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Conserved domains on  [gi|2462525142|ref|XP_054224723|]
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acyl-CoA (8-3)-desaturase isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 147-398 5.27e-69

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: 217.51  E-value: 5.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 147 LLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA 226
Cdd:cd03506     1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 227 LGKILsvelGKQKKKYMPYNHQHKYFFLIGPPALLplyfqwyifyfviqrkkwvdlawmitfyvrffltyvpllglkafl 306
Cdd:cd03506    80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL--------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 307 gLFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYH 383
Cdd:cd03506   111 -AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189

                         250
                  ....*....|....*
gi 2462525142 384 KVAPLVQSLCAKHGI 398
Cdd:cd03506   190 KVAPLVRELCKKHGL 204
DUF502 super family cl01107
Protein of unknown function (DUF502); Predicted to be an integral membrane protein.
 250-330 3.18e-05

Protein of unknown function (DUF502); Predicted to be an integral membrane protein.


The actual alignment was detected with superfamily member COG2928:

Pssm-ID: 470075  Cd Length: 208  Bit Score: 44.79  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 250 KYFF--LIgppALLPLYFQWYIFYFVIQrkkWVD--LAWMITFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFV---- 321
Cdd:COG2928     8 RYFLtgLL---VLLPLAITLYVLWWLFG---WLDglLGPLLKLLLPELGFYIPGLGLVVLLLLILLIGLLARNFLGrrll 81

                          90
                  ....*....|.
gi 2462525142 322 --WVTQMNHIP 330
Cdd:COG2928    82 rlGERLLNRIP 92
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 147-398 5.27e-69

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: 217.51  E-value: 5.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 147 LLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA 226
Cdd:cd03506     1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 227 LGKILsvelGKQKKKYMPYNHQHKYFFLIGPPALLplyfqwyifyfviqrkkwvdlawmitfyvrffltyvpllglkafl 306
Cdd:cd03506    80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL--------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 307 gLFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYH 383
Cdd:cd03506   111 -AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189

                         250
                  ....*....|....*
gi 2462525142 384 KVAPLVQSLCAKHGI 398
Cdd:cd03506   190 KVAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
131-421 7.72e-44

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 155.66  E-value: 7.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 131 AAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFvIGHLKGAPASWWNHMHFQHHAKPN 210
Cdd:COG3239    42 ALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRL-LGLPLGTPYDAWRRSHNRHHAYTN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 211 CFRKDPDINMHPfffalgkilsvelgkqkkkyMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQ-------RKKWVDLA 283
Cdd:COG3239   121 DPGKDPDIGYGV--------------------QAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPlrgrlelKERRLEAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 284 WMITFYVRFFLTYVpLLGLKAFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDwvstQLQATCNVHKSAFNDWFSG 363
Cdd:COG3239   181 LLLLFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFG 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462525142 364 HLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQ 421
Cdd:COG3239   256 NLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 55-418 2.07e-41

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 153.69  E-value: 2.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142  55 DPFVAFHinKGLVKKYMNSLLIGELSpeqpSFEPTKnkELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAwL 134
Cdd:PLN03198  154 DAFSSFH--AASTWKILQDFYIGDVD----NVEPTP--ELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAAS-I 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 135 TLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFR 213
Cdd:PLN03198  225 AIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 214 K----DPDINMHPFFFALGKILSVELGKQKKKYMPYNHqhkyffligppallpLYFQWYIFYfviQRKKWVDLAWMITFY 289
Cdd:PLN03198  305 LyqpiDEDIDTLPLIAWSKDILATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTST 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 290 VRffLTYVPLLGLKAFLgLFFIVRFLESNWF--------VW--VTQM------------NHIPMHIdHDRNMDWVSTQLQ 347
Cdd:PLN03198  367 AK--LAPADRLLEKGTI-LFHYFWFIGTACYllpgwkplVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIV 442

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462525142 348 ATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKE 418
Cdd:PLN03198  443 STRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 142-404 9.73e-23

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: 96.65  E-value: 9.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 142 SFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFV---IGHLKGAPASWWNHMHFQHHAKPNCFRKDPDI 218
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 219 NMHPFFFAlgkilsvELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKkWVDLAWMItFYVRFFLTYVP 298
Cdd:pfam00487  81 APLASRFR-------GLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRR-WRLIAWLL-LLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 299 LLGLKAFLGLFFIVRFLESNWF--VWVTQMNHIPMhidhdrnmDWVSTQLQATCNVHK-SAFNDWFSGHLNFQIEHHLFP 375
Cdd:pfam00487 152 FLGLGGLLLLLWLLPLLVFGFLlaLIFNYLEHYGG--------DWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFP 223

                         250       260
                  ....*....|....*....|....*....
gi 2462525142 376 TMPRHNYHKVAPLVQSLCAKHGIEYQSKP 404
Cdd:pfam00487 224 GVPWYRLPKLHRRLREALPEHGLPYRSLG 252
COG2928 COG2928
Uncharacterized membrane protein [Function unknown];
250-330 3.18e-05

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 442172  Cd Length: 208  Bit Score: 44.79  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 250 KYFF--LIgppALLPLYFQWYIFYFVIQrkkWVD--LAWMITFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFV---- 321
Cdd:COG2928     8 RYFLtgLL---VLLPLAITLYVLWWLFG---WLDglLGPLLKLLLPELGFYIPGLGLVVLLLLILLIGLLARNFLGrrll 81

                          90
                  ....*....|.
gi 2462525142 322 --WVTQMNHIP 330
Cdd:COG2928    82 rlGERLLNRIP 92
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 147-398 5.27e-69

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: 217.51  E-value: 5.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 147 LLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFA 226
Cdd:cd03506     1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 227 LGKILsvelGKQKKKYMPYNHQHKYFFLIGPPALLplyfqwyifyfviqrkkwvdlawmitfyvrffltyvpllglkafl 306
Cdd:cd03506    80 SEPAF----GKDQKKRFLHRYQHFYFFPLLALLLL--------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 307 gLFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYH 383
Cdd:cd03506   111 -AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYP 189

                         250
                  ....*....|....*
gi 2462525142 384 KVAPLVQSLCAKHGI 398
Cdd:cd03506   190 KVAPLVRELCKKHGL 204
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
131-421 7.72e-44

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 155.66  E-value: 7.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 131 AAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFvIGHLKGAPASWWNHMHFQHHAKPN 210
Cdd:COG3239    42 ALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRL-LGLPLGTPYDAWRRSHNRHHAYTN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 211 CFRKDPDINMHPfffalgkilsvelgkqkkkyMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQ-------RKKWVDLA 283
Cdd:COG3239   121 DPGKDPDIGYGV--------------------QAWRPLYLFQHLLRFFLLGLGGLYWLLALDFLPlrgrlelKERRLEAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 284 WMITFYVRFFLTYVpLLGLKAFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDwvstQLQATCNVHKSAFNDWFSG 363
Cdd:COG3239   181 LLLLFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFG 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462525142 364 HLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQ 421
Cdd:COG3239   256 NLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 55-418 2.07e-41

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 153.69  E-value: 2.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142  55 DPFVAFHinKGLVKKYMNSLLIGELSpeqpSFEPTKnkELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAwL 134
Cdd:PLN03198  154 DAFSSFH--AASTWKILQDFYIGDVD----NVEPTP--ELLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFAAS-I 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 135 TLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFR 213
Cdd:PLN03198  225 AIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 214 K----DPDINMHPFFFALGKILSVELGKQKKKYMPYNHqhkyffligppallpLYFQWYIFYfviQRKKWVDLAWMITFY 289
Cdd:PLN03198  305 LyqpiDEDIDTLPLIAWSKDILATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTST 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 290 VRffLTYVPLLGLKAFLgLFFIVRFLESNWF--------VW--VTQM------------NHIPMHIdHDRNMDWVSTQLQ 347
Cdd:PLN03198  367 AK--LAPADRLLEKGTI-LFHYFWFIGTACYllpgwkplVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIV 442

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462525142 348 ATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKE 418
Cdd:PLN03198  443 STRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 55-425 8.78e-35

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 134.78  E-value: 8.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142  55 DPFVAFHI--NKGLVKKYMnsllIGELSPEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHilllDGAA 132
Cdd:PLN03199   73 DIFAAFHApgSQALMKKFY----IGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLF----NMAI 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 133 WL---TLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKP 209
Cdd:PLN03199  145 WAaacALVFYSDRFAMHIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVP 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 210 NCFRK-------DPDINMHPFF-FALGKILSV-ELGKQKK-----KYMPYNHQHKYFfligpPALLPLYFQWYIFYF--- 272
Cdd:PLN03199  225 NLHCSsadaqdgDPDIDTMPLLaWSLKQAQSFrEINADGKdsgfvKFAIKFQAFFYF-----PILLLARISWLNESFkca 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 273 ----------VIQRKK-------------WVDLAWMITF---YVRFFLTYVPLLGLKAFL--GLFFIVRFlesnwfvwvt 324
Cdd:PLN03199  300 fglgaasenaALELEAkglqypllekagiLLHYAWMFTLssgFGRFSFAYSAFYFFTATAscGFFLAIVF---------- 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 325 QMNHIPMHI-DHDRNMDWVSTQLQATCNV-----HKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGI 398
Cdd:PLN03199  370 GLGHNGMATyDADARPDFWKLQVTTTRNIigghgFPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGV 449

                         410       420
                  ....*....|....*....|....*...
gi 2462525142 399 EYQSKPLLSAFADIIHSL-KESGQLWLD 425
Cdd:PLN03199  450 KYHEADLVDGTMEVLHHLgKVADDFLVD 477
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 142-404 9.73e-23

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: 96.65  E-value: 9.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 142 SFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFV---IGHLKGAPASWWNHMHFQHHAKPNCFRKDPDI 218
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 219 NMHPFFFAlgkilsvELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKkWVDLAWMItFYVRFFLTYVP 298
Cdd:pfam00487  81 APLASRFR-------GLLRYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRR-WRLIAWLL-LLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 299 LLGLKAFLGLFFIVRFLESNWF--VWVTQMNHIPMhidhdrnmDWVSTQLQATCNVHK-SAFNDWFSGHLNFQIEHHLFP 375
Cdd:pfam00487 152 FLGLGGLLLLLWLLPLLVFGFLlaLIFNYLEHYGG--------DWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFP 223

                         250       260
                  ....*....|....*....|....*....
gi 2462525142 376 TMPRHNYHKVAPLVQSLCAKHGIEYQSKP 404
Cdd:pfam00487 224 GVPWYRLPKLHRRLREALPEHGLPYRSLG 252
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 129-383 1.13e-13

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 [Multi-domain]  Cd Length: 222  Bit Score: 69.95  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 129 DGAAWLTLWVFGTSFLPFLLCAvLLSAVQAQAGW----LQHDFGHLSVFSTSKWNHLLHHfVIGHLKGAPASWWNHMHFQ 204
Cdd:cd03507    13 DILLLALLALAASLLLSWWLWP-LYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIVGH-ILHSPLLVPYHSWRISHNR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 205 HHAKPNCFRKDpdINMHPfffalgkilsvelgKQKKKYMPYNHQHKYFFLIGPPALLPLyfqwyifyfviqrkkwvdlAW 284
Cdd:cd03507    91 HHAHTGNLEGD--EVWVP--------------VTEEEYAELPKRLPYRLYRNPFLMLSL-------------------GW 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 285 MITFYVRFFLTY-VPLLGLKAflglffivrflesnWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKS--AFNDWF 361
Cdd:cd03507   136 PYYLLLNVLLYYlIPYLVVNA--------------WLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDygGWLNWL 201

                         250       260
                  ....*....|....*....|..
gi 2462525142 362 SGHLNFQIEHHLFPTMPrhNYH 383
Cdd:cd03507   202 THIIGTHVAHHLFPRIP--HYN 221
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 146-218 2.24e-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: 57.86  E-value: 2.24e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462525142 146 FLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLkGAPASWWNHMHFQHHAKPNCFRKDPDI 218
Cdd:cd01060     1 LLLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDS 72
COG2928 COG2928
Uncharacterized membrane protein [Function unknown];
250-330 3.18e-05

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 442172  Cd Length: 208  Bit Score: 44.79  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 250 KYFF--LIgppALLPLYFQWYIFYFVIQrkkWVD--LAWMITFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFV---- 321
Cdd:COG2928     8 RYFLtgLL---VLLPLAITLYVLWWLFG---WLDglLGPLLKLLLPELGFYIPGLGLVVLLLLILLIGLLARNFLGrrll 81

                          90
                  ....*....|.
gi 2462525142 322 --WVTQMNHIP 330
Cdd:COG2928    82 rlGERLLNRIP 92
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 131-218 4.99e-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 [Multi-domain]  Cd Length: 207  Bit Score: 38.12  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525142 131 AAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHfVIGHLKGAPASWWNHMHFQHHAKPN 210
Cdd:cd03514     9 LVWLSTWGYVISYLPLWVCFILNTLSLHLAGTVIHDASHKAASRNRWINELIGH-VSAFFLGFPFPVFRRVHMQHHAHTN 87


                  ....*...
gi 2462525142 211 CFRKDPDI 218
Cdd:cd03514    88 DPEKDPDH 95
 
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.
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