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Conserved domains on  [gi|162287208|ref|NP_445897|]
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acyl-CoA (8-3)-desaturase [Rattus norvegicus]

Protein Classification

fatty acid desaturase( domain architecture ID 13289118)

fatty acid desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond

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: ...
165-415 1.35e-67

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: 214.43  E-value: 1.35e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 165 LCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFAL 244
Cdd:cd03506    2 LLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 245 GKVLsvelGKEKKKHMPYNHQHKYFFLIGPPALLplyfqwyifyfvvqrkkwvdlawmlsfyvrvfftympllglkgllc 324
Cdd:cd03506   81 EPAF----GKDQKKRFLHRYQHFYFFPLLALLLL---------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 325 LFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYHK 401
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190
                        250
                 ....*....|....
gi 162287208 402 VAPLVQSLCAKYGI 415
Cdd:cd03506  191 VAPLVRELCKKHGL 204
PLN03198 super family cl31981
delta6-acyl-lipid desaturase; Provisional
13-435 2.98e-52

delta6-acyl-lipid desaturase; Provisional


The actual alignment was detected with superfamily member PLN03198:

Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 183.74  E-value: 2.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  13 SAQLRQMRYFTWEEVAQRSgREKERWLVIDRKVYNISDFSRRHPGGSrVISHYAGQDATDPFVAFHinKGLVRKYMNSLL 92
Cdd:PLN03198  97 SSKEKKSKSHLLSEVAAHN-KPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFH--AASTWKILQDFY 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  93 IGELAPEQPSFEptknkaLTDEFRELRATVERMGLMKANHLFFLFYLLHILLLdVAAWLTLWIFGTSLVPFTLCAVLLST 172
Cdd:PLN03198 173 IGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAI-FAASIAIICCSKSISAVLASACMMAL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 173 VQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPLFFALGKV 247
Cdd:PLN03198 246 CFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLIAWSKDI 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 248 LSVELGKEKKKHMPYNHqhkyffligppallpLYFQWYIFYfvvQRKKWVDLAWMLSFYVRVFFTYMPLLGLKGLLCLFF 327
Cdd:PLN03198 326 LATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAKLAPADRLLEKGTILFHYFW 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 328 IVR---FLESNW--FVW--VTQM------------NHIPMHIdHDRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEH 388
Cdd:PLN03198 388 FIGtacYLLPGWkpLVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEH 466
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 162287208 389 HLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKE 435
Cdd:PLN03198 467 HLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
165-415 1.35e-67

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: 214.43  E-value: 1.35e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 165 LCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFAL 244
Cdd:cd03506    2 LLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 245 GKVLsvelGKEKKKHMPYNHQHKYFFLIGPPALLplyfqwyifyfvvqrkkwvdlawmlsfyvrvfftympllglkgllc 324
Cdd:cd03506   81 EPAF----GKDQKKRFLHRYQHFYFFPLLALLLL---------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 325 LFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYHK 401
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190
                        250
                 ....*....|....
gi 162287208 402 VAPLVQSLCAKYGI 415
Cdd:cd03506  191 VAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
13-435 2.98e-52

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 183.74  E-value: 2.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  13 SAQLRQMRYFTWEEVAQRSgREKERWLVIDRKVYNISDFSRRHPGGSrVISHYAGQDATDPFVAFHinKGLVRKYMNSLL 92
Cdd:PLN03198  97 SSKEKKSKSHLLSEVAAHN-KPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFH--AASTWKILQDFY 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  93 IGELAPEQPSFEptknkaLTDEFRELRATVERMGLMKANHLFFLFYLLHILLLdVAAWLTLWIFGTSLVPFTLCAVLLST 172
Cdd:PLN03198 173 IGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAI-FAASIAIICCSKSISAVLASACMMAL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 173 VQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPLFFALGKV 247
Cdd:PLN03198 246 CFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLIAWSKDI 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 248 LSVELGKEKKKHMPYNHqhkyffligppallpLYFQWYIFYfvvQRKKWVDLAWMLSFYVRVFFTYMPLLGLKGLLCLFF 327
Cdd:PLN03198 326 LATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAKLAPADRLLEKGTILFHYFW 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 328 IVR---FLESNW--FVW--VTQM------------NHIPMHIdHDRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEH 388
Cdd:PLN03198 388 FIGtacYLLPGWkpLVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEH 466
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 162287208 389 HLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKE 435
Cdd:PLN03198 467 HLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
147-438 2.98e-39

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 143.72  E-value: 2.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 147 VAAWLTLWIFGTSLVPFTLCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFvIGHLKGAPASWWNHMHFQHHAKP 226
Cdd:COG3239   41 LALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRL-LGLPLGTPYDAWRRSHNRHHAYT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 227 NCFRKDPDINmhplffalgkvlsvelGKEKKKHMPYNHQHKY-FFLIGPPALLPLYFQWYIFYF--VVQRKKWVDLAWML 303
Cdd:COG3239  120 NDPGKDPDIG----------------YGVQAWRPLYLFQHLLrFFLLGLGGLYWLLALDFLPLRgrLELKERRLEALLLL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 304 SFYVRVFFTYMpLLGLKGLLCLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNVDwvstQLQATCNVHQSAFNNWFSGHLN 383
Cdd:COG3239  184 LFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNLN 258
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287208 384 FQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKESGQ 438
Cdd:COG3239  259 YHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
23-97 7.05e-24

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 94.61  E-value: 7.05e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162287208   23 TWEEVAQRSGrEKERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHINKGLVRKYMNSLLIGELA 97
Cdd:pfam00173   1 TLEELSKHNG-DGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGELA 74
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
159-417 6.47e-20

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: 88.94  E-value: 6.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  159 SLVPFTLCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFV---IGHLKGAPASWWNHMHFQHHAKPNCFRKDPDI 235
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  236 NMHPLFFALGKVLSVelgkekkkHMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVVQRKKWVDLAWMLSFYVRVFFTYMP 315
Cdd:pfam00487  81 APLASRFRGLLRYLL--------RWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  316 LLGLKGLLCLFFI-VRFLESNWFVWVTQMNHIPmhidhdrnVDWVSTQLQATCNVHQ-SAFNNWFSGHLNFQIEHHLFPT 393
Cdd:pfam00487 153 LGLGGLLLLLWLLpLLVFGFLLALIFNYLEHYG--------GDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPG 224
                         250       260
                  ....*....|....*....|....
gi 162287208  394 MPRHNYHKVAPLVQSLCAKYGIKY 417
Cdd:pfam00487 225 VPWYRLPKLHRRLREALPEHGLPY 248
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
1-97 6.36e-13

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 64.29  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208   1 MAPDPVQTPDPASAQlrqmRYFTWEEVAQRSGREkERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHIN 80
Cdd:COG5274    1 MKKNTTPATDAAAPE----KTYTLAEVATHNTLS-DCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPH 75
                         90
                 ....*....|....*..
gi 162287208  81 KGLVRKYMNSLLIGELA 97
Cdd:COG5274   76 SPKAERLLESYRIGRLA 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: ...
165-415 1.35e-67

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: 214.43  E-value: 1.35e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 165 LCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGhLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFAL 244
Cdd:cd03506    2 LLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLARS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 245 GKVLsvelGKEKKKHMPYNHQHKYFFLIGPPALLplyfqwyifyfvvqrkkwvdlawmlsfyvrvfftympllglkgllc 324
Cdd:cd03506   81 EPAF----GKDQKKRFLHRYQHFYFFPLLALLLL---------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 325 LFFIVRFLESNWFVWVTQMNHIPMHIDH---DRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYHK 401
Cdd:cd03506  111 AFLVVQLAGGLWLAVVFQLNHFGMPVEDppgESKNDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190
                        250
                 ....*....|....
gi 162287208 402 VAPLVQSLCAKYGI 415
Cdd:cd03506  191 VAPLVRELCKKHGL 204
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
13-435 2.98e-52

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 183.74  E-value: 2.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  13 SAQLRQMRYFTWEEVAQRSgREKERWLVIDRKVYNISDFSRRHPGGSrVISHYAGQDATDPFVAFHinKGLVRKYMNSLL 92
Cdd:PLN03198  97 SSKEKKSKSHLLSEVAAHN-KPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFH--AASTWKILQDFY 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  93 IGELAPEQPSFEptknkaLTDEFRELRATVERMGLMKANHLFFLFYLLHILLLdVAAWLTLWIFGTSLVPFTLCAVLLST 172
Cdd:PLN03198 173 IGDVDNVEPTPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAI-FAASIAIICCSKSISAVLASACMMAL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 173 VQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGHLKGAPASWWNHMHFQHHAKPN-CFRK----DPDINMHPLFFALGKV 247
Cdd:PLN03198 246 CFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHNLHHAAPNeCDQLyqpiDEDIDTLPLIAWSKDI 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 248 LSVELGKEKKKHMPYNHqhkyffligppallpLYFQWYIFYfvvQRKKWVDLAWMLSFYVRVFFTYMPLLGLKGLLCLFF 327
Cdd:PLN03198 326 LATVENKTFLRILQYQH---------------LFFMALLFF---ARGSWLFWSWRYTSTAKLAPADRLLEKGTILFHYFW 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 328 IVR---FLESNW--FVW--VTQM------------NHIPMHIdHDRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEH 388
Cdd:PLN03198 388 FIGtacYLLPGWkpLVWmaVTELmcgmllgfvfvlSHNGMEV-YNKSKEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEH 466
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 162287208 389 HLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKE 435
Cdd:PLN03198 467 HLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKE 513
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
12-442 1.93e-43

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 159.05  E-value: 1.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  12 ASAQLRQMRYFTWEEVAQRSGREkERWLVIDRKVYNISDFsRRHPGGSRVISHyAGQDATDPFVAFHINKGlvRKYMNSL 91
Cdd:PLN03199  16 ALKLAEKPQKISWQEVKKHASPD-DAWIIHQNKVYDVSNW-HDHPGGAVIFTH-AGDDMTDIFAAFHAPGS--QALMKKF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  92 LIGELAPEQPSFEPTKNKALTDEFRELRATVERMGLMKANHLFFLFYLLHilllDVAAWL---TLWIFGTSLVPFTLCAV 168
Cdd:PLN03199  91 YIGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLF----NMAIWAaacALVFYSDRFAMHIASAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 169 LLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRK-------DPDINMHPLF 241
Cdd:PLN03199 167 LLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqdgDPDIDTMPLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 242 -FALGKVLSV-ELGKEKK-----KHMPYNHQHKYFfligpPALLPLYFQWYIFYF-------------VVQRKK------ 295
Cdd:PLN03199 247 aWSLKQAQSFrEINADGKdsgfvKFAIKFQAFFYF-----PILLLARISWLNESFkcafglgaasenaALELEAkglqyp 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 296 -------WVDLAWML---SFYVRVFFTYmpllglkglLCLFFIVRFLESNWFV-WVTQMNHIPMHI-DHDRNVDWVSTQL 363
Cdd:PLN03199 322 llekagiLLHYAWMFtlsSGFGRFSFAY---------SAFYFFTATASCGFFLaIVFGLGHNGMATyDADARPDFWKLQV 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 364 QATCNV-----HQSAFNNWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSL-KESG 437
Cdd:PLN03199 393 TTTRNIigghgFPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEADLVDGTMEVLHHLgKVAD 472

                 ....*
gi 162287208 438 QLWLD 442
Cdd:PLN03199 473 DFLVD 477
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
147-438 2.98e-39

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 143.72  E-value: 2.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 147 VAAWLTLWIFGTSLVPFTLCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFvIGHLKGAPASWWNHMHFQHHAKP 226
Cdd:COG3239   41 LALLAALWLLLSWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLGRL-LGLPLGTPYDAWRRSHNRHHAYT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 227 NCFRKDPDINmhplffalgkvlsvelGKEKKKHMPYNHQHKY-FFLIGPPALLPLYFQWYIFYF--VVQRKKWVDLAWML 303
Cdd:COG3239  120 NDPGKDPDIG----------------YGVQAWRPLYLFQHLLrFFLLGLGGLYWLLALDFLPLRgrLELKERRLEALLLL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 304 SFYVRVFFTYMpLLGLKGLLCLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNVDwvstQLQATCNVHQSAFNNWFSGHLN 383
Cdd:COG3239  184 LFLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNLN 258
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162287208 384 FQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKESGQ 438
Cdd:COG3239  259 YHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLRLLRRLGL 313
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
23-97 7.05e-24

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 94.61  E-value: 7.05e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162287208   23 TWEEVAQRSGrEKERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHINKGLVRKYMNSLLIGELA 97
Cdd:pfam00173   1 TLEELSKHNG-DGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGELA 74
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
159-417 6.47e-20

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: 88.94  E-value: 6.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  159 SLVPFTLCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFV---IGHLKGAPASWWNHMHFQHHAKPNCFRKDPDI 235
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  236 NMHPLFFALGKVLSVelgkekkkHMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVVQRKKWVDLAWMLSFYVRVFFTYMP 315
Cdd:pfam00487  81 APLASRFRGLLRYLL--------RWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLGF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208  316 LLGLKGLLCLFFI-VRFLESNWFVWVTQMNHIPmhidhdrnVDWVSTQLQATCNVHQ-SAFNNWFSGHLNFQIEHHLFPT 393
Cdd:pfam00487 153 LGLGGLLLLLWLLpLLVFGFLLALIFNYLEHYG--------GDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPG 224
                         250       260
                  ....*....|....*....|....
gi 162287208  394 MPRHNYHKVAPLVQSLCAKYGIKY 417
Cdd:pfam00487 225 VPWYRLPKLHRRLREALPEHGLPY 248
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
1-97 6.36e-13

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 64.29  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208   1 MAPDPVQTPDPASAQlrqmRYFTWEEVAQRSGREkERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHIN 80
Cdd:COG5274    1 MKKNTTPATDAAAPE----KTYTLAEVATHNTLS-DCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPH 75
                         90
                 ....*....|....*..
gi 162287208  81 KGLVRKYMNSLLIGELA 97
Cdd:COG5274   76 SPKAERLLESYRIGRLA 92
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
146-400 1.77e-11

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: 63.40  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 146 DVAAWLTLWIFGTSLVPFTLCAvLLSTVQAQAGW----LQHDFGHLSVFSTSTWNHLVHHfVIGHLKGAPASWWNHMHFQ 221
Cdd:cd03507   13 DILLLALLALAASLLLSWWLWP-LYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIVGH-ILHSPLLVPYHSWRISHNR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 222 HHAKPNCFRKDpdINMHPLffalgkvlsvelgkEKKKHMPYNHQHKYFFLIGPPALLPLyfqwyifyfvvqrkkwvdlAW 301
Cdd:cd03507   91 HHAHTGNLEGD--EVWVPV--------------TEEEYAELPKRLPYRLYRNPFLMLSL-------------------GW 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 302 MLSFYVRVFFTY-MPllglkgllclFFIVRFlesnWFVWVTQMNHIPMHIDHDRNVDWVSTQLQATCNVHQS--AFNNWF 378
Cdd:cd03507  136 PYYLLLNVLLYYlIP----------YLVVNA----WLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDygGWLNWL 201
                        250       260
                 ....*....|....*....|..
gi 162287208 379 SGHLNFQIEHHLFPTMPrhNYH 400
Cdd:cd03507  202 THIIGTHVAHHLFPRIP--HYN 221
PLN02252 PLN02252
nitrate reductase [NADPH]
5-123 4.73e-10

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 62.00  E-value: 4.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208   5 PVQTPDPASAQLRQMRYFTWEEVAQRSgREKERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHINKGlv 84
Cdd:PLN02252 503 KKSVSTPFMNTNTGSKQYTMSEVRKHN-SEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDKA-- 579
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 162287208  85 RKYMNSLLIGELAPEQPSFEPTKNKALTDEFRELRATVE 123
Cdd:PLN02252 580 KKMLEDYRIGELVTTGAAASSSASSHPLSAISTASALAA 618
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
165-235 1.01e-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: 55.94  E-value: 1.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162287208 165 LCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHFVIGHLkGAPASWWNHMHFQHHAKPNCFRKDPDI 235
Cdd:cd01060    3 LALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDS 72
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
147-235 7.86e-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: 37.73  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287208 147 VAAWLTLWIFGTSLVPFTLCAVLLSTVQAQAGWLQHDFGHLSVFSTSTWNHLVHHfVIGHLKGAPASWWNHMHFQHHAKP 226
Cdd:cd03514    8 ALVWLSTWGYVISYLPLWVCFILNTLSLHLAGTVIHDASHKAASRNRWINELIGH-VSAFFLGFPFPVFRRVHMQHHAHT 86

                 ....*....
gi 162287208 227 NCFRKDPDI 235
Cdd:cd03514   87 NDPEKDPDH 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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