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Conserved domains on  [gi|511004590|gb|EPB85956|]
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hypothetical protein HMPREF1544_07288 [Mucor circinelloides f. circinelloides 1006PhL]

Protein Classification

fatty acid desaturase( domain architecture ID 10445761)

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

EC:  1.14.19.-
Gene Ontology:  GO:0046872|GO:0016020|GO:0006633|GO:0016717
PubMed:  9767077

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: ...
 215-476 1.43e-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: 221.75  E-value: 1.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 215 MAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGlSLGWWKDNHNVHHIVTNHPEHDPDIQHVPFMAI 294
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGA-SAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 295 TTKFFNniystyykrvlpFDAASRFFVRHQHYLYYLILSFGRFnlhrlsfaylltcknvrtrtlelvgitfffvwfgsll 374
Cdd:cd03506   80 SEPAFG------------KDQKKRFLHRYQHFYFFPLLALLLL------------------------------------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 375 stlptwniriAYIMVSYMLTFPLHVQITLSHFGMSTEDRGPDEP--FPAKMLRTTMDVDCPEWLDWFHGGLQYQAVHHLF 452
Cdd:cd03506  111 ----------AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGESKndWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLF 180

                        250       260
                 ....*....|....*....|....
gi 511004590 453 PRLPRHNLRQCVPLVKKFCDEVGL 476
Cdd:cd03506  181 PTMPRHNYPKVAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 23-95 1.42e-18

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: 79.97  E-value: 1.42e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511004590   23 TEEKFQELIKQGDSVFIYEQKVYRVNNFMAKHPGGEAALRSALGRDVTDEIRTM-HPPQVYEKMINLYCIGDYM 95
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIgHSEDAAEKLLKKYRIGELA 74
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 215-476 1.43e-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: 221.75  E-value: 1.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 215 MAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGlSLGWWKDNHNVHHIVTNHPEHDPDIQHVPFMAI 294
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGA-SAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 295 TTKFFNniystyykrvlpFDAASRFFVRHQHYLYYLILSFGRFnlhrlsfaylltcknvrtrtlelvgitfffvwfgsll 374
Cdd:cd03506   80 SEPAFG------------KDQKKRFLHRYQHFYFFPLLALLLL------------------------------------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 375 stlptwniriAYIMVSYMLTFPLHVQITLSHFGMSTEDRGPDEP--FPAKMLRTTMDVDCPEWLDWFHGGLQYQAVHHLF 452
Cdd:cd03506  111 ----------AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGESKndWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLF 180

                        250       260
                 ....*....|....*....|....
gi 511004590 453 PRLPRHNLRQCVPLVKKFCDEVGL 476
Cdd:cd03506  181 PTMPRHNYPKVAPLVRELCKKHGL 204
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 35-500 1.06e-49

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 177.92  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  35 DSVFIYEQKVYRVNNFMaKHPGGEAALRSAlGRDVTDEIRTMHPPQVYEKMINLYcIGDYMPDVIRPASmKQQHTFTKpk 114
Cdd:PLN03199  39 DAWIIHQNKVYDVSNWH-DHPGGAVIFTHA-GDDMTDIFAAFHAPGSQALMKKFY-IGDLIPESTEHKD-PQQIAFEK-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 115 edkpvltatweggftvqayddaiqdlhkhhshdlikdavlqkdlngdqirnAYRKLEAELYAKGLFKCNYWKYAREgCRY 194
Cdd:PLN03199 113 ---------------------------------------------------GYRDLRAKLIMMGMFKSNKMFYAYK-CLF 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 195 TLLIFL-SLWFTLKGTETWHYMAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGLSLGWWKDNHNVH 273
Cdd:PLN03199 141 NMAIWAaACALVFYSDRFAMHIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGH 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 274 HIVTN-------HPEHDPDIQHVPFMAITTKffnniYSTYYKRVLPFDAAS---RFFVRHQHYLYYLILSFGRFNLHRLS 343
Cdd:PLN03199 221 HAVPNlhcssadAQDGDPDIDTMPLLAWSLK-----QAQSFREINADGKDSgfvKFAIKFQAFFYFPILLLARISWLNES 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 344 F-------------AYLLTCKNVRTRTLELVGITFFFVWFGSLLSTLPTWNIriAYIMVsYMLT------FPLHVQITLS 404
Cdd:PLN03199 296 FkcafglgaasenaALELEAKGLQYPLLEKAGILLHYAWMFTLSSGFGRFSF--AYSAF-YFFTatascgFFLAIVFGLG 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 405 HFGMSTEDRGPDEPFPAKMLRTTMDV----DCPE-WLDWFHGGLQYQAVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYY 479
Cdd:PLN03199 373 HNGMATYDADARPDFWKLQVTTTRNIigghGFPQaFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYH 452

                        490       500
                 ....*....|....*....|.
gi 511004590 480 MYNFSTGNGVVLGTLKSVADQ 500
Cdd:PLN03199 453 EADLVDGTMEVLHHLGKVADD 473
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
164-498 1.12e-40

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 149.11  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 164 RNAYRKLEAELYAkgLFKCNYWKYAREGCRyTLLIFLSLWFTLkgTETWHYMAGAAFMAMFWHQLVFTAHDAGHNEITGK 243
Cdd:COG3239   12 EAELRALRARLRA--LLGRRDWRYLLKLAL-TLALLAALWLLL--SWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 244 SEIDHVIGVIIANFIGGlSLGWWKDNHNVHHIVTNHPEHDPDIQHvpfmaittkffnniystyykrvlPFDAASRFFvRH 323
Cdd:COG3239   87 RWLNDLLGRLLGLPLGT-PYDAWRRSHNRHHAYTNDPGKDPDIGY-----------------------GVQAWRPLY-LF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 324 QHYLYYLILSFGRFN-LHRLSFAYLLTCKNVRTRTLELVGITFFFVWFGSLLSTLPTWNIRIAYIMVSYMLTFPLHVQIT 402
Cdd:COG3239  142 QHLLRFFLLGLGGLYwLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLRFY 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 403 LSHFGMSTEDRGPDEPfpakmLRTTMDVDCPEWLDWFHGGLQYQAVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYYMYN 482
Cdd:COG3239  222 LEHRGEDTGDGEYRDQ-----LLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGS 296

                        330
                 ....*....|....*.
gi 511004590 483 FSTGNGVVLGTLKSVA 498
Cdd:COG3239  297 LLRSYREVLRLLRRLG 312
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 211-481 1.22e-27

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: 111.28  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  211 TWHYMAGAAFMAMFWHQLVFT-AHDAGHNEITGKSEIDHVIGVIIANFIG---GLSLGWWKDNHNVHHIVTNHPEHDPDI 286
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSlAHEASHGALFKKRRLNRWLNDLLGRLAGlplGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  287 QHVPFmaittkFFNNIYSTYYKRVLpfdAASRFFVRHQHYLYYLILSFGRFNLHRLSFAYLLTCKNVRTRTLELVGITFF 366
Cdd:pfam00487  81 APLAS------RFRGLLRYLLRWLL---GLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  367 FVWFGSLLSTLptWniriaYIMVSYMLTFPLHVQITLSHFGMSTEDRgpdepfPAKMLRTTMDvdCPEWLDWFHGGLQYQ 446
Cdd:pfam00487 152 FLGLGGLLLLL--W-----LLPLLVFGFLLALIFNYLEHYGGDWGER------PVETTRSIRS--PNWWLNLLTGNLNYH 216

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 511004590  447 AVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYYMY 481
Cdd:pfam00487 217 IEHHLFPGVPWYRLPKLHRRLREALPEHGLPYRSL 251
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 23-95 1.42e-18

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: 79.97  E-value: 1.42e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511004590   23 TEEKFQELIKQGDSVFIYEQKVYRVNNFMAKHPGGEAALRSALGRDVTDEIRTM-HPPQVYEKMINLYCIGDYM 95
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIgHSEDAAEKLLKKYRIGELA 74
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 215-476 1.43e-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: 221.75  E-value: 1.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 215 MAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGlSLGWWKDNHNVHHIVTNHPEHDPDIQHVPFMAI 294
Cdd:cd03506    1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGNLLGA-SAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 295 TTKFFNniystyykrvlpFDAASRFFVRHQHYLYYLILSFGRFnlhrlsfaylltcknvrtrtlelvgitfffvwfgsll 374
Cdd:cd03506   80 SEPAFG------------KDQKKRFLHRYQHFYFFPLLALLLL------------------------------------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 375 stlptwniriAYIMVSYMLTFPLHVQITLSHFGMSTEDRGPDEP--FPAKMLRTTMDVDCPEWLDWFHGGLQYQAVHHLF 452
Cdd:cd03506  111 ----------AFLVVQLAGGLWLAVVFQLNHFGMPVEDPPGESKndWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLF 180

                        250       260
                 ....*....|....*....|....
gi 511004590 453 PRLPRHNLRQCVPLVKKFCDEVGL 476
Cdd:cd03506  181 PTMPRHNYPKVAPLVRELCKKHGL 204
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 35-500 1.06e-49

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 177.92  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  35 DSVFIYEQKVYRVNNFMaKHPGGEAALRSAlGRDVTDEIRTMHPPQVYEKMINLYcIGDYMPDVIRPASmKQQHTFTKpk 114
Cdd:PLN03199  39 DAWIIHQNKVYDVSNWH-DHPGGAVIFTHA-GDDMTDIFAAFHAPGSQALMKKFY-IGDLIPESTEHKD-PQQIAFEK-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 115 edkpvltatweggftvqayddaiqdlhkhhshdlikdavlqkdlngdqirnAYRKLEAELYAKGLFKCNYWKYAREgCRY 194
Cdd:PLN03199 113 ---------------------------------------------------GYRDLRAKLIMMGMFKSNKMFYAYK-CLF 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 195 TLLIFL-SLWFTLKGTETWHYMAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGLSLGWWKDNHNVH 273
Cdd:PLN03199 141 NMAIWAaACALVFYSDRFAMHIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGH 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 274 HIVTN-------HPEHDPDIQHVPFMAITTKffnniYSTYYKRVLPFDAAS---RFFVRHQHYLYYLILSFGRFNLHRLS 343
Cdd:PLN03199 221 HAVPNlhcssadAQDGDPDIDTMPLLAWSLK-----QAQSFREINADGKDSgfvKFAIKFQAFFYFPILLLARISWLNES 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 344 F-------------AYLLTCKNVRTRTLELVGITFFFVWFGSLLSTLPTWNIriAYIMVsYMLT------FPLHVQITLS 404
Cdd:PLN03199 296 FkcafglgaasenaALELEAKGLQYPLLEKAGILLHYAWMFTLSSGFGRFSF--AYSAF-YFFTatascgFFLAIVFGLG 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 405 HFGMSTEDRGPDEPFPAKMLRTTMDV----DCPE-WLDWFHGGLQYQAVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYY 479
Cdd:PLN03199 373 HNGMATYDADARPDFWKLQVTTTRNIigghGFPQaFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYH 452

                        490       500
                 ....*....|....*....|.
gi 511004590 480 MYNFSTGNGVVLGTLKSVADQ 500
Cdd:PLN03199 453 EADLVDGTMEVLHHLGKVADD 473
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 32-499 5.10e-47

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 171.41  E-value: 5.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  32 KQGDSVFIYEQKVYRVNNFMAKHPGGeAALRSALGRDVTDEIRTMHPPQVYEKMINLYcIGDYmpDVIRPasmkqqhtft 111
Cdd:PLN03198 116 KPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTWKILQDFY-IGDV--DNVEP---------- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 112 kpkedkpvltatweggftvqayddaiqdlhkhhSHDLIKDavlqkdlngdqirnaYRKLEAELYAKGLFKCNYWKYAREG 191
Cdd:PLN03198 182 ---------------------------------TPELLKD---------------FRDLRALFLREQLFKSSKLYYVFKL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 192 CRYTLLIFLSLWFTLKGTETWHYMAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGLSLGWWKDNHN 271
Cdd:PLN03198 214 LTNIAIFAASIAIICCSKSISAVLASACMMALCFQQCGWLSHDFLHNQVFETRWLNEVVGYLIGNAVLGFSTGWWKEKHN 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 272 VHHIVTNHPEH-----DPDIQHVPFMAITTKFFNNIYSTYYKRVLpfdaasrffvRHQHYLYYLILSFGRFNLHRLSFAY 346
Cdd:PLN03198 294 LHHAAPNECDQlyqpiDEDIDTLPLIAWSKDILATVENKTFLRIL----------QYQHLFFMALLFFARGSWLFWSWRY 363

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 347 LLTCK-NVRTRTLELVGITFFFVWF-GSLLSTLPTWNIRIAYIMVSYMLTFPLHVQITLSHFGMSTEDRGPDepFPAKML 424
Cdd:PLN03198 364 TSTAKlAPADRLLEKGTILFHYFWFiGTACYLLPGWKPLVWMAVTELMCGMLLGFVFVLSHNGMEVYNKSKE--FVNAQI 441

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511004590 425 RTTMDVDCPEWLDWFHGGLQYQAVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYYMYNFSTGNGVVLGTLKSVAD 499
Cdd:PLN03198 442 VSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAFCIKHGLVYEDVSIAAGTCKVLKALKEVAE 516
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
164-498 1.12e-40

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 149.11  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 164 RNAYRKLEAELYAkgLFKCNYWKYAREGCRyTLLIFLSLWFTLkgTETWHYMAGAAFMAMFWHQLVFTAHDAGHNEITGK 243
Cdd:COG3239   12 EAELRALRARLRA--LLGRRDWRYLLKLAL-TLALLAALWLLL--SWSWLALLAALLLGLALAGLFSLGHDAGHGSLFRS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 244 SEIDHVIGVIIANFIGGlSLGWWKDNHNVHHIVTNHPEHDPDIQHvpfmaittkffnniystyykrvlPFDAASRFFvRH 323
Cdd:COG3239   87 RWLNDLLGRLLGLPLGT-PYDAWRRSHNRHHAYTNDPGKDPDIGY-----------------------GVQAWRPLY-LF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 324 QHYLYYLILSFGRFN-LHRLSFAYLLTCKNVRTRTLELVGITFFFVWFGSLLSTLPTWNIRIAYIMVSYMLTFPLHVQIT 402
Cdd:COG3239  142 QHLLRFFLLGLGGLYwLLALDFLPLRGRLELKERRLEALLLLLFLAALLALLLALGWWAVLLFWLLPLLVAGLLLGLRFY 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 403 LSHFGMSTEDRGPDEPfpakmLRTTMDVDCPEWLDWFHGGLQYQAVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYYMYN 482
Cdd:COG3239  222 LEHRGEDTGDGEYRDQ-----LLGSRNIRGGRLLRWLFGNLNYHIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGS 296

                        330
                 ....*....|....*.
gi 511004590 483 FSTGNGVVLGTLKSVA 498
Cdd:COG3239  297 LLRSYREVLRLLRRLG 312
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 211-481 1.22e-27

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: 111.28  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  211 TWHYMAGAAFMAMFWHQLVFT-AHDAGHNEITGKSEIDHVIGVIIANFIG---GLSLGWWKDNHNVHHIVTNHPEHDPDI 286
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSlAHEASHGALFKKRRLNRWLNDLLGRLAGlplGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  287 QHVPFmaittkFFNNIYSTYYKRVLpfdAASRFFVRHQHYLYYLILSFGRFNLHRLSFAYLLTCKNVRTRTLELVGITFF 366
Cdd:pfam00487  81 APLAS------RFRGLLRYLLRWLL---GLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWLG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590  367 FVWFGSLLSTLptWniriaYIMVSYMLTFPLHVQITLSHFGMSTEDRgpdepfPAKMLRTTMDvdCPEWLDWFHGGLQYQ 446
Cdd:pfam00487 152 FLGLGGLLLLL--W-----LLPLLVFGFLLALIFNYLEHYGGDWGER------PVETTRSIRS--PNWWLNLLTGNLNYH 216

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 511004590  447 AVHHLFPRLPRHNLRQCVPLVKKFCDEVGLHYYMY 481
Cdd:pfam00487 217 IEHHLFPGVPWYRLPKLHRRLREALPEHGLPYRSL 251
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 23-95 1.42e-18

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: 79.97  E-value: 1.42e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511004590   23 TEEKFQELIKQGDSVFIYEQKVYRVNNFMAKHPGGEAALRSALGRDVTDEIRTM-HPPQVYEKMINLYCIGDYM 95
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIgHSEDAAEKLLKKYRIGELA 74
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 216-288 4.60e-11

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: 60.18  E-value: 4.60e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511004590 216 AGAAFMAMFWH-QLVFTAHDAGHNEITGKSEIDHVIGVIIANFIGGlSLGWWKDNHNVHHIVTNHPEHDPDIQH 288
Cdd:cd01060    2 LLALLLGLLGGlGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGG-SYGWWRRSHRRHHRYTNTPGKDPDSAV 74
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 193-460 3.29e-04

The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.


Pssm-ID: 239584 [Multi-domain]  Cd Length: 222  Bit Score: 42.21  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 193 RYTLLIFLSLWFTLKGTETWHYMAGAAFMAMFWHQLVFTAHDAGHNEITGKSEIDHVIGviianFIGGLSLGW----WKD 268
Cdd:cd03507   12 PDILLLALLALAASLLLSWWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVG-----HILHSPLLVpyhsWRI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 269 NHNVHHIVTNHPEHDpdIQHVPfmaiTTKFFNNIYSTYYKRVLPFDAASRFFVRHQHYLYYlilsfgrfnlhrlsfayll 348
Cdd:cd03507   87 SHNRHHAHTGNLEGD--EVWVP----VTEEEYAELPKRLPYRLYRNPFLMLSLGWPYYLLL------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 349 tcknvrtrtlelvgitFFFVWFGsllstlptwnirIAYIMVSYMLTFPLHVQitlsHFGMSTE-DRGPDEPFPAKMLRTT 427
Cdd:cd03507  142 ----------------NVLLYYL------------IPYLVVNAWLVLITYLQ----HTFPDIPwYRADEWNFAQAGLLGT 189

                        250       260       270
                 ....*....|....*....|....*....|...
gi 511004590 428 MDVDCPEWLDWFHGGLQYQAVHHLFPRLPRHNL 460
Cdd:cd03507  190 VDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 196-286 2.95e-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: 39.27  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511004590 196 LLIFLSLWFTLKGTETWHYMAGAAFMAMFwhqLVFT-AHDAGHNEITGKSEIDHVIGVIIAnFIGGLSLGWWKDNHNVHH 274
Cdd:cd03514    8 ALVWLSTWGYVISYLPLWVCFILNTLSLH---LAGTvIHDASHKAASRNRWINELIGHVSA-FFLGFPFPVFRRVHMQHH 83

                         90
                 ....*....|..
gi 511004590 275 IVTNHPEHDPDI 286
Cdd:cd03514   84 AHTNDPEKDPDH 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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