NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1026105802|ref|XP_016551928|]
View 

delta(12)-acyl-lipid-desaturase [Capsicum annuum]

Protein Classification

fatty acid desaturase( domain architecture ID 10791388)

fatty acid desaturase removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond; similar to Arabidopsis thaliana delta(12) fatty acid desaturase and related proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 1-382 0e+00

omega-6 fatty acid desaturase


:

Pssm-ID: 178121  Cd Length: 381  Bit Score: 675.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802   1 MGAGGNMSTPTTKAEEKKNSLERVPISKPPFTIGDIKKAIPPHCFERSLIRSSSYLVQDLILVYVFYYIASTYIPVLPTP 80
Cdd:PLN02505    1 MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  81 YQYLAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPK 160
Cdd:PLN02505   81 LSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 161 LKTKLRWYTKlYINNPVGRLFILMFTLTAGLPLYYAINVAGKPYERFASHYDPYSPIYNDRERLQIIISDVGLIATSYVL 240
Cdd:PLN02505  161 KKSALPWYSK-YLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 241 YRVAMAQGLTWLICIYGVPVVIVNSFIVLITLLHHTHLSLPHYDSSEWSWIRGALATVDRDYGVLTKIFHNITDTHVLHH 320
Cdd:PLN02505  240 YRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHH 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026105802 321 LFSNIPHYNAMEATKAIKPVLGEYYQFDGTPFYKAIWRDF-ECIYVEKDEGSqdQGIFWYKQN 382
Cdd:PLN02505  320 LFSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAkECIYVEPDEGG--KGVFWYNNK 380
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 1-382 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 675.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802   1 MGAGGNMSTPTTKAEEKKNSLERVPISKPPFTIGDIKKAIPPHCFERSLIRSSSYLVQDLILVYVFYYIASTYIPVLPTP 80
Cdd:PLN02505    1 MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  81 YQYLAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPK 160
Cdd:PLN02505   81 LSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 161 LKTKLRWYTKlYINNPVGRLFILMFTLTAGLPLYYAINVAGKPYERFASHYDPYSPIYNDRERLQIIISDVGLIATSYVL 240
Cdd:PLN02505  161 KKSALPWYSK-YLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 241 YRVAMAQGLTWLICIYGVPVVIVNSFIVLITLLHHTHLSLPHYDSSEWSWIRGALATVDRDYGVLTKIFHNITDTHVLHH 320
Cdd:PLN02505  240 YRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHH 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026105802 321 LFSNIPHYNAMEATKAIKPVLGEYYQFDGTPFYKAIWRDF-ECIYVEKDEGSqdQGIFWYKQN 382
Cdd:PLN02505  320 LFSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAkECIYVEPDEGG--KGVFWYNNK 380
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 47-330 1.63e-76

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: 235.58  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  47 RSLIRSSSYLVQDLILVYVFYYIASTYIPvlptpyqYLAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVL 126
Cdd:cd03507     1 RSLFRSLSYLAPDILLLALLALAASLLLS-------WWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 127 HSALLTPYFSWKYSHRRHHANTNSLENDENHVPKLKTKLRWYTKlyiNNPVGRLFILMFTLTAGLPLYYAINVagkpyer 206
Cdd:cd03507    74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPK---RLPYRLYRNPFLMLSLGWPYYLLLNV------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 207 fashydpyspiyndrerlqiiisdvgliatsyvlyrvamaqgltwlICIYGVPVVIVNSFIVLITLLHHTHLSLPHYDSS 286
Cdd:cd03507   144 ----------------------------------------------LLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRAD 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1026105802 287 EWSWI-RGALATVDRDYGVLTKIFHNITDTHVLHHLFSNIPHYNA 330
Cdd:cd03507   178 EWNFAqAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
35-345 4.91e-36

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 133.70  E-value: 4.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  35 DIKKAIPPHCFERSLiRSSSYLVQDLILVYVFYYIAStyipvlptpYQYLAWPLyWIFQGSFSTGLWVIAHECGHQSFSD 114
Cdd:COG3239    17 ALRARLRALLGRRDW-RYLLKLALTLALLAALWLLLS---------WSWLALLA-ALLLGLALAGLFSLGHDAGHGSLFR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 115 YQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPKLKTKLRWYtklyinnpvGRLFILMFTLTAGLPLY 194
Cdd:COG3239    86 SRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLY---------LFQHLLRFFLLGLGGLY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 195 YAinvagkpyerFASHYDPYSPIYNDRERLQIIISDVGLIATSYVLYrvaMAQGLTWLICIYGVPVVIVNSFIVLITLLH 274
Cdd:COG3239   157 WL----------LALDFLPLRGRLELKERRLEALLLLLFLAALLALL---LALGWWAVLLFWLLPLLVAGLLLGLRFYLE 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026105802 275 HTHLslphyDSSEWSWIRGALATVDRDYG-VLTKIFHNItDTHVLHHLFSNIPHYNAMEATKAIKPVLGEYY 345
Cdd:COG3239   224 HRGE-----DTGDGEYRDQLLGSRNIRGGrLLRWLFGNL-NYHIEHHLFPSIPWYRLPEAHRILKELCPEYG 289
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 83-345 1.68e-21

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: 92.41  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  83 YLAWPLYWIFQGSFSTGLWVIAHECGHQSFSD----YQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHV 158
Cdd:pfam00487   2 WLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 159 PKLKTKLRWYtklyinnpVGRLFILMFTLTAGLPLYYAINVAGKPYERFASHYDPYSPIYNDRERLQIIISDVGLIAtsy 238
Cdd:pfam00487  82 PLASRFRGLL--------RYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWL--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 239 vlyrvAMAQGLTWLICIYGVPVVIVNSFIVLI-TLLHHTHLSLPHYDSSewswirgALATVDRDYGVLTKIFHNItDTHV 317
Cdd:pfam00487 151 -----GFLGLGGLLLLLWLLPLLVFGFLLALIfNYLEHYGGDWGERPVE-------TTRSIRSPNWWLNLLTGNL-NYHI 217

                         250       260
                  ....*....|....*....|....*...
gi 1026105802 318 LHHLFSNIPHYNAMEATKAIKPVLGEYY 345
Cdd:pfam00487 218 EHHLFPGVPWYRLPKLHRRLREALPEHG 245
 
Name Accession Description Interval E-value
PLN02505 PLN02505
omega-6 fatty acid desaturase
 1-382 0e+00

omega-6 fatty acid desaturase


Pssm-ID: 178121  Cd Length: 381  Bit Score: 675.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802   1 MGAGGNMSTPTTKAEEKKNSLERVPISKPPFTIGDIKKAIPPHCFERSLIRSSSYLVQDLILVYVFYYIASTYIPVLPTP 80
Cdd:PLN02505    1 MGAGGRMSVPTSSKKGSASAVKRVPSSKPPFTLGDIKKAIPPHCFKRSVLRSFSYLVYDLLIAALLYYVATNYIPLLPGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  81 YQYLAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPK 160
Cdd:PLN02505   81 LSYVAWPLYWAAQGCVLTGVWVIAHECGHHAFSDYQWLDDTVGLVLHSALLVPYFSWKYSHRRHHSNTGSLERDEVFVPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 161 LKTKLRWYTKlYINNPVGRLFILMFTLTAGLPLYYAINVAGKPYERFASHYDPYSPIYNDRERLQIIISDVGLIATSYVL 240
Cdd:PLN02505  161 KKSALPWYSK-YLNNPPGRLLHIVVQLTLGWPLYLAFNVSGRPYDRFACHFDPYSPIFNDRERLQIYISDAGILAVSFGL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 241 YRVAMAQGLTWLICIYGVPVVIVNSFIVLITLLHHTHLSLPHYDSSEWSWIRGALATVDRDYGVLTKIFHNITDTHVLHH 320
Cdd:PLN02505  240 YRLAAAKGLAWVLCVYGVPLLIVNAFLVLITYLQHTHPALPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHH 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026105802 321 LFSNIPHYNAMEATKAIKPVLGEYYQFDGTPFYKAIWRDF-ECIYVEKDEGSqdQGIFWYKQN 382
Cdd:PLN02505  320 LFSTMPHYHAMEATKAIKPILGEYYQFDGTPVYKALWREAkECIYVEPDEGG--KGVFWYNNK 380
Delta12-FADS-like cd03507
The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane ...
 47-330 1.63e-76

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: 235.58  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  47 RSLIRSSSYLVQDLILVYVFYYIASTYIPvlptpyqYLAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVL 126
Cdd:cd03507     1 RSLFRSLSYLAPDILLLALLALAASLLLS-------WWLWPLYWIVQGLFLTGLFVLGHDCGHGSFSDNRRLNDIVGHIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 127 HSALLTPYFSWKYSHRRHHANTNSLENDENHVPKLKTKLRWYTKlyiNNPVGRLFILMFTLTAGLPLYYAINVagkpyer 206
Cdd:cd03507    74 HSPLLVPYHSWRISHNRHHAHTGNLEGDEVWVPVTEEEYAELPK---RLPYRLYRNPFLMLSLGWPYYLLLNV------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 207 fashydpyspiyndrerlqiiisdvgliatsyvlyrvamaqgltwlICIYGVPVVIVNSFIVLITLLHHTHLSLPHYDSS 286
Cdd:cd03507   144 ----------------------------------------------LLYYLIPYLVVNAWLVLITYLQHTFPDIPWYRAD 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1026105802 287 EWSWI-RGALATVDRDYGVLTKIFHNITDTHVLHHLFSNIPHYNA 330
Cdd:cd03507   178 EWNFAqAGLLGTVDRDYGGWLNWLTHIIGTHVAHHLFPRIPHYNL 222
PLN02498 PLN02498
omega-3 fatty acid desaturase
 7-346 1.76e-74

omega-3 fatty acid desaturase


Pssm-ID: 215275 [Multi-domain]  Cd Length: 450  Bit Score: 238.19  E-value: 1.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802   7 MSTPTTKAEEKKNSLERV---------PISKPPFTIGDIKKAIPPHCFERSLIRSSSYLVQDLILVYVFYYIASTYipvl 77
Cdd:PLN02498   69 LTVPSGEEEEDEEGVNGVgedeegefdPGAPPPFNLADIRAAIPKHCWVKNPWRSMSYVVRDVAVVFGLAAAAAYF---- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  78 ptpYQYLAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENH 157
Cdd:PLN02498  145 ---NNWVVWPLYWFAQGTMFWALFVLGHDCGHGSFSNNPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESW 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 158 VPkLKTKLrwYTKLyiNNPVGRL-FILMFTLTAgLPLYYAINVAGKPyerfASHYDPYSPIYNDRERLQIIISDVGLIAT 236
Cdd:PLN02498  222 HP-LSEKI--YKSL--DKVTRTLrFTLPFPMLA-YPFYLWSRSPGKK----GSHFHPDSDLFVPKERKDVITSTACWTAM 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 237 SYVLYRVAMAQGLTWLICIYGVPVVIVNSFIVLITLLHH--THLSLPHYDSSEWSWIRGALATVDRDYGVLTKIFHNItD 314
Cdd:PLN02498  292 AALLVCLSFVMGPIQMLKLYGIPYWIFVMWLDFVTYLHHhgHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDI-G 370

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1026105802 315 THVLHHLFSNIPHYNAMEATKAIKPVLGEYYQ 346
Cdd:PLN02498  371 THVIHHLFPQIPHYHLVEATEAAKPVLGKYYR 402
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
35-345 4.91e-36

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 133.70  E-value: 4.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  35 DIKKAIPPHCFERSLiRSSSYLVQDLILVYVFYYIAStyipvlptpYQYLAWPLyWIFQGSFSTGLWVIAHECGHQSFSD 114
Cdd:COG3239    17 ALRARLRALLGRRDW-RYLLKLALTLALLAALWLLLS---------WSWLALLA-ALLLGLALAGLFSLGHDAGHGSLFR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 115 YQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPKLKTKLRWYtklyinnpvGRLFILMFTLTAGLPLY 194
Cdd:COG3239    86 SRWLNDLLGRLLGLPLGTPYDAWRRSHNRHHAYTNDPGKDPDIGYGVQAWRPLY---------LFQHLLRFFLLGLGGLY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 195 YAinvagkpyerFASHYDPYSPIYNDRERLQIIISDVGLIATSYVLYrvaMAQGLTWLICIYGVPVVIVNSFIVLITLLH 274
Cdd:COG3239   157 WL----------LALDFLPLRGRLELKERRLEALLLLLFLAALLALL---LALGWWAVLLFWLLPLLVAGLLLGLRFYLE 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026105802 275 HTHLslphyDSSEWSWIRGALATVDRDYG-VLTKIFHNItDTHVLHHLFSNIPHYNAMEATKAIKPVLGEYY 345
Cdd:COG3239   224 HRGE-----DTGDGEYRDQLLGSRNIRGGrLLRWLFGNL-NYHIEHHLFPSIPWYRLPEAHRILKELCPEYG 289
PLN02598 PLN02598
omega-6 fatty acid desaturase
 30-344 8.45e-25

omega-6 fatty acid desaturase


Pssm-ID: 215323 [Multi-domain]  Cd Length: 421  Bit Score: 104.91  E-value: 8.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  30 PFTIGDIKKAIPPHCFErslirsssylVQDL-----ILVYVFYYIASTY-IPVLPtpyQYLaWPLYWIFQGSFSTGLWVI 103
Cdd:PLN02598   77 NVTLKDVVKTLPKEVFE----------IDDFkawktVAITVTSYALGLAaIAVAP---WYL-LPLAWAWLGTAITGFFVI 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 104 AHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPKLKtklrwytKLYINNPVGRLFIL 183
Cdd:PLN02598  143 GHDCGHNSFSKNQLVEDIVGTIAFTPLIYPFEPWRIKHNTHHAHTNKLVMDTAWQPFRP-------HQFDNADPLRKAMM 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 184 MFTLTaglPLYYAINVAgkpyERFASHYD--PYSPiyNDRERLQIIISDV---GLIATSYVLYRVAMAQGLTWLIciygV 258
Cdd:PLN02598  216 RAGMG---PLWWWASIG----HWLFWHFDlnKFRP--QEVPRVKISLAAVfafMALGLPPLLYTTGPVGFVKWWL----M 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 259 PVVIVNSFIVLITLLHHTHLSLPHYDSSEWSWIRGALA-TVDRDYGVLTKIF-HNITdTHVLHHLFSNIPHYNAMEATKA 336
Cdd:PLN02598  283 PWLGYHFWMSTFTMVHHTAPHIPFKQAREWNAAQAQLNgTVHCDYPAWIEFLcHDIS-VHIPHHISSKIPSYNLRKAHAS 361


                  ....*...
gi 1026105802 337 IKPVLGEY 344
Cdd:PLN02598  362 LQENWGKH 369
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 83-345 1.68e-21

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: 92.41  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  83 YLAWPLYWIFQGSFSTGLWVIAHECGHQSFSD----YQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHV 158
Cdd:pfam00487   2 WLALLLALLLGLFLLGITGSLAHEASHGALFKkrrlNRWLNDLLGRLAGLPLGISYSAWRIAHLVHHRYTNGPDKDPDTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 159 PKLKTKLRWYtklyinnpVGRLFILMFTLTAGLPLYYAINVAGKPYERFASHYDPYSPIYNDRERLQIIISDVGLIAtsy 238
Cdd:pfam00487  82 PLASRFRGLL--------RYLLRWLLGLLVLAWLLALVLPLWLRRLARRKRPIKSRRRRWRLIAWLLLLAAWLGLWL--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 239 vlyrvAMAQGLTWLICIYGVPVVIVNSFIVLI-TLLHHTHLSLPHYDSSewswirgALATVDRDYGVLTKIFHNItDTHV 317
Cdd:pfam00487 151 -----GFLGLGGLLLLLWLLPLLVFGFLLALIfNYLEHYGGDWGERPVE-------TTRSIRSPNWWLNLLTGNL-NYHI 217

                         250       260
                  ....*....|....*....|....*...
gi 1026105802 318 LHHLFSNIPHYNAMEATKAIKPVLGEYY 345
Cdd:pfam00487 218 EHHLFPGVPWYRLPKLHRRLREALPEHG 245
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 83-154 1.94e-18

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: 80.59  E-value: 1.94e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026105802  83 YLAWPLYWIFQGsfsTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLEND 154
Cdd:cd01060     1 LLLALLLGLLGG---LGLTVLAHELGHRSFFRSRWLNRLLGALLGLALGGSYGWWRRSHRRHHRYTNTPGKD 69
Rhizopine-oxygenase-like cd03511
This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine ...
 83-338 3.88e-10

This CD includes the putative hydrocarbon oxygenase, MocD, a bacterial rhizopine (3-O-methyl-scyllo-inosamine, 3-O-MSI) oxygenase, and other related proteins. It has been proposed that MocD, MocE (Rieske-like ferredoxin), and MocF (ferredoxin reductase) under the regulation of MocR, act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine. 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, 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: 239588 [Multi-domain]  Cd Length: 285  Bit Score: 60.08  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  83 YLAWPLYWIfQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENHVPKLK 162
Cdd:cd03511    42 WWALPAFLV-YGVLYAALFARWHECVHGTAFATRWLNDAVGQIAGLMILLPPDFFRWSHARHHRYTQIPGRDPELAVPRP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 163 TKLRwytklyinnpvgRLFILMFtltaGLPLYYAINVAGKPYERFASHYDPYSPIyNDRERLQIIISDVGLIATSYVLYR 242
Cdd:cd03511   121 PTLR------------EYLLALS----GLPYWWGKLRTVFRHAFGAVSEAEKPFI-PAEERPKVVREARAMLAVYAGLIA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 243 VAMAQGLTWLICIYGVPVVIVNSFIVLITLLHHTHLS---LPHYDSsewswiRGALATvdrdyGVLTKIFHNItDTHVLH 319
Cdd:cd03511   184 LSLYLGSPLLVLVWGLPLLLGQPILRLFLLAEHGGCPedaNDLRNT------RTTLTN-----PPLRFLYWNM-PYHAEH 251

                         250
                  ....*....|....*....
gi 1026105802 320 HLFSNIPHYNAMEATKAIK 338
Cdd:cd03511   252 HMYPSVPFHALPKLHELIK 270
Delta6-FADS-like cd03506
The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: ...
 103-345 1.20e-08

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: 54.57  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 103 IAHECGHQSFSDYQWLNDTVGFVLHSALLTPYFSWKYSHRRHHANTNSLENDENhvpklktklrwytklyinnpVGRLFI 182
Cdd:cd03506    17 LAHDAGHGQVFKNRWLNKLLGLTVGNLLGASAGWWKNKHNVHHAYTNILGHDPD--------------------IDTLPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 183 LMFTLTAGLPlyyaiNVAGKPYERFASHYdpYSPIYndrerlqiiisdvGLIATSYVlyrvamaqgltwliciygVPVVI 262
Cdd:cd03506    77 LARSEPAFGK-----DQKKRFLHRYQHFY--FFPLL-------------ALLLLAFL------------------VVQLA 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802 263 VNSFIVLITLLhhTHLSLPHYDSSEWS----WIRGALATVDRDYGVLTKIFH---NItdtHVLHHLFSNIPHYNAMEATK 335
Cdd:cd03506   119 GGLWLAVVFQL--NHFGMPVEDPPGESkndwLERQVLTTRNITGSPFLDWLHgglNY---QIEHHLFPTMPRHNYPKVAP 193

                         250
                  ....*....|
gi 1026105802 336 AIKPVLGEYY 345
Cdd:cd03506   194 LVRELCKKHG 203
DUF3474 pfam11960
Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. ...
 6-64 3.36e-08

Domain of unknown function (DUF3474); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 126 to 140 amino acids in length. This domain is found associated with pfam00487.


Pssm-ID: 403244  Cd Length: 127  Bit Score: 51.65  E-value: 3.36e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026105802   6 NMSTPTTKA------EEKKNSLERV--------PISKPPFTIGDIKKAIPPHCFERSLIRSSSYLVQDLILVY 64
Cdd:pfam11960  51 KVSAPLRVAsvegeeDEETNGFNGVgeeeeefdPGAPPPFKLADIRAAIPKHCWVKDPWRSMSYVVRDVAVVF 123
CrtR_beta-carotene-hydroxylase cd03514
Beta-carotene hydroxylase (CrtR), the carotenoid zeaxanthin biosynthetic enzyme catalyzes the ...
 105-157 9.64e-05

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: 43.12  E-value: 9.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1026105802 105 HECGHQSFSDYQWLNDTVGfvlHSALLTPYFSW---KYSHRRHHANTNSLENDENH 157
Cdd:cd03514    43 HDASHKAASRNRWINELIG---HVSAFFLGFPFpvfRRVHMQHHAHTNDPEKDPDH 95
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 31-159 7.68e-04

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 41.60  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026105802  31 FTIGDIKKAIP-PHCFERSLIRSSSYLVQDLILVYVFYYIAS--TYIPVLPTPYQYLAWP-LYWIFQGS-------FSTG 99
Cdd:PLN03198  171 FYIGDVDNVEPtPELLKDFRDLRALFLREQLFKSSKLYYVFKllTNIAIFAASIAIICCSkSISAVLASacmmalcFQQC 250

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026105802 100 LWvIAHECGHQSFSDYQWLNDTVGFVLHSALLTpyFS---WKYSHRRHHANTNslENDENHVP 159
Cdd:PLN03198  251 GW-LSHDFLHNQVFETRWLNEVVGYLIGNAVLG--FStgwWKEKHNLHHAAPN--ECDQLYQP 308
Rhizobitoxine-FADS-like cd03510
This CD includes the dihydrorhizobitoxine fatty acid desaturase (RtxC) characterized in ...
 84-149 9.88e-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: 39.57  E-value: 9.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1026105802  84 LAWPLYWIFQGSFSTGLWVIAHECGHQSFSDYQWLNDTVGFVLHSA-LLTPYFSWKYSHRRHHANTN 149
Cdd:cd03510    19 LAYLLAVLLIGARQRALAILMHDAAHGLLFRNRRLNDFLGNWLAAVpIFQSLAAYRRSHLKHHRHLG 85
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH