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Conserved domains on  [gi|1622860866|ref|XP_028688696|]
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acyl-CoA 6-desaturase isoform X1 [Macaca mulatta]

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

 Zoom to residue level

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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: ...
 162-412 3.56e-65

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: 208.26  E-value: 3.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 162 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 241
Cdd:cd03506     1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 242 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPPLLIpmyfqyqiimtmivhknwvdlawaisyyirFFVtyipfygilgall 321
Cdd:cd03506    80 SEPAF---GKDQKKRFLHRYQHFYFFPLLALLLL------------------------------AFL------------- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 322 flnFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 398
Cdd:cd03506   114 ---VVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                         250
                  ....*....|....
gi 1622860866 399 IAPLVKSLCAKHGI 412
Cdd:cd03506   191 VAPLVRELCKKHGL 204
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 22-95 6.03e-25

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: 97.31  E-value: 6.03e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622860866  22 SWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAFHPDLKFVGKFLKPLLIGELA 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: ...
 162-412 3.56e-65

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: 208.26  E-value: 3.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 162 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 241
Cdd:cd03506     1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 242 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPPLLIpmyfqyqiimtmivhknwvdlawaisyyirFFVtyipfygilgall 321
Cdd:cd03506    80 SEPAF---GKDQKKRFLHRYQHFYFFPLLALLLL------------------------------AFL------------- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 322 flnFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 398
Cdd:cd03506   114 ---VVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                         250
                  ....*....|....
gi 1622860866 399 IAPLVKSLCAKHGI 412
Cdd:cd03506   191 VAPLVRELCKKHGL 204
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 1-428 4.77e-55

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 190.63  E-value: 4.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866   1 MGKGGN----QGEGAAEREVPMP-TFSWEEIQKHNLRTDRWLVIDRKVYNITKWStQHPGGQRVIGHyAGEDATDAFRAF 75
Cdd:PLN03199    1 MGKGGDaaaaKGRSAALKLAEKPqKISWQEVKKHASPDDAWIIHQNKVYDVSNWH-DHPGGAVIFTH-AGDDMTDIFAAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866  76 HPdlKFVGKFLKPLLIGELAPEEPSQDHGKNSKIIEDFRALKKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFG 155
Cdd:PLN03199   79 HA--PGSQALMKKFYIGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACALVFYSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 156 NGWIpTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHK------ 229
Cdd:PLN03199  157 RFAM-HIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqd 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 230 -DPDVNMLHVFVLGEWQPIEY------GKKK--LKYLPYNHQHEYFfligPPLLIPMY---------------------- 278
Cdd:PLN03199  236 gDPDIDTMPLLAWSLKQAQSFreinadGKDSgfVKFAIKFQAFFYF----PILLLARIswlnesfkcafglgaasenaal 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 279 ------FQYQII--MTMIVHKNWVDLA------WAISYYIRFFVTYIPFYGILGALLFlnfirfleshwfvwvtQMNHIV 344
Cdd:PLN03199  312 eleakgLQYPLLekAGILLHYAWMFTLssgfgrFSFAYSAFYFFTATASCGFFLAIVF----------------GLGHNG 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 345 MEI-DQEAYRDWFSSQLTATCNVE-----QSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKP 418
Cdd:PLN03199  376 MATyDADARPDFWKLQVTTTRNIIgghgfPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEAD 455

                         490
                  ....*....|
gi 1622860866 419 LLRALLDIIR 428
Cdd:PLN03199  456 LVDGTMEVLH 465
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
146-428 1.57e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.96  E-value: 1.57e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 146 IAWFTVFYFGNGWI-PTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHkFVIGHLKGASANWWNHRHFQHHAKP 224
Cdd:COG3239    41 LALLAALWLLLSWSwLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 225 NIFHKDPDvnmlHVFVLGEWQPIeygkkklkylpYNHQHEY-FFLIGPPLLIPMYFQYQIIMT--MIVHKNWVDLAWAIS 301
Cdd:COG3239   120 NDPGKDPD----IGYGVQAWRPL-----------YLFQHLLrFFLLGLGGLYWLLALDFLPLRgrLELKERRLEALLLLL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 302 YYIRFFVTYIpFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDwfssQLTATCNVEQSFFNDWFSGHLNF 381
Cdd:COG3239   185 FLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNLNY 259

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622860866 382 QIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIR 428
Cdd:COG3239   260 HIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLR 306
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 22-95 6.03e-25

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: 97.31  E-value: 6.03e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622860866  22 SWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAFHPDLKFVGKFLKPLLIGELA 95
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGELA 74
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 157-418 3.45e-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: 98.19  E-value: 3.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 157 GWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFV---IGHLKGASANWWNHRHFQHHAKPNIFHKDPDV 233
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 234 NMLHVFVLGEWQPIeygkkkLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIvHKNWVDLAWAIsYYIRFFVTYIPF 313
Cdd:pfam00487  81 APLASRFRGLLRYL------LRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSR-RRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 314 YGILGALLFLNFIRFLESHWFVwvtqmnHIVMEIDQEAYRDWFSSQLTATCNVEQ-SFFNDWFSGHLNFQIEHHLFPTMP 392
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVFGFLL------ALIFNYLEHYGGDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 1622860866 393 RHNLHKIAPLVKSLCAKHGIEYQEKP 418
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 17-95 4.72e-20

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


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 84.70  E-value: 4.72e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622860866  17 PMPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAFHPDLKFVGKFLKPLLIGELA 95
Cdd:COG5274    14 PEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHSPKAERLLESYRIGRLA 92
PLN02252 PLN02252
nitrate reductase [NADPH]
 5-115 7.17e-10

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 61.23  E-value: 7.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866   5 GNQGEGAAEREVPMP---------TFSWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAF 75
Cdd:PLN02252  495 ASAAAPALKKSVSTPfmntntgskQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAI 574

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622860866  76 HPDLkfVGKFLKPLLIGEL----------APEEPSQDHGKNSKIIEDFRA 115
Cdd:PLN02252  575 HSDK--AKKMLEDYRIGELvttgaaasssASSHPLSAISTASALAAASPA 622
 
Name Accession Description Interval E-value
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 162-412 3.56e-65

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: 208.26  E-value: 3.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 162 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGhLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVL 241
Cdd:cd03506     1 LLLAILLGLFWAQGGFLAHDAGHGQVFKNRWLNKLLGLTVGN-LLGASAGWWKNKHNVHHAYTNILGHDPDIDTLPLLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 242 GEWQPieyGKKKLKYLPYNHQHEYFFLIGPPLLIpmyfqyqiimtmivhknwvdlawaisyyirFFVtyipfygilgall 321
Cdd:cd03506    80 SEPAF---GKDQKKRFLHRYQHFYFFPLLALLLL------------------------------AFL------------- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 322 flnFIRFLESHWFVWVTQMNHIVMEIDQEAYR---DWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHK 398
Cdd:cd03506   114 ---VVQLAGGLWLAVVFQLNHFGMPVEDPPGEsknDWLERQVLTTRNITGSPFLDWLHGGLNYQIEHHLFPTMPRHNYPK 190

                         250
                  ....*....|....
gi 1622860866 399 IAPLVKSLCAKHGI 412
Cdd:cd03506   191 VAPLVRELCKKHGL 204
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 1-428 4.77e-55

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 190.63  E-value: 4.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866   1 MGKGGN----QGEGAAEREVPMP-TFSWEEIQKHNLRTDRWLVIDRKVYNITKWStQHPGGQRVIGHyAGEDATDAFRAF 75
Cdd:PLN03199    1 MGKGGDaaaaKGRSAALKLAEKPqKISWQEVKKHASPDDAWIIHQNKVYDVSNWH-DHPGGAVIFTH-AGDDMTDIFAAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866  76 HPdlKFVGKFLKPLLIGELAPEEPSQDHGKNSKIIEDFRALKKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFG 155
Cdd:PLN03199   79 HA--PGSQALMKKFYIGDLIPESTEHKDPQQIAFEKGYRDLRAKLIMMGMFKSNKMFYAYKCLFNMAIWAAACALVFYSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 156 NGWIpTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHK------ 229
Cdd:PLN03199  157 RFAM-HIASALLLGLFFQQCGWLAHDFLHHQVFKKRKHGDLGGIFWGDLMQGFSMQWWKNKHNGHHAVPNLHCSsadaqd 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 230 -DPDVNMLHVFVLGEWQPIEY------GKKK--LKYLPYNHQHEYFfligPPLLIPMY---------------------- 278
Cdd:PLN03199  236 gDPDIDTMPLLAWSLKQAQSFreinadGKDSgfVKFAIKFQAFFYF----PILLLARIswlnesfkcafglgaasenaal 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 279 ------FQYQII--MTMIVHKNWVDLA------WAISYYIRFFVTYIPFYGILGALLFlnfirfleshwfvwvtQMNHIV 344
Cdd:PLN03199  312 eleakgLQYPLLekAGILLHYAWMFTLssgfgrFSFAYSAFYFFTATASCGFFLAIVF----------------GLGHNG 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 345 MEI-DQEAYRDWFSSQLTATCNVE-----QSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKP 418
Cdd:PLN03199  376 MATyDADARPDFWKLQVTTTRNIIgghgfPQAFVDWFCGGLQYQVDHHLFPMLPRHNIAKCHALVESFCKEWGVKYHEAD 455

                         490
                  ....*....|
gi 1622860866 419 LLRALLDIIR 428
Cdd:PLN03199  456 LVDGTMEVLH 465
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 20-416 1.79e-53

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 187.21  E-value: 1.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866  20 TFSWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQrVIGHYAGEDATDAFRAFHPDLKFvgKFLKPLLIGELAPEEP 99
Cdd:PLN03198  105 SHLLSEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFHAASTW--KILQDFYIGDVDNVEP 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 100 SQDhgknskIIEDFRALKKTAEDMNLFKTNHVFFLLLLAHIIALESiAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQ 179
Cdd:PLN03198  182 TPE------LLKDFRDLRALFLREQLFKSSKLYYVFKLLTNIAIFA-ASIAIICCSKSISAVLASACMMALCFQQCGWLS 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 180 HDYGHLSVYrKPKWNHLVHKFVIGH-LKGASANWWNHRHFQHHAKPNIFHK-----DPDVNMLHVFVLGE--WQPIEyGK 251
Cdd:PLN03198  255 HDFLHNQVF-ETRWLNEVVGYLIGNaVLGFSTGWWKEKHNLHHAAPNECDQlyqpiDEDIDTLPLIAWSKdiLATVE-NK 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 252 KKLKYLPYNH---QHEYFFLIGPPLLIPMYFQYQIIMTMIVhknWVDLAWAISYYIRFFVTyIPFYGILG--ALLFLNFI 326
Cdd:PLN03198  333 TFLRILQYQHlffMALLFFARGSWLFWSWRYTSTAKLAPAD---RLLEKGTILFHYFWFIG-TACYLLPGwkPLVWMAVT 408

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 327 RFLESHWFVWVTQMNHIVMEIDQEAyRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSL 406
Cdd:PLN03198  409 ELMCGMLLGFVFVLSHNGMEVYNKS-KEFVNAQIVSTRDIKANIFNDWFTGGLNRQIEHHLFPTMPRHNLNKIAPQVEAF 487

                         410
                  ....*....|
gi 1622860866 407 CAKHGIEYQE 416
Cdd:PLN03198  488 CIKHGLVYED 497
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
146-428 1.57e-42

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 152.96  E-value: 1.57e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 146 IAWFTVFYFGNGWI-PTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHkFVIGHLKGASANWWNHRHFQHHAKP 224
Cdd:COG3239    41 LALLAALWLLLSWSwLALLAALLLGLALAGLFSLGHDAGHGSLFRSRWLNDLLG-RLLGLPLGTPYDAWRRSHNRHHAYT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 225 NIFHKDPDvnmlHVFVLGEWQPIeygkkklkylpYNHQHEY-FFLIGPPLLIPMYFQYQIIMT--MIVHKNWVDLAWAIS 301
Cdd:COG3239   120 NDPGKDPD----IGYGVQAWRPL-----------YLFQHLLrFFLLGLGGLYWLLALDFLPLRgrLELKERRLEALLLLL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 302 YYIRFFVTYIpFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDwfssQLTATCNVEQSFFNDWFSGHLNF 381
Cdd:COG3239   185 FLAALLALLL-ALGWWAVLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD----QLLGSRNIRGGRLLRWLFGNLNY 259

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622860866 382 QIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIR 428
Cdd:COG3239   260 HIEHHLFPSIPWYRLPEAHRILKELCPEYGLPYTEGSLLRSYREVLR 306
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 22-95 6.03e-25

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: 97.31  E-value: 6.03e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622860866  22 SWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAFHPDLKFVGKFLKPLLIGELA 95
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGELA 74
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 157-418 3.45e-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: 98.19  E-value: 3.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 157 GWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFV---IGHLKGASANWWNHRHFQHHAKPNIFHKDPDV 233
Cdd:pfam00487   1 SWLALLLALLLGLFLLGITGSLAHEASHGALFKKRRLNRWLNDLLgrlAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 234 NMLHVFVLGEWQPIeygkkkLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIvHKNWVDLAWAIsYYIRFFVTYIPF 313
Cdd:pfam00487  81 APLASRFRGLLRYL------LRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSR-RRRWRLIAWLL-LLAAWLGLWLGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 314 YGILGALLFLNFIRFLESHWFVwvtqmnHIVMEIDQEAYRDWFSSQLTATCNVEQ-SFFNDWFSGHLNFQIEHHLFPTMP 392
Cdd:pfam00487 153 LGLGGLLLLLWLLPLLVFGFLL------ALIFNYLEHYGGDWGERPVETTRSIRSpNWWLNLLTGNLNYHIEHHLFPGVP 226

                         250       260
                  ....*....|....*....|....*.
gi 1622860866 393 RHNLHKIAPLVKSLCAKHGIEYQEKP 418
Cdd:pfam00487 227 WYRLPKLHRRLREALPEHGLPYRSLG 252
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 17-95 4.72e-20

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


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 84.70  E-value: 4.72e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622860866  17 PMPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAFHPDLKFVGKFLKPLLIGELA 95
Cdd:COG5274    14 PEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHSPKAERLLESYRIGRLA 92
PLN02252 PLN02252
nitrate reductase [NADPH]
 5-115 7.17e-10

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 61.23  E-value: 7.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866   5 GNQGEGAAEREVPMP---------TFSWEEIQKHNLRTDRWLVIDRKVYNITKWSTQHPGGQRVIGHYAGEDATDAFRAF 75
Cdd:PLN02252  495 ASAAAPALKKSVSTPfmntntgskQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAI 574

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622860866  76 HPDLkfVGKFLKPLLIGEL----------APEEPSQDHGKNSKIIEDFRA 115
Cdd:PLN02252  575 HSDK--AKKMLEDYRIGELvttgaaasssASSHPLSAISTASALAAASPA 622
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 162-237 9.02e-10

The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase.


Pssm-ID: 238511 [Multi-domain]  Cd Length: 122  Bit Score: 56.32  E-value: 9.02e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622860866 162 LITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLkGASANWWNHRHFQHHAKPNIFHKDPD--VNMLH 237
Cdd:cd01060     2 LLALLLGLLGGLGLTVLAHELGHRSFFRSRWLNRLLGALLGLAL-GGSYGWWRRSHRRHHRYTNTPGKDPDsaVNYLE 78
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 146-396 1.02e-07

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: 52.61  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 146 IAWFTVFYFGNGWIPTLITAFVLATSQAQAGW----LQHDYGHLSVYRKPKWNHLVhkfviGHLKGASA----NWWNHRH 217
Cdd:cd03507    14 ILLLALLALAASLLLSWWLWPLYWIVQGLFLTglfvLGHDCGHGSFSDNRRLNDIV-----GHILHSPLlvpyHSWRISH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 218 FQHHAKPNifHKDPDVnmlhvfvlgEWQPIEygkkKLKYLPYNHQHEYFFLIGPPLLIPmyfqyqiimtmivhknwvdLA 297
Cdd:cd03507    89 NRHHAHTG--NLEGDE---------VWVPVT----EEEYAELPKRLPYRLYRNPFLMLS-------------------LG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 298 WAISYYIRFFVTYipfygiLGALLFLNFirfleshWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSF--FNDWF 375
Cdd:cd03507   135 WPYYLLLNVLLYY------LIPYLVVNA-------WLVLITYLQHTFPDIPWYRADEWNFAQAGLLGTVDRDYggWLNWL 201

                         250       260
                  ....*....|....*....|.
gi 1622860866 376 SGHLNFQIEHHLFPTMPRHNL 396
Cdd:cd03507   202 THIIGTHVAHHLFPRIPHYNL 222
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 146-239 7.79e-04

This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in Bradyrhizobium japonicum USDA110, and other related proteins. Dihydrorhizobitoxine desaturase is reported to be involved in the final step of rhizobitoxine biosynthesis. This domain family appears to be structurally related to the membrane fatty acid desaturases and the alkane hydroxylases. They all share in common 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 homologs, stearoyl CoA desaturase and alkane hydroxylase.


Pssm-ID: 239587 [Multi-domain]  Cd Length: 175  Bit Score: 40.35  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622860866 146 IAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPN 225
Cdd:cd03510     6 AAAVALALAWPNWLAYLLAVLLIGARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVPIFQSLAAYRRSHLKHHRHLG 85

                          90
                  ....*....|....
gi 1622860866 226 IfHKDPDVNMLHVF 239
Cdd:cd03510    86 T-EDDPDLALYLLL 98
 
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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