333 9.03e-83

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. 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: HXXXXH, HXXHH, and H/QXXHH. These 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. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


Pssm-ID: 239582  Cd Length: 178  Bit Score: 249.01  E-value: 9.03e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  93 KLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRG 172
Cdd:cd03505   1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 173 FFFSHVGWLLVrkhpavkekggkldmsdlkaeklvmfqrryykpglllmcfilptlvpwycwgetfvnslfvstFLRYTL 252
Cdd:cd03505  81 FWFSHVGWLGG---------------------------------------------------------------LLRIVL 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 253 VLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFIDCMAALGLAYDR 332
Cdd:cd03505  98 VLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDL 177

                .
gi 31543675 333 K 333
Cdd:cd03505 178 K 178
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
63-338 1.67e-63

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 224316  Cd Length: 289  Bit Score: 203.77  E-value: 1.67e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  63 PKLEYVWRNIILMVLLHLGGLYGIILVPSCKLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAF 142
Cdd:COG1398  14 PKYPYHWNNVLFFIGPLIVAYLAFYPDFFSWLAELIFTLAYYLIGGIGITLGLHRLWSHRAFKAHKWLEYVLAFWGALTT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 143 QNDVYEWARDHRAHHKFSETHADPH-NSRRGFFFSHVGWLLVRKhpavKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLM 221
Cdd:COG1398  94 QGPAIEWVGIHRKHHRKTDTDQDPHyDSFKGFWWSHIGWMLLYS----AEAKDRETIQKLGKDIPLDWQHRNLYLIALLM 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 222 CFILPTLVPWYCWGETFvnsLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFP 301
Cdd:COG1398 170 QIVLPLFIGYALGGWLG---LIWGGVQRLVLVQHATWCVNSLGHYIGYRPFDCRDTARNCWWVALVTFGEGWHNNHHAFP 246
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 31543675 302 FDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKA 338
Cdd:COG1398 247 NSARNGLKWWEFDVTWWIIKLLSLLGLAKVVKLAPKA 283
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
99-338 9.78e-31

delta-9 acyl-lipid desaturase


Pssm-ID: 177866  Cd Length: 299  Bit Score: 118.37  E-value: 9.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675   99 FGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHV 178
Cdd:PLN02220  60 FGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  179 GWLLVRKHpaVKEK-GGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTL--VPWYCWGetfvnsLFVSTFLRYtlvlN 255
Cdd:PLN02220 140 LWIFDTSY--IREKcGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWggLPYLTWG------VGVGGAIGY----H 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  256 ATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFIDCMAALGLAYDRKKV 335
Cdd:PLN02220 208 VTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEVLGLATDVKLP 287

                 ...
gi 31543675  336 SKA 338
Cdd:PLN02220 288 TEA 290
FA_desaturase pfam00487
Fatty acid desaturase;
98-301 7.82e-08

Fatty acid desaturase;


Pssm-ID: 395391 [Multi-domain]  Cd Length: 253  Bit Score: 52.73  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675    98 LFGIFYYMTSALGITAGAHRLWSHRTYKARLPLR----IFLIIANTMAFQNDVYEWARDHRAHHKFSETH-ADPH----- 167
Cdd:pfam00487   6 LLALLLGLFLLLGITGVLAHEASHGALFKKRRLNrwlnDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPdEDPDtapla 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675   168 NSRRGFFFSHVGWLLVRKHPAVKEKGGKLD-MSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCW-GETFVNSLFVS 245
Cdd:pfam00487  86 SRFRGLLRYLLRWLLGLLVLAWLLALVLGLwARRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFlGLGGLLLLLWL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675   246 TFLRYTLVLNATWLvNSAAHLYGYRPYDKNIQSRE----NILVSLGAVGEGFHNYHHTFP 301
Cdd:pfam00487 166 LPLLVAGFLLALIF-NYLEHYGGDWGERPVETTRSirspNWWLNLLTGNLNYHIEHHLFP 224
 
Name Accession Description Interval E-value
Delta9-FADS-like cd03505
The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl ...
93-333 9.03e-83

The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. 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: HXXXXH, HXXHH, and H/QXXHH. These 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. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.


Pssm-ID: 239582  Cd Length: 178  Bit Score: 249.01  E-value: 9.03e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  93 KLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRG 172
Cdd:cd03505   1 SWATLVFLVLYYLLTGLGITAGYHRLWAHRSFKAPKPLRIFLAILGSLAGQGSPLWWVADHRLHHRYSDTDGDPHSPKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 173 FFFSHVGWLLVrkhpavkekggkldmsdlkaeklvmfqrryykpglllmcfilptlvpwycwgetfvnslfvstFLRYTL 252
Cdd:cd03505  81 FWFSHVGWLGG---------------------------------------------------------------LLRIVL 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 253 VLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFIDCMAALGLAYDR 332
Cdd:cd03505  98 VLHATWLVNSLAHMWGYRPYDTRDTSRNNWWVALLTFGEGWHNNHHAFPGDARNGLKWYQIDPTKWVIRLLEKLGLAWDL 177

                .
gi 31543675 333 K 333
Cdd:cd03505 178 K 178
OLE1 COG1398
Fatty-acid desaturase [Lipid transport and metabolism];
63-338 1.67e-63

Fatty-acid desaturase [Lipid transport and metabolism];


Pssm-ID: 224316  Cd Length: 289  Bit Score: 203.77  E-value: 1.67e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  63 PKLEYVWRNIILMVLLHLGGLYGIILVPSCKLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAF 142
Cdd:COG1398  14 PKYPYHWNNVLFFIGPLIVAYLAFYPDFFSWLAELIFTLAYYLIGGIGITLGLHRLWSHRAFKAHKWLEYVLAFWGALTT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 143 QNDVYEWARDHRAHHKFSETHADPH-NSRRGFFFSHVGWLLVRKhpavKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLM 221
Cdd:COG1398  94 QGPAIEWVGIHRKHHRKTDTDQDPHyDSFKGFWWSHIGWMLLYS----AEAKDRETIQKLGKDIPLDWQHRNLYLIALLM 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675 222 CFILPTLVPWYCWGETFvnsLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFP 301
Cdd:COG1398 170 QIVLPLFIGYALGGWLG---LIWGGVQRLVLVQHATWCVNSLGHYIGYRPFDCRDTARNCWWVALVTFGEGWHNNHHAFP 246
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 31543675 302 FDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKA 338
Cdd:COG1398 247 NSARNGLKWWEFDVTWWIIKLLSLLGLAKVVKLAPKA 283
PLN02220 PLN02220
delta-9 acyl-lipid desaturase
99-338 9.78e-31

delta-9 acyl-lipid desaturase


Pssm-ID: 177866  Cd Length: 299  Bit Score: 118.37  E-value: 9.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675   99 FGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHV 178
Cdd:PLN02220  60 FGLILYIVTGLSITFSYHRNLAHRSFKLPKWLEYPFAYSALFALQGDPIDWVSTHRFHHQFTDSDRDPHSPIEGFWFSHV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  179 GWLLVRKHpaVKEK-GGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTL--VPWYCWGetfvnsLFVSTFLRYtlvlN 255
Cdd:PLN02220 140 LWIFDTSY--IREKcGGRDNVMDLKQQWFYRFLRKTIGLHILMFWTLLYLWggLPYLTWG------VGVGGAIGY----H 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  256 ATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFIDCMAALGLAYDRKKV 335
Cdd:PLN02220 208 VTWLINSACHIWGSRTWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRFFEVLGLATDVKLP 287

                 ...
gi 31543675  336 SKA 338
Cdd:PLN02220 288 TEA 290
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
98-179 5.74e-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: 56.32  E-value: 5.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675  98 LFGIFYYMTSALGITAGAHRLwSHRTY-KARLPLRIFLIIANtMAFQNDVYEWARDHRAHHKFSETH-ADPHNSRrgFFF 175
Cdd:cd01060   2 LLALLLGLLGGLGLTVLAHEL-GHRSFfRSRWLNRLLGALLG-LALGGSYGWWRRSHRRHHRYTNTPgKDPDSAV--NYL 77

                ....
gi 31543675 176 SHVG 179
Cdd:cd01060  78 EHYG 81
FA_desaturase pfam00487
Fatty acid desaturase;
98-301 7.82e-08

Fatty acid desaturase;


Pssm-ID: 395391 [Multi-domain]  Cd Length: 253  Bit Score: 52.73  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675    98 LFGIFYYMTSALGITAGAHRLWSHRTYKARLPLR----IFLIIANTMAFQNDVYEWARDHRAHHKFSETH-ADPH----- 167
Cdd:pfam00487   6 LLALLLGLFLLLGITGVLAHEASHGALFKKRRLNrwlnDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPdEDPDtapla 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675   168 NSRRGFFFSHVGWLLVRKHPAVKEKGGKLD-MSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCW-GETFVNSLFVS 245
Cdd:pfam00487  86 SRFRGLLRYLLRWLLGLLVLAWLLALVLGLwARRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGFlGLGGLLLLLWL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543675   246 TFLRYTLVLNATWLvNSAAHLYGYRPYDKNIQSRE----NILVSLGAVGEGFHNYHHTFP 301
Cdd:pfam00487 166 LPLLVAGFLLALIF-NYLEHYGGDWGERPVETTRSirspNWWLNLLTGNLNYHIEHHLFP 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
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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